HEADER HYDROLASE 09-DEC-14 4X6Z
TITLE YEAST 20S PROTEASOME IN COMPLEX WITH PR-VI MODULATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 3 CHAIN: 1, M;
COMPND 4 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 5 COMPONENT C5;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 9 CHAIN: 2, N;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 15 CHAIN: A, O;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA,MULTICATALYTIC ENDOPEPTIDASE
COMPND 17 COMPLEX C7,PROTEASOME COMPONENT C7-ALPHA,PROTEASOME COMPONENT Y8,
COMPND 18 PROTEINASE YSCE SUBUNIT 7,SCL1 SUPPRESSOR PROTEIN;
COMPND 19 EC: 3.4.25.1;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 22 CHAIN: B, P;
COMPND 23 SYNONYM: MACROPAIN SUBUNIT Y7,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 24 SUBUNIT Y7,PROTEASOME COMPONENT Y7,PROTEINASE YSCE SUBUNIT 7;
COMPND 25 EC: 3.4.25.1;
COMPND 26 MOL_ID: 5;
COMPND 27 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 28 CHAIN: C, Q;
COMPND 29 SYNONYM: MACROPAIN SUBUNIT Y13,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 30 SUBUNIT Y13,PROTEASOME COMPONENT Y13,PROTEINASE YSCE SUBUNIT 13;
COMPND 31 EC: 3.4.25.1;
COMPND 32 MOL_ID: 6;
COMPND 33 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 34 CHAIN: D, R;
COMPND 35 SYNONYM: MACROPAIN SUBUNIT PRE6,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 36 SUBUNIT PRE6,PROTEASOME COMPONENT PRE6,PROTEINASE YSCE SUBUNIT PRE6;
COMPND 37 EC: 3.4.25.1;
COMPND 38 MOL_ID: 7;
COMPND 39 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 40 CHAIN: E, S;
COMPND 41 SYNONYM: MACROPAIN SUBUNIT PUP2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 42 SUBUNIT PUP2,PROTEASOME COMPONENT PUP2,PROTEINASE YSCE SUBUNIT PUP2;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 46 CHAIN: F, T;
COMPND 47 SYNONYM: MACROPAIN SUBUNIT PRE5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 48 SUBUNIT PRE5,PROTEASOME COMPONENT PRE5,PROTEINASE YSCE SUBUNIT PRE5;
COMPND 49 EC: 3.4.25.1;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 52 CHAIN: G, U;
COMPND 53 SYNONYM: MACROPAIN SUBUNIT C1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 54 SUBUNIT C1,PROTEASOME COMPONENT C1,PROTEINASE YSCE SUBUNIT 1;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 58 CHAIN: H, V;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 60 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 64 CHAIN: I, W;
COMPND 65 SYNONYM: MACROPAIN SUBUNIT PUP1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 66 SUBUNIT PUP1,PROTEASOME COMPONENT PUP1,PROTEINASE YSCE SUBUNIT PUP1;
COMPND 67 EC: 3.4.25.1;
COMPND 68 MOL_ID: 12;
COMPND 69 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 70 CHAIN: J, X;
COMPND 71 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 72 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;
COMPND 73 EC: 3.4.25.1;
COMPND 74 MOL_ID: 13;
COMPND 75 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 76 CHAIN: K, Y;
COMPND 77 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 78 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;
COMPND 79 EC: 3.4.25.1;
COMPND 80 MOL_ID: 14;
COMPND 81 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 82 CHAIN: L, Z;
COMPND 83 SYNONYM: MACROPAIN SUBUNIT PRE2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 84 SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,PROTEINASE YSCE SUBUNIT PRE2;
COMPND 85 EC: 3.4.25.1;
COMPND 86 MOL_ID: 15;
COMPND 87 MOLECULE: SYNTHETIC PEPTIDE (POLYMER);
COMPND 88 CHAIN: a, e;
COMPND 89 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 9 S288C);
SOURCE 10 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 11 ORGANISM_TAXID: 559292;
SOURCE 12 STRAIN: ATCC 204508 / S288C;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 15 S288C);
SOURCE 16 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 17 ORGANISM_TAXID: 559292;
SOURCE 18 STRAIN: ATCC 204508 / S288C;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 21 S288C);
SOURCE 22 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 23 ORGANISM_TAXID: 559292;
SOURCE 24 STRAIN: ATCC 204508 / S288C;
SOURCE 25 MOL_ID: 5;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 27 S288C);
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 559292;
SOURCE 30 STRAIN: ATCC 204508 / S288C;
SOURCE 31 MOL_ID: 6;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 33 S288C);
SOURCE 34 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 35 ORGANISM_TAXID: 559292;
SOURCE 36 STRAIN: ATCC 204508 / S288C;
SOURCE 37 MOL_ID: 7;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 39 S288C);
SOURCE 40 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 41 ORGANISM_TAXID: 559292;
SOURCE 42 STRAIN: ATCC 204508 / S288C;
SOURCE 43 MOL_ID: 8;
SOURCE 44 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 45 S288C);
SOURCE 46 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 47 ORGANISM_TAXID: 559292;
SOURCE 48 STRAIN: ATCC 204508 / S288C;
SOURCE 49 MOL_ID: 9;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 51 S288C);
SOURCE 52 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 53 ORGANISM_TAXID: 559292;
SOURCE 54 STRAIN: ATCC 204508 / S288C;
SOURCE 55 MOL_ID: 10;
SOURCE 56 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 57 S288C);
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 MOL_ID: 11;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 63 S288C);
SOURCE 64 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 65 ORGANISM_TAXID: 559292;
SOURCE 66 STRAIN: ATCC 204508 / S288C;
SOURCE 67 MOL_ID: 12;
SOURCE 68 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 69 S288C);
SOURCE 70 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 71 ORGANISM_TAXID: 559292;
SOURCE 72 STRAIN: ATCC 204508 / S288C;
SOURCE 73 MOL_ID: 13;
SOURCE 74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 75 S288C);
SOURCE 76 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 77 ORGANISM_TAXID: 559292;
SOURCE 78 STRAIN: ATCC 204508 / S288C;
SOURCE 79 MOL_ID: 14;
SOURCE 80 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 81 S288C);
SOURCE 82 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 83 ORGANISM_TAXID: 559292;
SOURCE 84 STRAIN: ATCC 204508 / S288C;
SOURCE 85 MOL_ID: 15;
SOURCE 86 SYNTHETIC: YES;
SOURCE 87 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 88 ORGANISM_TAXID: 32630
KEYWDS 20S PROTEASOME, LOW-MOLECULAR MASS ACTIVATORS, ALLOSTERIC REGULATION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ROSTANKOWSKI,J.WITKOWSKA,D.BOREK,Z.OTWINOWSKI,E.JANKOWSKA
REVDAT 2 10-JAN-24 4X6Z 1 REMARK
REVDAT 1 23-DEC-15 4X6Z 0
JRNL AUTH J.WITKOWSKA,R.ROSTANKOWSKI,G.DUBIN,P.GRUDNIK,P.GOLIK,
JRNL AUTH 2 M.GACZYNSKA,P.OSMULSKI,D.BOREK,Z.OTWINOWSKI,E.JANKOWSKA
JRNL TITL CRYSTAL STRUCTURES REVEALED THE COMMON PLACE OF BINDING OF
JRNL TITL 2 LOW-MOLECULAR MASS ACTIVATORS WITH THE 20S PROTEASOME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 68.3
REMARK 3 NUMBER OF REFLECTIONS : 186914
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9928
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3070
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 15.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 176
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 356
REMARK 3 SOLVENT ATOMS : 359
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.19000
REMARK 3 B22 (A**2) : 0.42000
REMARK 3 B33 (A**2) : -1.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.55000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.359
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.230
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.718
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50699 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48553 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68524 ; 1.684 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES):111781 ; 0.980 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6343 ; 7.167 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2268 ;37.984 ;24.374
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8784 ;18.371 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 292 ;18.397 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7729 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57362 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11348 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25426 ; 1.523 ; 2.419
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25425 ; 1.523 ; 2.419
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31736 ; 2.565 ; 3.622
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31737 ; 2.565 ; 3.622
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25273 ; 2.013 ; 2.701
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25273 ; 2.012 ; 2.701
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36784 ; 3.353 ; 3.940
REMARK 3 LONG RANGE B REFINED ATOMS (A**2):209795 ; 6.019 ;23.042
REMARK 3 LONG RANGE B OTHER ATOMS (A**2):209751 ; 6.017 ;23.041
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 14
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 1 -8 213 M -8 213 13182 0.08 0.05
REMARK 3 2 2 -7 225 N -7 225 14647 0.05 0.05
REMARK 3 3 A 11 250 O 11 250 14696 0.09 0.05
REMARK 3 4 B 2 248 P 2 248 14622 0.07 0.05
REMARK 3 5 C 2 245 Q 2 245 14432 0.10 0.05
REMARK 3 6 D 3 243 R 3 243 14301 0.11 0.05
REMARK 3 7 E 9 250 S 9 250 14104 0.10 0.05
REMARK 3 8 F 3 234 T 3 234 13684 0.10 0.05
REMARK 3 9 G 4 247 U 4 247 14426 0.09 0.05
REMARK 3 10 H 1 196 V 1 196 11801 0.06 0.05
REMARK 3 11 I 1 219 W 1 219 12688 0.08 0.05
REMARK 3 12 J -7 196 X -7 196 12512 0.06 0.05
REMARK 3 13 K 0 195 Y 0 195 12361 0.06 0.05
REMARK 3 14 L 1 212 Z 1 212 12588 0.06 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 112
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 1 -8 1 13
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8535 -11.9470 28.4371
REMARK 3 T TENSOR
REMARK 3 T11: 0.2199 T22: 0.1064
REMARK 3 T33: 0.1564 T12: 0.0279
REMARK 3 T13: -0.0289 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 10.5658 L22: 2.5364
REMARK 3 L33: 3.0027 L12: 0.0808
REMARK 3 L13: -4.5423 L23: 0.8350
REMARK 3 S TENSOR
REMARK 3 S11: 0.4057 S12: 0.1647 S13: 0.7975
REMARK 3 S21: -0.1501 S22: 0.0618 S23: -0.2868
REMARK 3 S31: -0.2605 S32: 0.0831 S33: -0.4675
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 1 14 1 128
REMARK 3 ORIGIN FOR THE GROUP (A): 67.9841 -20.1625 26.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.0982 T22: 0.0540
REMARK 3 T33: 0.2571 T12: 0.0413
REMARK 3 T13: 0.0749 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.7514 L22: 0.7530
REMARK 3 L33: 1.1483 L12: -0.0851
REMARK 3 L13: 0.0600 L23: 0.3483
REMARK 3 S TENSOR
REMARK 3 S11: 0.0814 S12: 0.0428 S13: -0.1019
REMARK 3 S21: -0.1752 S22: -0.0178 S23: -0.2907
REMARK 3 S31: 0.0354 S32: 0.0764 S33: -0.0637
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 1 129 1 165
REMARK 3 ORIGIN FOR THE GROUP (A): 79.7674 1.2009 12.9803
REMARK 3 T TENSOR
REMARK 3 T11: 0.2972 T22: 0.3265
REMARK 3 T33: 0.4764 T12: 0.1130
REMARK 3 T13: 0.0974 T23: -0.1401
REMARK 3 L TENSOR
REMARK 3 L11: 2.5537 L22: 2.1450
REMARK 3 L33: 1.3049 L12: 1.0121
REMARK 3 L13: -0.5000 L23: -1.3043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1068 S12: 0.2628 S13: -0.1367
REMARK 3 S21: -0.5093 S22: 0.0336 S23: -0.5718
REMARK 3 S31: 0.5341 S32: 0.3233 S33: 0.0732
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 1 166 1 213
REMARK 3 ORIGIN FOR THE GROUP (A): 81.0534 -7.3660 30.9893
REMARK 3 T TENSOR
REMARK 3 T11: 0.0339 T22: 0.1784
REMARK 3 T33: 0.3294 T12: 0.0109
REMARK 3 T13: 0.0119 T23: -0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 1.9722 L22: 5.0324
REMARK 3 L33: 3.4388 L12: -0.8696
REMARK 3 L13: -1.5181 L23: 1.6505
REMARK 3 S TENSOR
REMARK 3 S11: 0.1509 S12: -0.1714 S13: -0.0575
REMARK 3 S21: 0.0244 S22: -0.0257 S23: -0.5552
REMARK 3 S31: -0.0978 S32: 0.5005 S33: -0.1252
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 2 -7 2 62
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5670 -18.5060 58.0789
REMARK 3 T TENSOR
REMARK 3 T11: 0.1320 T22: 0.0463
REMARK 3 T33: 0.0841 T12: 0.0190
REMARK 3 T13: -0.0553 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.9371 L22: 1.6253
REMARK 3 L33: 1.0240 L12: -0.2484
REMARK 3 L13: 0.3975 L23: -0.3161
REMARK 3 S TENSOR
REMARK 3 S11: 0.0825 S12: -0.1954 S13: -0.1238
REMARK 3 S21: 0.2716 S22: -0.0569 S23: -0.1376
REMARK 3 S31: 0.0387 S32: 0.0017 S33: -0.0256
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 2 63 2 148
REMARK 3 ORIGIN FOR THE GROUP (A): 62.8654 -22.6738 49.6614
REMARK 3 T TENSOR
REMARK 3 T11: 0.0652 T22: 0.0275
REMARK 3 T33: 0.1568 T12: 0.0326
REMARK 3 T13: -0.0396 T23: -0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 0.4577 L22: 1.9725
REMARK 3 L33: 0.8507 L12: 0.4019
REMARK 3 L13: 0.1769 L23: -0.2390
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.0522 S13: -0.0878
REMARK 3 S21: 0.0911 S22: 0.0199 S23: -0.3233
REMARK 3 S31: 0.1375 S32: 0.1108 S33: -0.0343
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 2 149 2 205
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2716 -11.2566 63.4996
REMARK 3 T TENSOR
REMARK 3 T11: 0.0894 T22: 0.0507
REMARK 3 T33: 0.1878 T12: 0.0089
REMARK 3 T13: -0.1228 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.7116 L22: 1.6145
REMARK 3 L33: 1.1932 L12: -0.0635
REMARK 3 L13: -0.1002 L23: -0.1088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: -0.2101 S13: -0.0822
REMARK 3 S21: 0.2309 S22: 0.0328 S23: -0.3686
REMARK 3 S31: 0.0036 S32: 0.1738 S33: 0.0253
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 2 206 2 225
REMARK 3 ORIGIN FOR THE GROUP (A): 57.6863 12.0317 71.1466
REMARK 3 T TENSOR
REMARK 3 T11: 0.2158 T22: 0.0984
REMARK 3 T33: 0.1711 T12: -0.0713
REMARK 3 T13: -0.0288 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.8820 L22: 5.6652
REMARK 3 L33: 1.7846 L12: -2.6358
REMARK 3 L13: 1.6362 L23: -0.8028
REMARK 3 S TENSOR
REMARK 3 S11: -0.1643 S12: -0.1640 S13: 0.3680
REMARK 3 S21: 0.4704 S22: 0.1517 S23: -0.3458
REMARK 3 S31: -0.2096 S32: -0.0439 S33: 0.0127
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 130
REMARK 3 ORIGIN FOR THE GROUP (A): 43.7021 54.7100 64.6634
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.0324
REMARK 3 T33: 0.0892 T12: -0.0027
REMARK 3 T13: 0.0239 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 0.7660 L22: 1.0070
REMARK 3 L33: 1.7333 L12: 0.1119
REMARK 3 L13: -0.0488 L23: 0.0234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: -0.0095 S13: 0.1136
REMARK 3 S21: 0.2778 S22: -0.0197 S23: 0.0481
REMARK 3 S31: -0.1323 S32: -0.1109 S33: 0.0052
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 131 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0953 56.8104 66.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.0460
REMARK 3 T33: 0.1506 T12: -0.0414
REMARK 3 T13: 0.0296 T23: -0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 0.9463 L22: 2.2968
REMARK 3 L33: 1.6102 L12: -0.4092
REMARK 3 L13: 0.5729 L23: -0.5633
REMARK 3 S TENSOR
REMARK 3 S11: 0.1456 S12: -0.1204 S13: -0.0552
REMARK 3 S21: 0.0746 S22: -0.0348 S23: -0.0318
REMARK 3 S31: -0.0125 S32: -0.0453 S33: -0.1108
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 183 A 223
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8312 57.9529 84.7178
REMARK 3 T TENSOR
REMARK 3 T11: 0.2899 T22: 0.1360
REMARK 3 T33: 0.0834 T12: -0.0351
REMARK 3 T13: -0.0908 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 4.9725 L22: 3.1602
REMARK 3 L33: 2.1544 L12: -0.8580
REMARK 3 L13: -0.4427 L23: 1.7176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0660 S12: -0.2734 S13: 0.1674
REMARK 3 S21: 0.2992 S22: 0.1379 S23: -0.3412
REMARK 3 S31: -0.0237 S32: 0.3827 S33: -0.0719
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 224 A 252
REMARK 3 ORIGIN FOR THE GROUP (A): 47.2761 49.7531 87.1892
REMARK 3 T TENSOR
REMARK 3 T11: 0.2093 T22: 0.1549
REMARK 3 T33: 0.1429 T12: -0.0050
REMARK 3 T13: 0.0104 T23: 0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 4.9257 L22: 4.6533
REMARK 3 L33: 9.1531 L12: -0.8392
REMARK 3 L13: -2.7763 L23: 2.7543
REMARK 3 S TENSOR
REMARK 3 S11: -0.1502 S12: -0.5980 S13: 0.0997
REMARK 3 S21: 0.6658 S22: 0.0403 S23: 0.0976
REMARK 3 S31: -0.0043 S32: 0.2790 S33: 0.1099
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 47
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8184 64.3435 41.3436
REMARK 3 T TENSOR
REMARK 3 T11: 0.1697 T22: 0.0353
REMARK 3 T33: 0.1478 T12: -0.0534
REMARK 3 T13: 0.0391 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 3.4086 L22: 0.6658
REMARK 3 L33: 1.6103 L12: -0.9397
REMARK 3 L13: 0.8497 L23: 0.1618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: -0.0008 S13: 0.0154
REMARK 3 S21: -0.0142 S22: -0.0513 S23: -0.0800
REMARK 3 S31: -0.0950 S32: -0.1214 S33: 0.0823
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 48 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5748 59.8144 63.1295
REMARK 3 T TENSOR
REMARK 3 T11: 0.2210 T22: 0.4179
REMARK 3 T33: 0.4523 T12: -0.0034
REMARK 3 T13: -0.0544 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 2.0566 L22: 0.1504
REMARK 3 L33: 17.7257 L12: 0.4136
REMARK 3 L13: -6.0260 L23: -1.1987
REMARK 3 S TENSOR
REMARK 3 S11: 0.1527 S12: 0.0023 S13: 0.0324
REMARK 3 S21: 0.0446 S22: -0.1695 S23: -0.0363
REMARK 3 S31: -0.5543 S32: -0.0725 S33: 0.0168
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 64 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): 63.9661 54.7690 41.2882
REMARK 3 T TENSOR
REMARK 3 T11: 0.0954 T22: 0.0364
REMARK 3 T33: 0.1778 T12: -0.0387
REMARK 3 T13: 0.0362 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 1.2257 L22: 1.1039
REMARK 3 L33: 0.7706 L12: -0.2597
REMARK 3 L13: 0.0934 L23: 0.0935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.1437 S13: 0.0957
REMARK 3 S21: -0.0114 S22: -0.0057 S23: -0.3477
REMARK 3 S31: -0.1538 S32: 0.0465 S33: 0.0034
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 180 B 249
REMARK 3 ORIGIN FOR THE GROUP (A): 78.5091 54.0674 52.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.0774 T22: 0.1420
REMARK 3 T33: 0.2487 T12: -0.0636
REMARK 3 T13: -0.0294 T23: -0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 1.4688 L22: 3.2718
REMARK 3 L33: 1.3184 L12: 0.4777
REMARK 3 L13: -0.3059 L23: -1.1389
REMARK 3 S TENSOR
REMARK 3 S11: -0.0658 S12: -0.2122 S13: 0.1132
REMARK 3 S21: 0.0522 S22: 0.1690 S23: -0.3484
REMARK 3 S31: -0.1711 S32: 0.1711 S33: -0.1032
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 48
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7280 67.4722 22.2397
REMARK 3 T TENSOR
REMARK 3 T11: 0.2690 T22: 0.0294
REMARK 3 T33: 0.2001 T12: 0.0159
REMARK 3 T13: -0.0344 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 3.2421 L22: 1.0119
REMARK 3 L33: 1.6846 L12: 0.3257
REMARK 3 L13: -0.4338 L23: -0.3438
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.1165 S13: 0.1089
REMARK 3 S21: -0.2385 S22: -0.0659 S23: 0.1276
REMARK 3 S31: -0.4668 S32: 0.0331 S33: 0.0898
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 49 C 64
REMARK 3 ORIGIN FOR THE GROUP (A): 70.7646 64.5634 28.7087
REMARK 3 T TENSOR
REMARK 3 T11: 0.2577 T22: 0.4165
REMARK 3 T33: 0.4372 T12: -0.0737
REMARK 3 T13: 0.1044 T23: 0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 2.9769 L22: 2.8164
REMARK 3 L33: 12.0633 L12: 1.3901
REMARK 3 L13: 5.9525 L23: 2.1885
REMARK 3 S TENSOR
REMARK 3 S11: -0.0731 S12: 0.0160 S13: 0.0907
REMARK 3 S21: -0.1184 S22: -0.0737 S23: 0.1519
REMARK 3 S31: -0.1216 S32: 0.0556 S33: 0.1468
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 65 C 175
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5831 55.4969 15.6899
REMARK 3 T TENSOR
REMARK 3 T11: 0.1735 T22: 0.0377
REMARK 3 T33: 0.1484 T12: -0.0292
REMARK 3 T13: 0.0660 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 1.6614 L22: 0.6933
REMARK 3 L33: 0.8411 L12: 0.2681
REMARK 3 L13: -0.1865 L23: 0.2688
REMARK 3 S TENSOR
REMARK 3 S11: -0.1005 S12: 0.0589 S13: 0.1428
REMARK 3 S21: -0.2095 S22: 0.0958 S23: -0.0654
REMARK 3 S31: -0.1685 S32: 0.0620 S33: 0.0047
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 176 C 245
REMARK 3 ORIGIN FOR THE GROUP (A): 71.8656 64.2975 11.1440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2292 T22: 0.3087
REMARK 3 T33: 0.2540 T12: -0.0834
REMARK 3 T13: 0.1322 T23: 0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 4.1318 L22: 4.5855
REMARK 3 L33: 3.5969 L12: 0.1929
REMARK 3 L13: 1.6097 L23: 1.0660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: 0.3105 S13: -0.0384
REMARK 3 S21: 0.0368 S22: 0.0370 S23: -0.6461
REMARK 3 S31: -0.0479 S32: 0.5538 S33: -0.0870
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 48
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3641 65.9857 12.0537
REMARK 3 T TENSOR
REMARK 3 T11: 0.1649 T22: 0.1058
REMARK 3 T33: 0.2747 T12: 0.0641
REMARK 3 T13: -0.0241 T23: 0.0960
REMARK 3 L TENSOR
REMARK 3 L11: 0.5718 L22: 1.4922
REMARK 3 L33: 4.2799 L12: 0.6016
REMARK 3 L13: -0.9527 L23: 0.2272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0450 S12: 0.0221 S13: 0.1584
REMARK 3 S21: -0.1218 S22: -0.0429 S23: 0.0623
REMARK 3 S31: -0.3000 S32: 0.1242 S33: -0.0020
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 49 D 65
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4145 63.6808 2.1902
REMARK 3 T TENSOR
REMARK 3 T11: 0.8881 T22: 0.4596
REMARK 3 T33: 0.4946 T12: -0.0959
REMARK 3 T13: 0.0576 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 7.1759 L22: 2.3813
REMARK 3 L33: 1.3395 L12: 4.1321
REMARK 3 L13: 3.0992 L23: 1.7847
REMARK 3 S TENSOR
REMARK 3 S11: -0.2808 S12: -0.0631 S13: 0.5918
REMARK 3 S21: -0.1597 S22: -0.0013 S23: 0.3468
REMARK 3 S31: -0.1299 S32: -0.0249 S33: 0.2821
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 66 D 210
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7844 58.7423 1.3730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2375 T22: 0.0411
REMARK 3 T33: 0.1405 T12: -0.0331
REMARK 3 T13: -0.0234 T23: 0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 1.0979 L22: 2.2477
REMARK 3 L33: 2.0723 L12: 0.2563
REMARK 3 L13: -0.0101 L23: -0.8470
REMARK 3 S TENSOR
REMARK 3 S11: -0.0895 S12: 0.1587 S13: 0.1049
REMARK 3 S21: -0.4684 S22: 0.1260 S23: 0.0260
REMARK 3 S31: -0.2069 S32: -0.0106 S33: -0.0365
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 211 D 243
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3691 64.8428 -14.5097
REMARK 3 T TENSOR
REMARK 3 T11: 0.4990 T22: 0.5339
REMARK 3 T33: 0.4631 T12: -0.0508
REMARK 3 T13: 0.1286 T23: -0.0898
REMARK 3 L TENSOR
REMARK 3 L11: 1.9540 L22: 0.7011
REMARK 3 L33: 2.4830 L12: -0.9386
REMARK 3 L13: 1.0883 L23: -0.9978
REMARK 3 S TENSOR
REMARK 3 S11: 0.1070 S12: 0.4357 S13: 0.3989
REMARK 3 S21: 0.1855 S22: -0.1426 S23: -0.2868
REMARK 3 S31: -0.4375 S32: 0.6400 S33: 0.0356
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 9 E 30
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5702 67.8703 33.5361
REMARK 3 T TENSOR
REMARK 3 T11: 0.1883 T22: 0.1710
REMARK 3 T33: 0.4451 T12: 0.0196
REMARK 3 T13: -0.0711 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 0.8433 L22: 4.7391
REMARK 3 L33: 13.2155 L12: 0.3025
REMARK 3 L13: -3.3323 L23: -1.4626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0915 S12: -0.0179 S13: 0.0268
REMARK 3 S21: 0.3095 S22: -0.1097 S23: -0.2998
REMARK 3 S31: -0.4222 S32: 0.0529 S33: 0.0182
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 31 E 83
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7298 59.0315 8.9440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2598 T22: 0.0985
REMARK 3 T33: 0.3339 T12: 0.0700
REMARK 3 T13: -0.1319 T23: 0.0896
REMARK 3 L TENSOR
REMARK 3 L11: 2.3335 L22: 1.6827
REMARK 3 L33: 2.8159 L12: -0.3158
REMARK 3 L13: -1.3465 L23: -0.7781
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: 0.0027 S13: 0.2105
REMARK 3 S21: -0.1938 S22: -0.0128 S23: 0.1762
REMARK 3 S31: -0.1871 S32: -0.1570 S33: -0.0323
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 84 E 140
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9388 48.0568 24.0985
REMARK 3 T TENSOR
REMARK 3 T11: 0.1528 T22: 0.1568
REMARK 3 T33: 0.1815 T12: 0.0706
REMARK 3 T13: -0.0060 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 3.2310 L22: 6.4933
REMARK 3 L33: 1.4189 L12: 3.7044
REMARK 3 L13: 0.4916 L23: 1.8260
REMARK 3 S TENSOR
REMARK 3 S11: 0.1018 S12: -0.2746 S13: -0.0721
REMARK 3 S21: 0.4011 S22: 0.0727 S23: -0.3754
REMARK 3 S31: 0.0373 S32: 0.2741 S33: -0.1745
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 141 E 250
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2723 60.8011 8.7443
REMARK 3 T TENSOR
REMARK 3 T11: 0.2192 T22: 0.1072
REMARK 3 T33: 0.4310 T12: 0.1136
REMARK 3 T13: -0.1221 T23: 0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 1.7395 L22: 1.5288
REMARK 3 L33: 2.7114 L12: 0.6250
REMARK 3 L13: 0.1096 L23: -1.5306
REMARK 3 S TENSOR
REMARK 3 S11: -0.0439 S12: 0.0106 S13: 0.1102
REMARK 3 S21: -0.2121 S22: 0.1006 S23: 0.3821
REMARK 3 S31: -0.1179 S32: -0.3106 S33: -0.0568
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 81
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3549 59.4740 43.2808
REMARK 3 T TENSOR
REMARK 3 T11: 0.1526 T22: 0.0837
REMARK 3 T33: 0.5113 T12: 0.1019
REMARK 3 T13: 0.0100 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.6256 L22: 0.2410
REMARK 3 L33: 1.5090 L12: -0.1386
REMARK 3 L13: 0.4627 L23: 0.1078
REMARK 3 S TENSOR
REMARK 3 S11: -0.0681 S12: -0.0844 S13: 0.0999
REMARK 3 S21: -0.0654 S22: -0.0362 S23: 0.2488
REMARK 3 S31: -0.2580 S32: -0.0944 S33: 0.1044
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 82 F 126
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8529 44.5232 47.0001
REMARK 3 T TENSOR
REMARK 3 T11: 0.0984 T22: 0.0870
REMARK 3 T33: 0.2033 T12: 0.0597
REMARK 3 T13: 0.0421 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.2475 L22: 4.4868
REMARK 3 L33: 2.4239 L12: 0.3776
REMARK 3 L13: 0.6723 L23: -0.4184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0511 S12: 0.0062 S13: -0.0426
REMARK 3 S21: 0.1106 S22: 0.0614 S23: -0.1189
REMARK 3 S31: -0.1687 S32: -0.0164 S33: -0.0103
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 127 F 172
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7444 55.0934 51.2809
REMARK 3 T TENSOR
REMARK 3 T11: 0.2161 T22: 0.1121
REMARK 3 T33: 0.4502 T12: 0.1054
REMARK 3 T13: 0.1398 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 3.0788 L22: 0.3687
REMARK 3 L33: 1.3760 L12: 0.6092
REMARK 3 L13: 1.0801 L23: 0.6135
REMARK 3 S TENSOR
REMARK 3 S11: -0.0379 S12: -0.1776 S13: 0.1709
REMARK 3 S21: 0.0591 S22: -0.0711 S23: 0.2112
REMARK 3 S31: -0.1431 S32: -0.2204 S33: 0.1090
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 173 F 234
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4675 54.1368 45.3338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0559 T22: 0.3200
REMARK 3 T33: 0.5945 T12: 0.1149
REMARK 3 T13: 0.0298 T23: 0.0474
REMARK 3 L TENSOR
REMARK 3 L11: 1.0415 L22: 2.4211
REMARK 3 L33: 4.6837 L12: -0.6436
REMARK 3 L13: -0.3234 L23: -0.2830
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: -0.1656 S13: 0.1885
REMARK 3 S21: -0.0263 S22: 0.1368 S23: 0.5958
REMARK 3 S31: -0.1487 S32: -0.6087 S33: -0.1695
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 4 G 162
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8686 52.7888 64.7569
REMARK 3 T TENSOR
REMARK 3 T11: 0.1913 T22: 0.0995
REMARK 3 T33: 0.1809 T12: 0.0532
REMARK 3 T13: 0.1081 T23: -0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 1.3685 L22: 0.7232
REMARK 3 L33: 0.7516 L12: 0.0904
REMARK 3 L13: 0.2711 L23: -0.0199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: -0.1157 S13: 0.0851
REMARK 3 S21: 0.1342 S22: 0.0226 S23: 0.1959
REMARK 3 S31: -0.1170 S32: -0.0926 S33: -0.0085
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 163 G 175
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4432 63.9542 76.1428
REMARK 3 T TENSOR
REMARK 3 T11: 0.1560 T22: 0.1873
REMARK 3 T33: 0.2807 T12: 0.0182
REMARK 3 T13: 0.0550 T23: -0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 3.8217 L22: 13.7500
REMARK 3 L33: 34.3671 L12: 0.1427
REMARK 3 L13: -1.2095 L23: -5.0538
REMARK 3 S TENSOR
REMARK 3 S11: -0.1024 S12: -0.2355 S13: 0.2032
REMARK 3 S21: 0.4249 S22: 0.0763 S23: 0.3081
REMARK 3 S31: -1.0054 S32: -0.5615 S33: 0.0261
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 176 G 207
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6639 57.7115 83.5201
REMARK 3 T TENSOR
REMARK 3 T11: 0.3333 T22: 0.2668
REMARK 3 T33: 0.2051 T12: 0.0360
REMARK 3 T13: 0.1498 T23: -0.1087
REMARK 3 L TENSOR
REMARK 3 L11: 8.5947 L22: 3.2024
REMARK 3 L33: 3.2403 L12: -0.4203
REMARK 3 L13: 1.8815 L23: 0.2126
REMARK 3 S TENSOR
REMARK 3 S11: -0.1310 S12: -0.2137 S13: 0.6119
REMARK 3 S21: 0.4341 S22: -0.0126 S23: 0.1374
REMARK 3 S31: -0.5792 S32: -0.2556 S33: 0.1436
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 208 G 247
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1830 50.3408 78.1485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2355 T22: 0.2020
REMARK 3 T33: 0.2590 T12: -0.0153
REMARK 3 T13: 0.2124 T23: -0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 5.2712 L22: 4.6484
REMARK 3 L33: 1.6443 L12: -3.0636
REMARK 3 L13: 1.6159 L23: -0.5108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: -0.0759 S13: 0.0406
REMARK 3 S21: 0.1682 S22: -0.1138 S23: 0.5090
REMARK 3 S31: -0.1727 S32: -0.3643 S33: 0.0350
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 17
REMARK 3 ORIGIN FOR THE GROUP (A): 38.9496 12.7871 77.1595
REMARK 3 T TENSOR
REMARK 3 T11: 0.1370 T22: 0.0919
REMARK 3 T33: 0.0942 T12: -0.0159
REMARK 3 T13: -0.0323 T23: 0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 6.9153 L22: 8.8122
REMARK 3 L33: 6.4364 L12: -2.2204
REMARK 3 L13: -1.9138 L23: 6.1567
REMARK 3 S TENSOR
REMARK 3 S11: -0.0811 S12: -0.3353 S13: 0.2083
REMARK 3 S21: 0.6404 S22: -0.0927 S23: 0.2571
REMARK 3 S31: 0.1995 S32: -0.1321 S33: 0.1738
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 18 H 84
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8920 21.9460 65.4289
REMARK 3 T TENSOR
REMARK 3 T11: 0.1439 T22: 0.0318
REMARK 3 T33: 0.0664 T12: -0.0266
REMARK 3 T13: 0.0027 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.8524 L22: 2.0591
REMARK 3 L33: 0.9951 L12: -0.8632
REMARK 3 L13: -0.4611 L23: 0.5077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: 0.0208 S13: -0.0225
REMARK 3 S21: 0.1872 S22: -0.0160 S23: 0.0401
REMARK 3 S31: -0.1121 S32: 0.0359 S33: -0.0121
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 85 H 147
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4308 13.1185 70.3079
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: 0.0430
REMARK 3 T33: 0.0345 T12: -0.0284
REMARK 3 T13: 0.0299 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.1069 L22: 2.6472
REMARK 3 L33: 1.0699 L12: -0.3949
REMARK 3 L13: 0.2567 L23: -0.7794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.1520 S13: 0.0709
REMARK 3 S21: 0.2450 S22: 0.0545 S23: 0.1397
REMARK 3 S31: -0.1141 S32: 0.0049 S33: -0.0723
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 148 H 196
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2784 6.7911 77.4068
REMARK 3 T TENSOR
REMARK 3 T11: 0.1936 T22: 0.1913
REMARK 3 T33: 0.0978 T12: 0.0105
REMARK 3 T13: -0.0582 T23: 0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 1.9795 L22: 3.6417
REMARK 3 L33: 2.0068 L12: -0.7988
REMARK 3 L13: -0.7242 L23: 2.3007
REMARK 3 S TENSOR
REMARK 3 S11: -0.0826 S12: -0.3190 S13: -0.1254
REMARK 3 S21: 0.4292 S22: 0.0579 S23: -0.2493
REMARK 3 S31: 0.1711 S32: 0.2563 S33: 0.0248
REMARK 3
REMARK 3 TLS GROUP : 41
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 45
REMARK 3 ORIGIN FOR THE GROUP (A): 68.4967 17.8141 49.0206
REMARK 3 T TENSOR
REMARK 3 T11: 0.1461 T22: 0.1845
REMARK 3 T33: 0.2853 T12: -0.0336
REMARK 3 T13: -0.0435 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 0.9767 L22: 4.5693
REMARK 3 L33: 0.9018 L12: -0.7717
REMARK 3 L13: -0.8284 L23: 1.4426
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: 0.0076 S13: -0.0264
REMARK 3 S21: -0.4434 S22: -0.1348 S23: -0.1732
REMARK 3 S31: -0.1813 S32: 0.0187 S33: 0.0699
REMARK 3
REMARK 3 TLS GROUP : 42
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 46 I 75
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5228 32.4066 50.1218
REMARK 3 T TENSOR
REMARK 3 T11: 0.1340 T22: 0.1674
REMARK 3 T33: 0.1806 T12: 0.0323
REMARK 3 T13: -0.0069 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 0.4842 L22: 5.8903
REMARK 3 L33: 0.9493 L12: 1.6764
REMARK 3 L13: 0.6008 L23: 2.1100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: 0.0362 S13: -0.1426
REMARK 3 S21: -0.0887 S22: 0.1724 S23: -0.4635
REMARK 3 S31: 0.0633 S32: 0.2194 S33: -0.1717
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 76 I 198
REMARK 3 ORIGIN FOR THE GROUP (A): 65.9537 16.0671 54.6379
REMARK 3 T TENSOR
REMARK 3 T11: 0.0803 T22: 0.0432
REMARK 3 T33: 0.1388 T12: -0.0214
REMARK 3 T13: -0.0293 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.4165 L22: 1.8580
REMARK 3 L33: 1.0301 L12: -0.5585
REMARK 3 L13: 0.1122 L23: 0.3157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: 0.0042 S13: -0.0474
REMARK 3 S21: 0.0683 S22: 0.1116 S23: -0.3254
REMARK 3 S31: 0.0054 S32: 0.1853 S33: -0.0706
REMARK 3
REMARK 3 TLS GROUP : 44
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 199 I 221
REMARK 3 ORIGIN FOR THE GROUP (A): 82.1879 16.1745 13.9796
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.2618
REMARK 3 T33: 0.3300 T12: -0.0645
REMARK 3 T13: 0.1649 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 1.9941 L22: 2.0010
REMARK 3 L33: 4.6657 L12: 0.3855
REMARK 3 L13: 0.6669 L23: -2.0293
REMARK 3 S TENSOR
REMARK 3 S11: 0.1155 S12: 0.2069 S13: 0.2908
REMARK 3 S21: -0.0656 S22: -0.0202 S23: -0.3370
REMARK 3 S31: -0.2436 S32: 0.3991 S33: -0.0953
REMARK 3
REMARK 3 TLS GROUP : 45
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J -7 J 67
REMARK 3 ORIGIN FOR THE GROUP (A): 63.1014 23.3600 18.0297
REMARK 3 T TENSOR
REMARK 3 T11: 0.1167 T22: 0.0672
REMARK 3 T33: 0.1684 T12: -0.0090
REMARK 3 T13: 0.1321 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.5449 L22: 2.1887
REMARK 3 L33: 1.2888 L12: 0.4064
REMARK 3 L13: 0.3507 L23: 0.5122
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0170 S13: -0.0736
REMARK 3 S21: -0.1896 S22: 0.0191 S23: -0.1738
REMARK 3 S31: -0.0091 S32: 0.1236 S33: -0.0226
REMARK 3
REMARK 3 TLS GROUP : 46
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 68 J 114
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4243 29.6007 29.0094
REMARK 3 T TENSOR
REMARK 3 T11: 0.1204 T22: 0.0365
REMARK 3 T33: 0.2077 T12: 0.0072
REMARK 3 T13: 0.0584 T23: -0.0657
REMARK 3 L TENSOR
REMARK 3 L11: 1.2294 L22: 2.8711
REMARK 3 L33: 2.4247 L12: 1.2904
REMARK 3 L13: -1.5069 L23: -0.6490
REMARK 3 S TENSOR
REMARK 3 S11: 0.1343 S12: -0.0449 S13: 0.0018
REMARK 3 S21: 0.1815 S22: 0.0613 S23: -0.3507
REMARK 3 S31: -0.1306 S32: 0.1121 S33: -0.1957
REMARK 3
REMARK 3 TLS GROUP : 47
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 115 J 126
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5477 20.1443 32.6402
REMARK 3 T TENSOR
REMARK 3 T11: 0.5193 T22: 0.9334
REMARK 3 T33: 0.5776 T12: 0.1048
REMARK 3 T13: 0.0117 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 0.5082 L22: 0.0182
REMARK 3 L33: 0.9264 L12: -0.0909
REMARK 3 L13: -0.6816 L23: 0.1213
REMARK 3 S TENSOR
REMARK 3 S11: -0.0596 S12: -0.2601 S13: -0.0767
REMARK 3 S21: 0.0405 S22: 0.0377 S23: 0.0133
REMARK 3 S31: 0.0633 S32: 0.3469 S33: 0.0219
REMARK 3
REMARK 3 TLS GROUP : 48
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 127 J 196
REMARK 3 ORIGIN FOR THE GROUP (A): 74.9152 14.3558 16.9536
REMARK 3 T TENSOR
REMARK 3 T11: 0.1282 T22: 0.1132
REMARK 3 T33: 0.3338 T12: -0.0235
REMARK 3 T13: 0.1617 T23: -0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 2.0410 L22: 1.4268
REMARK 3 L33: 1.1915 L12: 0.1923
REMARK 3 L13: -0.0567 L23: 0.2084
REMARK 3 S TENSOR
REMARK 3 S11: 0.0953 S12: 0.2002 S13: 0.0858
REMARK 3 S21: -0.0385 S22: 0.0062 S23: -0.4758
REMARK 3 S31: -0.0166 S32: 0.2991 S33: -0.1015
REMARK 3
REMARK 3 TLS GROUP : 49
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 0 K 28
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5683 16.6099 -2.9736
REMARK 3 T TENSOR
REMARK 3 T11: 0.2272 T22: 0.1007
REMARK 3 T33: 0.1204 T12: 0.0374
REMARK 3 T13: -0.0081 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 12.2884 L22: 3.6757
REMARK 3 L33: 1.4989 L12: 5.0486
REMARK 3 L13: -1.7059 L23: -0.6678
REMARK 3 S TENSOR
REMARK 3 S11: 0.1816 S12: -0.2372 S13: -0.1102
REMARK 3 S21: 0.1190 S22: -0.1161 S23: -0.0187
REMARK 3 S31: -0.1068 S32: 0.0394 S33: -0.0655
REMARK 3
REMARK 3 TLS GROUP : 50
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 29 K 88
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0980 31.2528 4.2851
REMARK 3 T TENSOR
REMARK 3 T11: 0.1743 T22: 0.0816
REMARK 3 T33: 0.0925 T12: -0.0153
REMARK 3 T13: 0.0498 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.9809 L22: 3.0566
REMARK 3 L33: 0.6180 L12: 0.1398
REMARK 3 L13: 0.4514 L23: 0.7438
REMARK 3 S TENSOR
REMARK 3 S11: -0.0381 S12: 0.0425 S13: 0.1469
REMARK 3 S21: -0.3821 S22: 0.0466 S23: 0.0356
REMARK 3 S31: -0.0539 S32: 0.0091 S33: -0.0086
REMARK 3
REMARK 3 TLS GROUP : 51
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 89 K 160
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9494 20.0055 0.6667
REMARK 3 T TENSOR
REMARK 3 T11: 0.1661 T22: 0.0192
REMARK 3 T33: 0.0619 T12: -0.0120
REMARK 3 T13: 0.0876 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.6341 L22: 1.6081
REMARK 3 L33: 3.0095 L12: -0.1668
REMARK 3 L13: -0.2546 L23: 0.2265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.0318 S13: 0.1243
REMARK 3 S21: -0.2553 S22: 0.0663 S23: -0.2182
REMARK 3 S31: 0.0702 S32: 0.0160 S33: -0.0467
REMARK 3
REMARK 3 TLS GROUP : 52
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 161 K 195
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3961 15.1435 -9.7460
REMARK 3 T TENSOR
REMARK 3 T11: 0.2513 T22: 0.2466
REMARK 3 T33: 0.1021 T12: -0.0077
REMARK 3 T13: 0.0092 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.6700 L22: 5.3853
REMARK 3 L33: 0.1721 L12: 0.7466
REMARK 3 L13: -0.1148 L23: -0.2077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0255 S12: 0.3028 S13: -0.0749
REMARK 3 S21: -0.7050 S22: 0.0320 S23: 0.1318
REMARK 3 S31: 0.1297 S32: -0.0639 S33: -0.0065
REMARK 3
REMARK 3 TLS GROUP : 53
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 96
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4369 23.3922 8.9740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1376 T22: 0.0527
REMARK 3 T33: 0.2424 T12: 0.0398
REMARK 3 T13: -0.1002 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 1.1307 L22: 0.7235
REMARK 3 L33: 1.2302 L12: 0.4179
REMARK 3 L13: -0.4034 L23: 0.5092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.0332 S13: 0.0132
REMARK 3 S21: -0.1769 S22: 0.0065 S23: 0.1778
REMARK 3 S31: -0.1016 S32: -0.0185 S33: -0.0251
REMARK 3
REMARK 3 TLS GROUP : 54
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 97 L 109
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6509 27.4893 -0.8953
REMARK 3 T TENSOR
REMARK 3 T11: 0.2140 T22: 0.1346
REMARK 3 T33: 0.2102 T12: -0.0167
REMARK 3 T13: -0.0382 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 3.6411 L22: 8.2370
REMARK 3 L33: 11.9287 L12: -2.0119
REMARK 3 L13: 2.9532 L23: -7.6278
REMARK 3 S TENSOR
REMARK 3 S11: -0.1264 S12: 0.3017 S13: 0.2026
REMARK 3 S21: -0.1526 S22: -0.0066 S23: -0.0163
REMARK 3 S31: -0.4602 S32: 0.0549 S33: 0.1330
REMARK 3
REMARK 3 TLS GROUP : 55
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 110 L 197
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7185 13.4523 -1.5067
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.0731
REMARK 3 T33: 0.1742 T12: 0.0009
REMARK 3 T13: -0.1011 T23: 0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 1.3214 L22: 2.2266
REMARK 3 L33: 1.3814 L12: 0.6040
REMARK 3 L13: 0.0438 L23: 0.3345
REMARK 3 S TENSOR
REMARK 3 S11: -0.0347 S12: 0.1780 S13: 0.0024
REMARK 3 S21: -0.4587 S22: 0.1345 S23: 0.1914
REMARK 3 S31: 0.0106 S32: -0.0343 S33: -0.0998
REMARK 3
REMARK 3 TLS GROUP : 56
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 198 L 212
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5747 -3.5356 -5.7815
REMARK 3 T TENSOR
REMARK 3 T11: 0.1474 T22: 0.1812
REMARK 3 T33: 0.1700 T12: -0.0328
REMARK 3 T13: -0.0846 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 5.9598 L22: 10.4368
REMARK 3 L33: 13.2787 L12: 2.0943
REMARK 3 L13: -1.5583 L23: -4.9465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0735 S12: 0.5733 S13: -0.2934
REMARK 3 S21: -0.3477 S22: -0.0714 S23: 0.4355
REMARK 3 S31: 0.0309 S32: -0.2793 S33: 0.1449
REMARK 3
REMARK 3 TLS GROUP : 57
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M -8 M 17
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5023 12.1084 31.9065
REMARK 3 T TENSOR
REMARK 3 T11: 0.1876 T22: 0.0703
REMARK 3 T33: 0.1471 T12: 0.0065
REMARK 3 T13: 0.0306 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 8.8612 L22: 2.1493
REMARK 3 L33: 2.8037 L12: -0.5686
REMARK 3 L13: 2.8361 L23: -0.6326
REMARK 3 S TENSOR
REMARK 3 S11: 0.3438 S12: -0.0887 S13: -0.6003
REMARK 3 S21: -0.0607 S22: 0.0119 S23: 0.2894
REMARK 3 S31: 0.1886 S32: -0.1540 S33: -0.3557
REMARK 3
REMARK 3 TLS GROUP : 58
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 18 M 126
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6204 21.3134 30.8521
REMARK 3 T TENSOR
REMARK 3 T11: 0.0410 T22: 0.0184
REMARK 3 T33: 0.2590 T12: 0.0099
REMARK 3 T13: -0.0076 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 0.3705 L22: 1.2649
REMARK 3 L33: 1.1564 L12: 0.1213
REMARK 3 L13: 0.2597 L23: -0.3559
REMARK 3 S TENSOR
REMARK 3 S11: 0.0254 S12: -0.0216 S13: 0.0635
REMARK 3 S21: -0.1089 S22: 0.0491 S23: 0.3107
REMARK 3 S31: -0.0199 S32: -0.0719 S33: -0.0744
REMARK 3
REMARK 3 TLS GROUP : 59
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 127 M 164
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1648 1.9382 14.8564
REMARK 3 T TENSOR
REMARK 3 T11: 0.1386 T22: 0.1404
REMARK 3 T33: 0.3906 T12: 0.0391
REMARK 3 T13: -0.0834 T23: 0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 2.1003 L22: 1.3798
REMARK 3 L33: 3.7343 L12: 0.4210
REMARK 3 L13: 1.6940 L23: 1.2015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: -0.0752 S13: 0.1714
REMARK 3 S21: -0.2440 S22: -0.1100 S23: 0.4291
REMARK 3 S31: -0.4016 S32: -0.4862 S33: 0.1056
REMARK 3
REMARK 3 TLS GROUP : 60
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 165 M 213
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8216 7.4700 33.1393
REMARK 3 T TENSOR
REMARK 3 T11: 0.0431 T22: 0.1271
REMARK 3 T33: 0.3580 T12: -0.0192
REMARK 3 T13: -0.0106 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 1.8271 L22: 4.7204
REMARK 3 L33: 2.0036 L12: -1.2049
REMARK 3 L13: -0.3970 L23: 0.0211
REMARK 3 S TENSOR
REMARK 3 S11: 0.2217 S12: -0.0014 S13: 0.0055
REMARK 3 S21: -0.2011 S22: -0.1447 S23: 0.6498
REMARK 3 S31: 0.0929 S32: -0.2262 S33: -0.0771
REMARK 3
REMARK 3 TLS GROUP : 61
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N -7 N 61
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8439 13.4080 61.5705
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.0429
REMARK 3 T33: 0.0936 T12: 0.0176
REMARK 3 T13: 0.0938 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.0456 L22: 2.1182
REMARK 3 L33: 1.1093 L12: 0.4181
REMARK 3 L13: 0.3119 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0739 S12: -0.2100 S13: 0.0839
REMARK 3 S21: 0.2698 S22: -0.0408 S23: 0.1784
REMARK 3 S31: -0.1058 S32: -0.0756 S33: -0.0331
REMARK 3
REMARK 3 TLS GROUP : 62
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 62 N 141
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7856 21.0219 54.0332
REMARK 3 T TENSOR
REMARK 3 T11: 0.0498 T22: 0.0261
REMARK 3 T33: 0.2022 T12: 0.0200
REMARK 3 T13: 0.0736 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 0.4398 L22: 1.3444
REMARK 3 L33: 1.0065 L12: 0.1240
REMARK 3 L13: -0.2030 L23: 0.1334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0428 S12: -0.0337 S13: 0.0702
REMARK 3 S21: 0.1511 S22: -0.0062 S23: 0.3724
REMARK 3 S31: -0.0455 S32: -0.0911 S33: -0.0366
REMARK 3
REMARK 3 TLS GROUP : 63
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 142 N 205
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1516 4.9631 65.0263
REMARK 3 T TENSOR
REMARK 3 T11: 0.1215 T22: 0.1291
REMARK 3 T33: 0.2717 T12: -0.0287
REMARK 3 T13: 0.1688 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.4012 L22: 1.8452
REMARK 3 L33: 1.9360 L12: -0.7657
REMARK 3 L13: 0.4001 L23: 0.2698
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.3242 S13: -0.0638
REMARK 3 S21: 0.2715 S22: 0.0591 S23: 0.4101
REMARK 3 S31: 0.0919 S32: -0.2764 S33: -0.0552
REMARK 3
REMARK 3 TLS GROUP : 64
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 206 N 225
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2689 -19.4636 68.7967
REMARK 3 T TENSOR
REMARK 3 T11: 0.3541 T22: 0.1928
REMARK 3 T33: 0.2935 T12: -0.0820
REMARK 3 T13: 0.0759 T23: 0.0738
REMARK 3 L TENSOR
REMARK 3 L11: 5.3479 L22: 5.8533
REMARK 3 L33: 3.0197 L12: -3.8506
REMARK 3 L13: -2.0483 L23: -1.1468
REMARK 3 S TENSOR
REMARK 3 S11: -0.3213 S12: -0.2358 S13: -0.5589
REMARK 3 S21: 0.2354 S22: 0.1891 S23: 0.5231
REMARK 3 S31: 0.1564 S32: 0.0680 S33: 0.1322
REMARK 3
REMARK 3 TLS GROUP : 65
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 11 O 77
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2621 -65.9892 56.3358
REMARK 3 T TENSOR
REMARK 3 T11: 0.3445 T22: 0.0705
REMARK 3 T33: 0.1724 T12: 0.0234
REMARK 3 T13: -0.0381 T23: 0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 1.3567 L22: 1.0895
REMARK 3 L33: 1.1078 L12: 0.0558
REMARK 3 L13: 0.5801 L23: -0.8990
REMARK 3 S TENSOR
REMARK 3 S11: 0.1321 S12: 0.0257 S13: -0.1302
REMARK 3 S21: 0.0115 S22: -0.0806 S23: 0.0050
REMARK 3 S31: 0.2051 S32: 0.1080 S33: -0.0514
REMARK 3
REMARK 3 TLS GROUP : 66
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 78 O 136
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3408 -52.3321 51.5389
REMARK 3 T TENSOR
REMARK 3 T11: 0.1899 T22: 0.0408
REMARK 3 T33: 0.1345 T12: -0.0186
REMARK 3 T13: -0.0086 T23: 0.0706
REMARK 3 L TENSOR
REMARK 3 L11: 0.3939 L22: 2.5437
REMARK 3 L33: 0.3378 L12: -0.9863
REMARK 3 L13: -0.0926 L23: 0.2605
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: -0.0336 S13: -0.0120
REMARK 3 S21: -0.0805 S22: 0.0638 S23: -0.0210
REMARK 3 S31: -0.0359 S32: -0.0315 S33: -0.0545
REMARK 3
REMARK 3 TLS GROUP : 67
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 137 O 197
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4893 -63.2831 62.7795
REMARK 3 T TENSOR
REMARK 3 T11: 0.1897 T22: 0.1104
REMARK 3 T33: 0.2956 T12: -0.0857
REMARK 3 T13: 0.0261 T23: 0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 0.2329 L22: 1.5642
REMARK 3 L33: 2.9164 L12: -0.0550
REMARK 3 L13: 0.3702 L23: 1.0999
REMARK 3 S TENSOR
REMARK 3 S11: 0.1366 S12: -0.1233 S13: -0.1190
REMARK 3 S21: 0.1829 S22: -0.1186 S23: 0.4915
REMARK 3 S31: 0.2107 S32: -0.2842 S33: -0.0181
REMARK 3
REMARK 3 TLS GROUP : 68
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 198 O 251
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2584 -62.7821 76.8849
REMARK 3 T TENSOR
REMARK 3 T11: 0.2601 T22: 0.1070
REMARK 3 T33: 0.0971 T12: 0.0188
REMARK 3 T13: 0.0001 T23: 0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.4006 L22: 2.8205
REMARK 3 L33: 2.7167 L12: -0.5702
REMARK 3 L13: 0.7394 L23: -1.3768
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: -0.4029 S13: -0.1480
REMARK 3 S21: 0.3130 S22: 0.0429 S23: -0.1181
REMARK 3 S31: 0.0090 S32: 0.1777 S33: -0.0493
REMARK 3
REMARK 3 TLS GROUP : 69
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 2 P 46
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0125 -65.0297 30.4576
REMARK 3 T TENSOR
REMARK 3 T11: 0.2456 T22: 0.0957
REMARK 3 T33: 0.3032 T12: -0.1022
REMARK 3 T13: -0.0799 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.3274 L22: 2.6137
REMARK 3 L33: 1.6103 L12: -0.4353
REMARK 3 L13: -0.5545 L23: -0.1961
REMARK 3 S TENSOR
REMARK 3 S11: -0.0516 S12: 0.0300 S13: -0.2103
REMARK 3 S21: 0.0534 S22: -0.1490 S23: 0.2047
REMARK 3 S31: 0.1374 S32: 0.0019 S33: 0.2006
REMARK 3
REMARK 3 TLS GROUP : 70
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 47 P 63
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3453 -64.4511 52.5969
REMARK 3 T TENSOR
REMARK 3 T11: 0.2217 T22: 0.2780
REMARK 3 T33: 0.3405 T12: 0.0022
REMARK 3 T13: 0.0237 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 4.0814 L22: 0.2300
REMARK 3 L33: 18.6481 L12: -0.9263
REMARK 3 L13: 8.7234 L23: -1.9849
REMARK 3 S TENSOR
REMARK 3 S11: 0.1200 S12: -0.0577 S13: -0.0282
REMARK 3 S21: -0.0416 S22: -0.0599 S23: 0.0284
REMARK 3 S31: 0.2848 S32: -0.1080 S33: -0.0601
REMARK 3
REMARK 3 TLS GROUP : 71
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 64 P 195
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1875 -56.5212 33.1860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1347 T22: 0.0567
REMARK 3 T33: 0.2374 T12: -0.0776
REMARK 3 T13: -0.0739 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.9141 L22: 1.1102
REMARK 3 L33: 0.9782 L12: 0.2505
REMARK 3 L13: -0.2100 L23: -0.2268
REMARK 3 S TENSOR
REMARK 3 S11: -0.0332 S12: 0.0847 S13: -0.1649
REMARK 3 S21: -0.0711 S22: -0.0042 S23: 0.3750
REMARK 3 S31: 0.1807 S32: -0.1702 S33: 0.0374
REMARK 3
REMARK 3 TLS GROUP : 72
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 196 P 250
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0440 -55.4163 46.6569
REMARK 3 T TENSOR
REMARK 3 T11: 0.1625 T22: 0.1980
REMARK 3 T33: 0.2989 T12: -0.0754
REMARK 3 T13: 0.0469 T23: 0.0716
REMARK 3 L TENSOR
REMARK 3 L11: 1.2143 L22: 6.4694
REMARK 3 L33: 0.9726 L12: 0.9504
REMARK 3 L13: 0.1949 L23: 0.1398
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.2236 S13: -0.1715
REMARK 3 S21: 0.1929 S22: -0.0117 S23: 0.6758
REMARK 3 S31: 0.2023 S32: -0.1215 S33: 0.0200
REMARK 3
REMARK 3 TLS GROUP : 73
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 2 Q 44
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6660 -65.3264 11.6115
REMARK 3 T TENSOR
REMARK 3 T11: 0.5716 T22: 0.0441
REMARK 3 T33: 0.2700 T12: -0.0009
REMARK 3 T13: -0.1127 T23: -0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 2.7288 L22: 1.1012
REMARK 3 L33: 0.6114 L12: 0.6503
REMARK 3 L13: -0.4936 L23: 0.2354
REMARK 3 S TENSOR
REMARK 3 S11: 0.1005 S12: -0.1225 S13: -0.3033
REMARK 3 S21: -0.2235 S22: 0.0025 S23: -0.1229
REMARK 3 S31: 0.3288 S32: 0.0606 S33: -0.1030
REMARK 3
REMARK 3 TLS GROUP : 74
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 45 Q 65
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5652 -62.0593 16.0648
REMARK 3 T TENSOR
REMARK 3 T11: 0.2593 T22: 0.3305
REMARK 3 T33: 0.3760 T12: -0.0765
REMARK 3 T13: -0.0973 T23: -0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 4.3028 L22: 2.6873
REMARK 3 L33: 12.0106 L12: 3.0041
REMARK 3 L13: -6.6611 L23: -3.6510
REMARK 3 S TENSOR
REMARK 3 S11: 0.1567 S12: 0.1596 S13: 0.1313
REMARK 3 S21: 0.2155 S22: -0.0888 S23: 0.1871
REMARK 3 S31: -0.0273 S32: -0.5931 S33: -0.0679
REMARK 3
REMARK 3 TLS GROUP : 75
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 66 Q 177
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0644 -52.1643 6.5390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2084 T22: 0.0241
REMARK 3 T33: 0.1613 T12: -0.0377
REMARK 3 T13: -0.0905 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 1.4082 L22: 0.5679
REMARK 3 L33: 0.0690 L12: 0.0394
REMARK 3 L13: 0.0523 L23: -0.1114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.0316 S13: -0.0839
REMARK 3 S21: -0.1706 S22: 0.0484 S23: 0.0034
REMARK 3 S31: 0.0753 S32: -0.0146 S33: -0.0376
REMARK 3
REMARK 3 TLS GROUP : 76
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 178 Q 245
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8199 -59.4534 1.8185
REMARK 3 T TENSOR
REMARK 3 T11: 0.2370 T22: 0.2254
REMARK 3 T33: 0.3338 T12: -0.0456
REMARK 3 T13: -0.1664 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 1.9889 L22: 3.5379
REMARK 3 L33: 4.4929 L12: 0.2382
REMARK 3 L13: -0.6632 L23: -1.4316
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: 0.2064 S13: 0.0956
REMARK 3 S21: 0.0631 S22: 0.0726 S23: 0.6733
REMARK 3 S31: -0.1592 S32: -0.6616 S33: -0.1303
REMARK 3
REMARK 3 TLS GROUP : 77
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 3 R 39
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7518 -63.2892 4.6679
REMARK 3 T TENSOR
REMARK 3 T11: 0.2586 T22: 0.0872
REMARK 3 T33: 0.2822 T12: 0.0006
REMARK 3 T13: 0.0309 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 0.8283 L22: 0.9071
REMARK 3 L33: 4.0685 L12: -0.3396
REMARK 3 L13: 1.5354 L23: 0.1070
REMARK 3 S TENSOR
REMARK 3 S11: 0.1604 S12: 0.0501 S13: -0.2207
REMARK 3 S21: -0.1516 S22: -0.0129 S23: 0.0188
REMARK 3 S31: 0.3593 S32: 0.0165 S33: -0.1474
REMARK 3
REMARK 3 TLS GROUP : 78
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 40 R 63
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9467 -57.2608 -10.6438
REMARK 3 T TENSOR
REMARK 3 T11: 0.6580 T22: 0.4268
REMARK 3 T33: 0.2642 T12: -0.0738
REMARK 3 T13: -0.0182 T23: -0.1477
REMARK 3 L TENSOR
REMARK 3 L11: 6.0826 L22: 0.1176
REMARK 3 L33: 0.0688 L12: 0.6309
REMARK 3 L13: 0.5296 L23: 0.0869
REMARK 3 S TENSOR
REMARK 3 S11: -0.1428 S12: 0.6785 S13: -0.1135
REMARK 3 S21: 0.0675 S22: 0.1044 S23: 0.0414
REMARK 3 S31: 0.0609 S32: 0.0474 S33: 0.0384
REMARK 3
REMARK 3 TLS GROUP : 79
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 64 R 187
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7665 -51.0604 -6.2401
REMARK 3 T TENSOR
REMARK 3 T11: 0.3375 T22: 0.0623
REMARK 3 T33: 0.1574 T12: -0.0026
REMARK 3 T13: 0.0143 T23: -0.0886
REMARK 3 L TENSOR
REMARK 3 L11: 1.1841 L22: 1.9131
REMARK 3 L33: 1.9405 L12: 0.0095
REMARK 3 L13: -0.1124 L23: 0.8226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: 0.1133 S13: -0.1617
REMARK 3 S21: -0.5085 S22: 0.1048 S23: 0.0017
REMARK 3 S31: 0.1503 S32: 0.1793 S33: -0.0939
REMARK 3
REMARK 3 TLS GROUP : 80
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 188 R 243
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1409 -58.4066 -23.2481
REMARK 3 T TENSOR
REMARK 3 T11: 0.6043 T22: 0.4593
REMARK 3 T33: 0.3145 T12: -0.0780
REMARK 3 T13: -0.1289 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.2874 L22: 1.7181
REMARK 3 L33: 1.3411 L12: -0.1063
REMARK 3 L13: 0.3444 L23: 0.5023
REMARK 3 S TENSOR
REMARK 3 S11: 0.1437 S12: 0.5199 S13: -0.3421
REMARK 3 S21: -0.2065 S22: 0.1855 S23: 0.2715
REMARK 3 S31: 0.2654 S32: -0.2562 S33: -0.3292
REMARK 3
REMARK 3 TLS GROUP : 81
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 9 S 35
REMARK 3 ORIGIN FOR THE GROUP (A): 55.3866 -66.8234 18.3885
REMARK 3 T TENSOR
REMARK 3 T11: 0.2586 T22: 0.1069
REMARK 3 T33: 0.3031 T12: 0.0654
REMARK 3 T13: 0.0453 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 0.4859 L22: 1.7353
REMARK 3 L33: 11.9196 L12: -0.0919
REMARK 3 L13: 2.0007 L23: -0.9157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.0402 S13: 0.0136
REMARK 3 S21: -0.0991 S22: -0.1290 S23: -0.0298
REMARK 3 S31: 0.3921 S32: 0.3465 S33: 0.1270
REMARK 3
REMARK 3 TLS GROUP : 82
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 36 S 85
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6925 -53.0989 -2.0771
REMARK 3 T TENSOR
REMARK 3 T11: 0.2886 T22: 0.1126
REMARK 3 T33: 0.2379 T12: 0.0543
REMARK 3 T13: 0.1600 T23: -0.0911
REMARK 3 L TENSOR
REMARK 3 L11: 3.3337 L22: 1.4096
REMARK 3 L33: 2.2217 L12: -0.3999
REMARK 3 L13: 1.4168 L23: -0.0910
REMARK 3 S TENSOR
REMARK 3 S11: 0.0463 S12: 0.2055 S13: -0.1914
REMARK 3 S21: -0.3116 S22: -0.0120 S23: -0.2977
REMARK 3 S31: -0.0273 S32: -0.0198 S33: -0.0343
REMARK 3
REMARK 3 TLS GROUP : 83
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 86 S 133
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9456 -44.0574 15.5831
REMARK 3 T TENSOR
REMARK 3 T11: 0.2241 T22: 0.1543
REMARK 3 T33: 0.2069 T12: 0.0489
REMARK 3 T13: 0.0280 T23: -0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 1.8599 L22: 4.1248
REMARK 3 L33: 0.8143 L12: 2.4130
REMARK 3 L13: -0.1165 L23: -0.2701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0300 S12: -0.1375 S13: 0.0381
REMARK 3 S21: 0.0349 S22: 0.0202 S23: 0.1231
REMARK 3 S31: 0.2590 S32: -0.0845 S33: -0.0503
REMARK 3
REMARK 3 TLS GROUP : 84
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 134 S 250
REMARK 3 ORIGIN FOR THE GROUP (A): 70.5344 -56.0197 -1.5704
REMARK 3 T TENSOR
REMARK 3 T11: 0.3507 T22: 0.1284
REMARK 3 T33: 0.3477 T12: 0.1292
REMARK 3 T13: 0.1736 T23: -0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 2.6295 L22: 0.3991
REMARK 3 L33: 1.7666 L12: -0.1143
REMARK 3 L13: -0.3045 L23: 0.3630
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: 0.2259 S13: -0.0991
REMARK 3 S21: -0.2601 S22: 0.0041 S23: -0.2964
REMARK 3 S31: 0.1324 S32: 0.2061 S33: -0.0273
REMARK 3
REMARK 3 TLS GROUP : 85
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 3 T 24
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3620 -70.8254 36.5598
REMARK 3 T TENSOR
REMARK 3 T11: 0.3652 T22: 0.2610
REMARK 3 T33: 0.3030 T12: 0.1329
REMARK 3 T13: -0.0728 T23: -0.0728
REMARK 3 L TENSOR
REMARK 3 L11: 8.4536 L22: 0.4335
REMARK 3 L33: 6.4820 L12: 1.9131
REMARK 3 L13: -7.3557 L23: -1.6670
REMARK 3 S TENSOR
REMARK 3 S11: -0.2428 S12: 0.2792 S13: -0.2997
REMARK 3 S21: -0.0530 S22: 0.0545 S23: -0.0746
REMARK 3 S31: 0.3218 S32: -0.1069 S33: 0.1883
REMARK 3
REMARK 3 TLS GROUP : 86
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 25 T 105
REMARK 3 ORIGIN FOR THE GROUP (A): 71.1378 -50.9449 32.3178
REMARK 3 T TENSOR
REMARK 3 T11: 0.2214 T22: 0.1488
REMARK 3 T33: 0.4733 T12: 0.1423
REMARK 3 T13: 0.0278 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.6468 L22: 1.3379
REMARK 3 L33: 2.1225 L12: -0.4006
REMARK 3 L13: -0.3690 L23: 1.2218
REMARK 3 S TENSOR
REMARK 3 S11: 0.1528 S12: -0.0128 S13: -0.2193
REMARK 3 S21: -0.1820 S22: -0.1004 S23: -0.2650
REMARK 3 S31: 0.2517 S32: 0.2015 S33: -0.0524
REMARK 3
REMARK 3 TLS GROUP : 87
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 106 T 125
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2959 -53.2703 39.8501
REMARK 3 T TENSOR
REMARK 3 T11: 0.2364 T22: 0.1129
REMARK 3 T33: 0.1830 T12: 0.0889
REMARK 3 T13: 0.0487 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 13.6648 L22: 9.3987
REMARK 3 L33: 3.6053 L12: 4.9772
REMARK 3 L13: 1.5779 L23: 0.7585
REMARK 3 S TENSOR
REMARK 3 S11: -0.3580 S12: 0.1094 S13: 0.2969
REMARK 3 S21: -0.2499 S22: 0.1024 S23: 0.3391
REMARK 3 S31: 0.0336 S32: -0.2278 S33: 0.2556
REMARK 3
REMARK 3 TLS GROUP : 88
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 126 T 234
REMARK 3 ORIGIN FOR THE GROUP (A): 80.1767 -56.4140 36.6669
REMARK 3 T TENSOR
REMARK 3 T11: 0.1657 T22: 0.1986
REMARK 3 T33: 0.5546 T12: 0.1602
REMARK 3 T13: -0.0195 T23: -0.0831
REMARK 3 L TENSOR
REMARK 3 L11: 1.2702 L22: 0.6783
REMARK 3 L33: 2.3157 L12: 0.0522
REMARK 3 L13: -0.0468 L23: -0.0449
REMARK 3 S TENSOR
REMARK 3 S11: 0.0427 S12: -0.0042 S13: -0.2410
REMARK 3 S21: -0.0341 S22: 0.0324 S23: -0.4986
REMARK 3 S31: 0.2931 S32: 0.5339 S33: -0.0751
REMARK 3
REMARK 3 TLS GROUP : 89
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 4 U 26
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3704 -72.0903 43.6171
REMARK 3 T TENSOR
REMARK 3 T11: 0.3043 T22: 0.0932
REMARK 3 T33: 0.1943 T12: -0.0394
REMARK 3 T13: -0.0322 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 11.9854 L22: 0.4937
REMARK 3 L33: 0.8537 L12: 0.3353
REMARK 3 L13: -1.8765 L23: -0.5647
REMARK 3 S TENSOR
REMARK 3 S11: -0.2641 S12: 0.3220 S13: -0.6732
REMARK 3 S21: -0.3585 S22: 0.0860 S23: -0.0416
REMARK 3 S31: 0.4041 S32: -0.1005 S33: 0.1780
REMARK 3
REMARK 3 TLS GROUP : 90
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 27 U 60
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2016 -62.3868 58.7965
REMARK 3 T TENSOR
REMARK 3 T11: 0.3367 T22: 0.1267
REMARK 3 T33: 0.3868 T12: 0.1394
REMARK 3 T13: -0.1484 T23: 0.0863
REMARK 3 L TENSOR
REMARK 3 L11: 1.8373 L22: 1.3309
REMARK 3 L33: 2.0972 L12: 1.1146
REMARK 3 L13: -0.0062 L23: -1.1264
REMARK 3 S TENSOR
REMARK 3 S11: 0.1773 S12: -0.1847 S13: -0.6641
REMARK 3 S21: 0.0392 S22: -0.1248 S23: -0.3889
REMARK 3 S31: 0.3444 S32: 0.1496 S33: -0.0526
REMARK 3
REMARK 3 TLS GROUP : 91
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 61 U 171
REMARK 3 ORIGIN FOR THE GROUP (A): 48.8163 -54.1275 56.1507
REMARK 3 T TENSOR
REMARK 3 T11: 0.2041 T22: 0.0502
REMARK 3 T33: 0.1613 T12: 0.0416
REMARK 3 T13: -0.0609 T23: 0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 1.2660 L22: 0.8672
REMARK 3 L33: 1.5048 L12: 0.2706
REMARK 3 L13: -0.0155 L23: 0.5852
REMARK 3 S TENSOR
REMARK 3 S11: 0.0432 S12: -0.1375 S13: -0.1543
REMARK 3 S21: 0.1180 S22: 0.0278 S23: -0.1834
REMARK 3 S31: 0.1686 S32: 0.0417 S33: -0.0710
REMARK 3
REMARK 3 TLS GROUP : 92
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 172 U 247
REMARK 3 ORIGIN FOR THE GROUP (A): 63.1992 -61.5265 69.5812
REMARK 3 T TENSOR
REMARK 3 T11: 0.2562 T22: 0.1919
REMARK 3 T33: 0.2637 T12: 0.0208
REMARK 3 T13: -0.1858 T23: 0.1130
REMARK 3 L TENSOR
REMARK 3 L11: 3.9731 L22: 4.0256
REMARK 3 L33: 1.5958 L12: -1.4959
REMARK 3 L13: -1.4113 L23: 0.6099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0338 S12: -0.4104 S13: -0.3306
REMARK 3 S21: 0.2067 S22: 0.0732 S23: -0.4494
REMARK 3 S31: 0.3253 S32: 0.2548 S33: -0.1070
REMARK 3
REMARK 3 TLS GROUP : 93
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 102
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5414 -25.6197 62.4411
REMARK 3 T TENSOR
REMARK 3 T11: 0.1377 T22: 0.0312
REMARK 3 T33: 0.0652 T12: -0.0263
REMARK 3 T13: 0.0138 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 0.7988 L22: 1.2163
REMARK 3 L33: 0.5322 L12: -0.0309
REMARK 3 L13: -0.1528 L23: -0.1855
REMARK 3 S TENSOR
REMARK 3 S11: 0.0620 S12: -0.0776 S13: -0.0854
REMARK 3 S21: 0.1514 S22: -0.0029 S23: 0.1684
REMARK 3 S31: 0.0512 S32: 0.0011 S33: -0.0591
REMARK 3
REMARK 3 TLS GROUP : 94
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 103 V 143
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8646 -17.6760 70.5155
REMARK 3 T TENSOR
REMARK 3 T11: 0.1100 T22: 0.1249
REMARK 3 T33: 0.0846 T12: -0.0346
REMARK 3 T13: -0.0160 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 2.1719 L22: 3.5476
REMARK 3 L33: 1.9722 L12: -0.5356
REMARK 3 L13: -0.1916 L23: 0.9023
REMARK 3 S TENSOR
REMARK 3 S11: 0.0586 S12: -0.2471 S13: -0.1684
REMARK 3 S21: 0.3639 S22: 0.0187 S23: -0.1457
REMARK 3 S31: 0.2253 S32: 0.0474 S33: -0.0773
REMARK 3
REMARK 3 TLS GROUP : 95
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 144 V 184
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1124 -15.8642 76.2466
REMARK 3 T TENSOR
REMARK 3 T11: 0.1452 T22: 0.1691
REMARK 3 T33: 0.0451 T12: -0.0190
REMARK 3 T13: 0.0675 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 1.4251 L22: 4.6774
REMARK 3 L33: 2.5486 L12: -1.9027
REMARK 3 L13: 1.6012 L23: -2.4172
REMARK 3 S TENSOR
REMARK 3 S11: -0.0594 S12: -0.2693 S13: 0.0134
REMARK 3 S21: 0.5100 S22: 0.0172 S23: 0.0919
REMARK 3 S31: -0.0887 S32: -0.0959 S33: 0.0422
REMARK 3
REMARK 3 TLS GROUP : 96
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 185 V 196
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1201 -12.4242 77.1921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2927 T22: 0.2889
REMARK 3 T33: 0.1295 T12: -0.0141
REMARK 3 T13: 0.0959 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 7.2497 L22: 13.5568
REMARK 3 L33: 2.1475 L12: 2.0182
REMARK 3 L13: 2.0477 L23: -3.6908
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: -0.5229 S13: 0.5913
REMARK 3 S21: 0.2123 S22: -0.0001 S23: 0.5032
REMARK 3 S31: -0.2718 S32: -0.1351 S33: -0.0199
REMARK 3
REMARK 3 TLS GROUP : 97
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 150
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7175 -24.1548 50.4525
REMARK 3 T TENSOR
REMARK 3 T11: 0.0953 T22: 0.0381
REMARK 3 T33: 0.1975 T12: -0.0342
REMARK 3 T13: 0.0017 T23: 0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 0.5148 L22: 1.4983
REMARK 3 L33: 0.5867 L12: -0.3328
REMARK 3 L13: -0.1029 L23: 0.4535
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: -0.0603 S13: -0.0259
REMARK 3 S21: 0.0891 S22: -0.0164 S23: 0.2736
REMARK 3 S31: 0.0789 S32: -0.0624 S33: -0.0146
REMARK 3
REMARK 3 TLS GROUP : 98
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 151 W 193
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6639 -17.9634 51.0573
REMARK 3 T TENSOR
REMARK 3 T11: 0.0421 T22: 0.1780
REMARK 3 T33: 0.2695 T12: -0.0408
REMARK 3 T13: 0.0427 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 0.0174 L22: 5.0945
REMARK 3 L33: 1.5495 L12: 0.0465
REMARK 3 L13: 0.1067 L23: -0.6820
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0116 S13: 0.0349
REMARK 3 S21: 0.2271 S22: -0.0219 S23: 0.5073
REMARK 3 S31: 0.0183 S32: -0.2331 S33: 0.0156
REMARK 3
REMARK 3 TLS GROUP : 99
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 194 W 201
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9730 -4.3097 34.1288
REMARK 3 T TENSOR
REMARK 3 T11: 0.1977 T22: 0.2669
REMARK 3 T33: 0.3176 T12: -0.0609
REMARK 3 T13: 0.0112 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 12.5231 L22: 13.5361
REMARK 3 L33: 32.2679 L12: -12.7806
REMARK 3 L13: 16.6028 L23: -19.1190
REMARK 3 S TENSOR
REMARK 3 S11: 0.1475 S12: 0.3251 S13: 0.0368
REMARK 3 S21: -0.2650 S22: -0.1655 S23: 0.0125
REMARK 3 S31: 0.8167 S32: -0.0290 S33: 0.0180
REMARK 3
REMARK 3 TLS GROUP : 100
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 202 W 220
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7197 -14.1518 10.2436
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.3156
REMARK 3 T33: 0.5165 T12: -0.0486
REMARK 3 T13: -0.1678 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 1.9170 L22: 1.8344
REMARK 3 L33: 4.4512 L12: 0.4685
REMARK 3 L13: -0.8810 L23: 1.7143
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: 0.3948 S13: -0.2172
REMARK 3 S21: -0.0117 S22: -0.0445 S23: 0.4535
REMARK 3 S31: 0.1656 S32: -0.0628 S33: 0.0236
REMARK 3
REMARK 3 TLS GROUP : 101
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X -7 X 67
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8065 -20.7270 15.0899
REMARK 3 T TENSOR
REMARK 3 T11: 0.1063 T22: 0.0436
REMARK 3 T33: 0.1595 T12: -0.0173
REMARK 3 T13: -0.1167 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.5780 L22: 2.8751
REMARK 3 L33: 1.1021 L12: 0.3042
REMARK 3 L13: -0.0226 L23: -0.9225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0300 S12: -0.0836 S13: -0.0083
REMARK 3 S21: -0.2403 S22: -0.0083 S23: 0.2412
REMARK 3 S31: 0.0147 S32: -0.1267 S33: 0.0383
REMARK 3
REMARK 3 TLS GROUP : 102
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 68 X 114
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8106 -28.7434 24.9026
REMARK 3 T TENSOR
REMARK 3 T11: 0.1137 T22: 0.0445
REMARK 3 T33: 0.1491 T12: 0.0107
REMARK 3 T13: -0.0336 T23: 0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 2.5503 L22: 3.4384
REMARK 3 L33: 2.5223 L12: 1.7821
REMARK 3 L13: 0.8071 L23: 0.9946
REMARK 3 S TENSOR
REMARK 3 S11: 0.1459 S12: 0.0211 S13: -0.0868
REMARK 3 S21: 0.0902 S22: -0.0470 S23: 0.2967
REMARK 3 S31: 0.1094 S32: -0.1036 S33: -0.0989
REMARK 3
REMARK 3 TLS GROUP : 103
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 115 X 126
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9251 -20.1801 30.1452
REMARK 3 T TENSOR
REMARK 3 T11: 0.4522 T22: 0.8743
REMARK 3 T33: 0.7160 T12: 0.0340
REMARK 3 T13: -0.0175 T23: 0.1377
REMARK 3 L TENSOR
REMARK 3 L11: 9.3365 L22: 0.0853
REMARK 3 L33: 0.2496 L12: 0.8410
REMARK 3 L13: 1.5185 L23: 0.1356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -1.4784 S13: 0.0641
REMARK 3 S21: -0.0090 S22: -0.0510 S23: 0.0026
REMARK 3 S31: -0.0245 S32: -0.2477 S33: 0.0491
REMARK 3
REMARK 3 TLS GROUP : 104
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 127 X 196
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0045 -11.6968 15.9570
REMARK 3 T TENSOR
REMARK 3 T11: 0.0726 T22: 0.0788
REMARK 3 T33: 0.3569 T12: -0.0207
REMARK 3 T13: -0.1192 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.9905 L22: 1.4437
REMARK 3 L33: 2.0706 L12: -0.2674
REMARK 3 L13: 0.0358 L23: 0.0095
REMARK 3 S TENSOR
REMARK 3 S11: 0.1211 S12: -0.0080 S13: -0.0013
REMARK 3 S21: -0.0345 S22: -0.0486 S23: 0.3752
REMARK 3 S31: 0.0064 S32: -0.3238 S33: -0.0725
REMARK 3
REMARK 3 TLS GROUP : 105
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 0 Y 28
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6455 -10.4109 -5.1581
REMARK 3 T TENSOR
REMARK 3 T11: 0.2992 T22: 0.0813
REMARK 3 T33: 0.1476 T12: 0.0338
REMARK 3 T13: 0.0050 T23: 0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 10.9379 L22: 2.8395
REMARK 3 L33: 1.0072 L12: 4.3236
REMARK 3 L13: 0.9893 L23: 0.7779
REMARK 3 S TENSOR
REMARK 3 S11: 0.3154 S12: 0.0267 S13: 0.2338
REMARK 3 S21: 0.1214 S22: -0.1072 S23: 0.0181
REMARK 3 S31: 0.1937 S32: 0.0924 S33: -0.2083
REMARK 3
REMARK 3 TLS GROUP : 106
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 29 Y 159
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3820 -19.7106 -1.1697
REMARK 3 T TENSOR
REMARK 3 T11: 0.1864 T22: 0.0053
REMARK 3 T33: 0.0537 T12: -0.0131
REMARK 3 T13: -0.0565 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.5586 L22: 1.9718
REMARK 3 L33: 1.2264 L12: -0.3418
REMARK 3 L13: -0.0796 L23: -0.2394
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: -0.0122 S13: -0.0868
REMARK 3 S21: -0.2315 S22: 0.0933 S23: 0.0736
REMARK 3 S31: -0.0137 S32: -0.0359 S33: -0.0271
REMARK 3
REMARK 3 TLS GROUP : 107
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 160 Y 190
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9395 -7.5928 -10.3159
REMARK 3 T TENSOR
REMARK 3 T11: 0.2041 T22: 0.1242
REMARK 3 T33: 0.0719 T12: 0.0102
REMARK 3 T13: -0.0083 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.1438 L22: 5.4050
REMARK 3 L33: 0.6677 L12: 0.9231
REMARK 3 L13: -0.0295 L23: 0.6692
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: 0.1113 S13: 0.0366
REMARK 3 S21: -0.4774 S22: -0.0550 S23: 0.0319
REMARK 3 S31: -0.0342 S32: -0.1100 S33: 0.0305
REMARK 3
REMARK 3 TLS GROUP : 108
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 191 Y 195
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5472 -8.6347 -17.5899
REMARK 3 T TENSOR
REMARK 3 T11: 0.8886 T22: 0.8775
REMARK 3 T33: 1.1870 T12: -0.2014
REMARK 3 T13: 0.1745 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 21.1784 L22: 10.7344
REMARK 3 L33: 2.2765 L12: 14.7161
REMARK 3 L13: -5.2216 L23: -4.3347
REMARK 3 S TENSOR
REMARK 3 S11: -0.2260 S12: 0.4049 S13: 0.7162
REMARK 3 S21: -0.0961 S22: -0.2135 S23: 0.0141
REMARK 3 S31: 0.0085 S32: 0.6304 S33: 0.4395
REMARK 3
REMARK 3 TLS GROUP : 109
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 32
REMARK 3 ORIGIN FOR THE GROUP (A): 60.1403 -7.4976 3.1727
REMARK 3 T TENSOR
REMARK 3 T11: 0.1553 T22: 0.1029
REMARK 3 T33: 0.2303 T12: -0.0313
REMARK 3 T13: 0.0809 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.8628 L22: 2.2328
REMARK 3 L33: 10.4946 L12: 1.1234
REMARK 3 L13: 3.5906 L23: 3.0365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.0257 S13: 0.1247
REMARK 3 S21: -0.0684 S22: 0.0022 S23: -0.1468
REMARK 3 S31: -0.2571 S32: -0.0773 S33: 0.0101
REMARK 3
REMARK 3 TLS GROUP : 110
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 33 Z 96
REMARK 3 ORIGIN FOR THE GROUP (A): 52.6189 -24.6159 5.3813
REMARK 3 T TENSOR
REMARK 3 T11: 0.2335 T22: 0.0467
REMARK 3 T33: 0.1243 T12: 0.0072
REMARK 3 T13: 0.0931 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 0.9696 L22: 1.0637
REMARK 3 L33: 1.2308 L12: 0.2155
REMARK 3 L13: 0.1371 L23: -0.0376
REMARK 3 S TENSOR
REMARK 3 S11: 0.0973 S12: 0.0406 S13: -0.0919
REMARK 3 S21: -0.4387 S22: 0.0277 S23: -0.2359
REMARK 3 S31: -0.0607 S32: 0.0089 S33: -0.1250
REMARK 3
REMARK 3 TLS GROUP : 111
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 97 Z 171
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5709 -8.6954 -4.5986
REMARK 3 T TENSOR
REMARK 3 T11: 0.2996 T22: 0.1325
REMARK 3 T33: 0.1611 T12: -0.0259
REMARK 3 T13: 0.1128 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 0.6096 L22: 2.7263
REMARK 3 L33: 1.0660 L12: 0.4869
REMARK 3 L13: 0.5970 L23: 0.0890
REMARK 3 S TENSOR
REMARK 3 S11: -0.0513 S12: 0.1960 S13: -0.0043
REMARK 3 S21: -0.4690 S22: 0.1445 S23: -0.0722
REMARK 3 S31: 0.1365 S32: 0.1408 S33: -0.0932
REMARK 3
REMARK 3 TLS GROUP : 112
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 172 Z 212
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8837 -2.8673 -4.2331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1485 T22: 0.1790
REMARK 3 T33: 0.1569 T12: 0.0222
REMARK 3 T13: 0.1100 T23: -0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 0.7770 L22: 6.9729
REMARK 3 L33: 0.8954 L12: 1.3990
REMARK 3 L13: 0.0738 L23: 0.0798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: 0.2418 S13: -0.0539
REMARK 3 S21: -0.3033 S22: 0.1154 S23: -0.5008
REMARK 3 S31: -0.0859 S32: 0.1206 S33: -0.1009
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4X6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 207816
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 49.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 68.4
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.19200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 20.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1RYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30MM MAGNESIUM ACETATE, 12% MPD, 0.1M
REMARK 280 MES PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 150.39500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 30-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 30-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 136650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 211550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -821.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, A, B, C, D, E, F, G, H,
REMARK 350 AND CHAINS: I, J, K, L, M, N, O, P, Q,
REMARK 350 AND CHAINS: R, S, T, U, V, W, X, Y, Z, a,
REMARK 350 AND CHAINS: e
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET 1 -27
REMARK 465 ALA 1 -26
REMARK 465 THR 1 -25
REMARK 465 ILE 1 -24
REMARK 465 ALA 1 -23
REMARK 465 SER 1 -22
REMARK 465 GLU 1 -21
REMARK 465 TYR 1 -20
REMARK 465 SER 1 -19
REMARK 465 SER 1 -18
REMARK 465 GLU 1 -17
REMARK 465 ALA 1 -16
REMARK 465 SER 1 -15
REMARK 465 ASN 1 -14
REMARK 465 THR 1 -13
REMARK 465 PRO 1 -12
REMARK 465 ILE 1 -11
REMARK 465 GLU 1 -10
REMARK 465 HIS 1 -9
REMARK 465 MET 2 -40
REMARK 465 ASN 2 -39
REMARK 465 HIS 2 -38
REMARK 465 ASP 2 -37
REMARK 465 PRO 2 -36
REMARK 465 PHE 2 -35
REMARK 465 SER 2 -34
REMARK 465 TRP 2 -33
REMARK 465 GLY 2 -32
REMARK 465 ARG 2 -31
REMARK 465 PRO 2 -30
REMARK 465 ALA 2 -29
REMARK 465 ASP 2 -28
REMARK 465 SER 2 -27
REMARK 465 THR 2 -26
REMARK 465 TYR 2 -25
REMARK 465 GLY 2 -24
REMARK 465 ALA 2 -23
REMARK 465 TYR 2 -22
REMARK 465 ASN 2 -21
REMARK 465 THR 2 -20
REMARK 465 GLN 2 -19
REMARK 465 ILE 2 -18
REMARK 465 ALA 2 -17
REMARK 465 ASN 2 -16
REMARK 465 ALA 2 -15
REMARK 465 GLY 2 -14
REMARK 465 ALA 2 -13
REMARK 465 SER 2 -12
REMARK 465 PRO 2 -11
REMARK 465 MET 2 -10
REMARK 465 VAL 2 -9
REMARK 465 ASN 2 -8
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 MET B 1
REMARK 465 LEU B 250
REMARK 465 MET C 1
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 ASP C 248
REMARK 465 GLU C 249
REMARK 465 ASP C 250
REMARK 465 GLU C 251
REMARK 465 GLU C 252
REMARK 465 ALA C 253
REMARK 465 ASP C 254
REMARK 465 GLU C 255
REMARK 465 ASP C 256
REMARK 465 MET C 257
REMARK 465 LYS C 258
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 244
REMARK 465 GLU D 245
REMARK 465 GLN D 246
REMARK 465 ASP D 247
REMARK 465 LYS D 248
REMARK 465 LYS D 249
REMARK 465 LYS D 250
REMARK 465 LYS D 251
REMARK 465 SER D 252
REMARK 465 ASN D 253
REMARK 465 HIS D 254
REMARK 465 MET E 1
REMARK 465 PHE E 2
REMARK 465 LEU E 3
REMARK 465 THR E 4
REMARK 465 ARG E 5
REMARK 465 SER E 6
REMARK 465 GLU E 7
REMARK 465 TYR E 8
REMARK 465 SER E 251
REMARK 465 PRO E 252
REMARK 465 GLU E 253
REMARK 465 GLU E 254
REMARK 465 ALA E 255
REMARK 465 ASP E 256
REMARK 465 VAL E 257
REMARK 465 GLU E 258
REMARK 465 MET E 259
REMARK 465 SER E 260
REMARK 465 MET F 1
REMARK 465 PHE F 2
REMARK 465 MET G 0
REMARK 465 THR G 1
REMARK 465 SER G 2
REMARK 465 ILE G 3
REMARK 465 GLY G 248
REMARK 465 ASP G 249
REMARK 465 ASP G 250
REMARK 465 ASP G 251
REMARK 465 GLU G 252
REMARK 465 ASP G 253
REMARK 465 GLU G 254
REMARK 465 ASP G 255
REMARK 465 ASP G 256
REMARK 465 SER G 257
REMARK 465 ASP G 258
REMARK 465 ASN G 259
REMARK 465 VAL G 260
REMARK 465 MET G 261
REMARK 465 SER G 262
REMARK 465 SER G 263
REMARK 465 ASP G 264
REMARK 465 ASP G 265
REMARK 465 GLU G 266
REMARK 465 ASN G 267
REMARK 465 ALA G 268
REMARK 465 PRO G 269
REMARK 465 VAL G 270
REMARK 465 ALA G 271
REMARK 465 THR G 272
REMARK 465 ASN G 273
REMARK 465 ALA G 274
REMARK 465 ASN G 275
REMARK 465 ALA G 276
REMARK 465 THR G 277
REMARK 465 THR G 278
REMARK 465 ASP G 279
REMARK 465 GLN G 280
REMARK 465 GLU G 281
REMARK 465 GLY G 282
REMARK 465 ASP G 283
REMARK 465 ILE G 284
REMARK 465 HIS G 285
REMARK 465 LEU G 286
REMARK 465 GLU G 287
REMARK 465 MET H -18
REMARK 465 ASN H -17
REMARK 465 GLY H -16
REMARK 465 ILE H -15
REMARK 465 GLN H -14
REMARK 465 VAL H -13
REMARK 465 ASP H -12
REMARK 465 ILE H -11
REMARK 465 ASN H -10
REMARK 465 ARG H -9
REMARK 465 LEU H -8
REMARK 465 LYS H -7
REMARK 465 LYS H -6
REMARK 465 GLY H -5
REMARK 465 GLU H -4
REMARK 465 VAL H -3
REMARK 465 SER H -2
REMARK 465 LEU H -1
REMARK 465 GLY H 0
REMARK 465 MET I -28
REMARK 465 ALA I -27
REMARK 465 GLY I -26
REMARK 465 LEU I -25
REMARK 465 SER I -24
REMARK 465 PHE I -23
REMARK 465 ASP I -22
REMARK 465 ASN I -21
REMARK 465 TYR I -20
REMARK 465 GLN I -19
REMARK 465 ARG I -18
REMARK 465 ASN I -17
REMARK 465 ASN I -16
REMARK 465 PHE I -15
REMARK 465 LEU I -14
REMARK 465 ALA I -13
REMARK 465 GLU I -12
REMARK 465 ASN I -11
REMARK 465 SER I -10
REMARK 465 HIS I -9
REMARK 465 THR I -8
REMARK 465 GLN I -7
REMARK 465 PRO I -6
REMARK 465 LYS I -5
REMARK 465 ALA I -4
REMARK 465 THR I -3
REMARK 465 SER I -2
REMARK 465 THR I -1
REMARK 465 GLY I 0
REMARK 465 ASP I 222
REMARK 465 ILE I 223
REMARK 465 GLN I 224
REMARK 465 GLU I 225
REMARK 465 GLU I 226
REMARK 465 GLN I 227
REMARK 465 VAL I 228
REMARK 465 ASP I 229
REMARK 465 ILE I 230
REMARK 465 THR I 231
REMARK 465 ALA I 232
REMARK 465 MET J -8
REMARK 465 ALA K 196
REMARK 465 GLN K 197
REMARK 465 MET L -74
REMARK 465 GLN L -73
REMARK 465 ALA L -72
REMARK 465 ILE L -71
REMARK 465 ALA L -70
REMARK 465 ASP L -69
REMARK 465 SER L -68
REMARK 465 PHE L -67
REMARK 465 SER L -66
REMARK 465 VAL L -65
REMARK 465 PRO L -64
REMARK 465 ASN L -63
REMARK 465 ARG L -62
REMARK 465 LEU L -61
REMARK 465 VAL L -60
REMARK 465 LYS L -59
REMARK 465 GLU L -58
REMARK 465 LEU L -57
REMARK 465 GLN L -56
REMARK 465 TYR L -55
REMARK 465 ASP L -54
REMARK 465 ASN L -53
REMARK 465 GLU L -52
REMARK 465 GLN L -51
REMARK 465 ASN L -50
REMARK 465 LEU L -49
REMARK 465 GLU L -48
REMARK 465 SER L -47
REMARK 465 ASP L -46
REMARK 465 PHE L -45
REMARK 465 VAL L -44
REMARK 465 THR L -43
REMARK 465 GLY L -42
REMARK 465 ALA L -41
REMARK 465 SER L -40
REMARK 465 GLN L -39
REMARK 465 PHE L -38
REMARK 465 GLN L -37
REMARK 465 ARG L -36
REMARK 465 LEU L -35
REMARK 465 ALA L -34
REMARK 465 PRO L -33
REMARK 465 SER L -32
REMARK 465 LEU L -31
REMARK 465 THR L -30
REMARK 465 VAL L -29
REMARK 465 PRO L -28
REMARK 465 PRO L -27
REMARK 465 ILE L -26
REMARK 465 ALA L -25
REMARK 465 SER L -24
REMARK 465 PRO L -23
REMARK 465 GLN L -22
REMARK 465 GLN L -21
REMARK 465 PHE L -20
REMARK 465 LEU L -19
REMARK 465 ARG L -18
REMARK 465 ALA L -17
REMARK 465 HIS L -16
REMARK 465 THR L -15
REMARK 465 ASP L -14
REMARK 465 ASP L -13
REMARK 465 SER L -12
REMARK 465 ARG L -11
REMARK 465 ASN L -10
REMARK 465 PRO L -9
REMARK 465 ASP L -8
REMARK 465 CYS L -7
REMARK 465 LYS L -6
REMARK 465 ILE L -5
REMARK 465 LYS L -4
REMARK 465 ILE L -3
REMARK 465 ALA L -2
REMARK 465 HIS L -1
REMARK 465 GLY L 0
REMARK 465 MET M -27
REMARK 465 ALA M -26
REMARK 465 THR M -25
REMARK 465 ILE M -24
REMARK 465 ALA M -23
REMARK 465 SER M -22
REMARK 465 GLU M -21
REMARK 465 TYR M -20
REMARK 465 SER M -19
REMARK 465 SER M -18
REMARK 465 GLU M -17
REMARK 465 ALA M -16
REMARK 465 SER M -15
REMARK 465 ASN M -14
REMARK 465 THR M -13
REMARK 465 PRO M -12
REMARK 465 ILE M -11
REMARK 465 GLU M -10
REMARK 465 HIS M -9
REMARK 465 MET N -40
REMARK 465 ASN N -39
REMARK 465 HIS N -38
REMARK 465 ASP N -37
REMARK 465 PRO N -36
REMARK 465 PHE N -35
REMARK 465 SER N -34
REMARK 465 TRP N -33
REMARK 465 GLY N -32
REMARK 465 ARG N -31
REMARK 465 PRO N -30
REMARK 465 ALA N -29
REMARK 465 ASP N -28
REMARK 465 SER N -27
REMARK 465 THR N -26
REMARK 465 TYR N -25
REMARK 465 GLY N -24
REMARK 465 ALA N -23
REMARK 465 TYR N -22
REMARK 465 ASN N -21
REMARK 465 THR N -20
REMARK 465 GLN N -19
REMARK 465 ILE N -18
REMARK 465 ALA N -17
REMARK 465 ASN N -16
REMARK 465 ALA N -15
REMARK 465 GLY N -14
REMARK 465 ALA N -13
REMARK 465 SER N -12
REMARK 465 PRO N -11
REMARK 465 MET N -10
REMARK 465 VAL N -9
REMARK 465 ASN N -8
REMARK 465 MET O 1
REMARK 465 SER O 2
REMARK 465 GLY O 3
REMARK 465 ALA O 4
REMARK 465 ALA O 5
REMARK 465 ALA O 6
REMARK 465 ALA O 7
REMARK 465 SER O 8
REMARK 465 ALA O 9
REMARK 465 ALA O 10
REMARK 465 ASP O 252
REMARK 465 MET P 1
REMARK 465 MET Q 1
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 ASP Q 248
REMARK 465 GLU Q 249
REMARK 465 ASP Q 250
REMARK 465 GLU Q 251
REMARK 465 GLU Q 252
REMARK 465 ALA Q 253
REMARK 465 ASP Q 254
REMARK 465 GLU Q 255
REMARK 465 ASP Q 256
REMARK 465 MET Q 257
REMARK 465 LYS Q 258
REMARK 465 MET R 1
REMARK 465 SER R 2
REMARK 465 GLN R 244
REMARK 465 GLU R 245
REMARK 465 GLN R 246
REMARK 465 ASP R 247
REMARK 465 LYS R 248
REMARK 465 LYS R 249
REMARK 465 LYS R 250
REMARK 465 LYS R 251
REMARK 465 SER R 252
REMARK 465 ASN R 253
REMARK 465 HIS R 254
REMARK 465 MET S 1
REMARK 465 PHE S 2
REMARK 465 LEU S 3
REMARK 465 THR S 4
REMARK 465 ARG S 5
REMARK 465 SER S 6
REMARK 465 GLU S 7
REMARK 465 TYR S 8
REMARK 465 SER S 251
REMARK 465 PRO S 252
REMARK 465 GLU S 253
REMARK 465 GLU S 254
REMARK 465 ALA S 255
REMARK 465 ASP S 256
REMARK 465 VAL S 257
REMARK 465 GLU S 258
REMARK 465 MET S 259
REMARK 465 SER S 260
REMARK 465 MET T 1
REMARK 465 PHE T 2
REMARK 465 MET U 0
REMARK 465 THR U 1
REMARK 465 SER U 2
REMARK 465 ILE U 3
REMARK 465 GLY U 248
REMARK 465 ASP U 249
REMARK 465 ASP U 250
REMARK 465 ASP U 251
REMARK 465 GLU U 252
REMARK 465 ASP U 253
REMARK 465 GLU U 254
REMARK 465 ASP U 255
REMARK 465 ASP U 256
REMARK 465 SER U 257
REMARK 465 ASP U 258
REMARK 465 ASN U 259
REMARK 465 VAL U 260
REMARK 465 MET U 261
REMARK 465 SER U 262
REMARK 465 SER U 263
REMARK 465 ASP U 264
REMARK 465 ASP U 265
REMARK 465 GLU U 266
REMARK 465 ASN U 267
REMARK 465 ALA U 268
REMARK 465 PRO U 269
REMARK 465 VAL U 270
REMARK 465 ALA U 271
REMARK 465 THR U 272
REMARK 465 ASN U 273
REMARK 465 ALA U 274
REMARK 465 ASN U 275
REMARK 465 ALA U 276
REMARK 465 THR U 277
REMARK 465 THR U 278
REMARK 465 ASP U 279
REMARK 465 GLN U 280
REMARK 465 GLU U 281
REMARK 465 GLY U 282
REMARK 465 ASP U 283
REMARK 465 ILE U 284
REMARK 465 HIS U 285
REMARK 465 LEU U 286
REMARK 465 GLU U 287
REMARK 465 MET V -18
REMARK 465 ASN V -17
REMARK 465 GLY V -16
REMARK 465 ILE V -15
REMARK 465 GLN V -14
REMARK 465 VAL V -13
REMARK 465 ASP V -12
REMARK 465 ILE V -11
REMARK 465 ASN V -10
REMARK 465 ARG V -9
REMARK 465 LEU V -8
REMARK 465 LYS V -7
REMARK 465 LYS V -6
REMARK 465 GLY V -5
REMARK 465 GLU V -4
REMARK 465 VAL V -3
REMARK 465 SER V -2
REMARK 465 LEU V -1
REMARK 465 GLY V 0
REMARK 465 MET W -28
REMARK 465 ALA W -27
REMARK 465 GLY W -26
REMARK 465 LEU W -25
REMARK 465 SER W -24
REMARK 465 PHE W -23
REMARK 465 ASP W -22
REMARK 465 ASN W -21
REMARK 465 TYR W -20
REMARK 465 GLN W -19
REMARK 465 ARG W -18
REMARK 465 ASN W -17
REMARK 465 ASN W -16
REMARK 465 PHE W -15
REMARK 465 LEU W -14
REMARK 465 ALA W -13
REMARK 465 GLU W -12
REMARK 465 ASN W -11
REMARK 465 SER W -10
REMARK 465 HIS W -9
REMARK 465 THR W -8
REMARK 465 GLN W -7
REMARK 465 PRO W -6
REMARK 465 LYS W -5
REMARK 465 ALA W -4
REMARK 465 THR W -3
REMARK 465 SER W -2
REMARK 465 THR W -1
REMARK 465 GLY W 0
REMARK 465 CYS W 221
REMARK 465 ASP W 222
REMARK 465 ILE W 223
REMARK 465 GLN W 224
REMARK 465 GLU W 225
REMARK 465 GLU W 226
REMARK 465 GLN W 227
REMARK 465 VAL W 228
REMARK 465 ASP W 229
REMARK 465 ILE W 230
REMARK 465 THR W 231
REMARK 465 ALA W 232
REMARK 465 MET X -8
REMARK 465 ALA Y 196
REMARK 465 GLN Y 197
REMARK 465 MET Z -74
REMARK 465 GLN Z -73
REMARK 465 ALA Z -72
REMARK 465 ILE Z -71
REMARK 465 ALA Z -70
REMARK 465 ASP Z -69
REMARK 465 SER Z -68
REMARK 465 PHE Z -67
REMARK 465 SER Z -66
REMARK 465 VAL Z -65
REMARK 465 PRO Z -64
REMARK 465 ASN Z -63
REMARK 465 ARG Z -62
REMARK 465 LEU Z -61
REMARK 465 VAL Z -60
REMARK 465 LYS Z -59
REMARK 465 GLU Z -58
REMARK 465 LEU Z -57
REMARK 465 GLN Z -56
REMARK 465 TYR Z -55
REMARK 465 ASP Z -54
REMARK 465 ASN Z -53
REMARK 465 GLU Z -52
REMARK 465 GLN Z -51
REMARK 465 ASN Z -50
REMARK 465 LEU Z -49
REMARK 465 GLU Z -48
REMARK 465 SER Z -47
REMARK 465 ASP Z -46
REMARK 465 PHE Z -45
REMARK 465 VAL Z -44
REMARK 465 THR Z -43
REMARK 465 GLY Z -42
REMARK 465 ALA Z -41
REMARK 465 SER Z -40
REMARK 465 GLN Z -39
REMARK 465 PHE Z -38
REMARK 465 GLN Z -37
REMARK 465 ARG Z -36
REMARK 465 LEU Z -35
REMARK 465 ALA Z -34
REMARK 465 PRO Z -33
REMARK 465 SER Z -32
REMARK 465 LEU Z -31
REMARK 465 THR Z -30
REMARK 465 VAL Z -29
REMARK 465 PRO Z -28
REMARK 465 PRO Z -27
REMARK 465 ILE Z -26
REMARK 465 ALA Z -25
REMARK 465 SER Z -24
REMARK 465 PRO Z -23
REMARK 465 GLN Z -22
REMARK 465 GLN Z -21
REMARK 465 PHE Z -20
REMARK 465 LEU Z -19
REMARK 465 ARG Z -18
REMARK 465 ALA Z -17
REMARK 465 HIS Z -16
REMARK 465 THR Z -15
REMARK 465 ASP Z -14
REMARK 465 ASP Z -13
REMARK 465 SER Z -12
REMARK 465 ARG Z -11
REMARK 465 ASN Z -10
REMARK 465 PRO Z -9
REMARK 465 ASP Z -8
REMARK 465 CYS Z -7
REMARK 465 LYS Z -6
REMARK 465 ILE Z -5
REMARK 465 LYS Z -4
REMARK 465 ILE Z -3
REMARK 465 ALA Z -2
REMARK 465 HIS Z -1
REMARK 465 GLY Z 0
REMARK 465 ARG a -9
REMARK 465 ARG a -8
REMARK 465 ARG a -7
REMARK 465 PRO a -6
REMARK 465 ARG a -5
REMARK 465 PRO a -4
REMARK 465 PRO a -3
REMARK 465 TYR a -2
REMARK 465 LEU a -1
REMARK 465 PRO a 0
REMARK 465 ARG e 1
REMARK 465 ARG e 2
REMARK 465 ARG e 3
REMARK 465 PRO e 4
REMARK 465 ARG e 5
REMARK 465 PRO e 6
REMARK 465 PRO e 7
REMARK 465 TYR e 8
REMARK 465 LEU e 9
REMARK 465 PRO e 10
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG J 19 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG J 19 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG Q 143 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP T 7 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG X 19 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG X 19 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP 1 23 -115.91 56.30
REMARK 500 ASP 1 39 29.59 48.86
REMARK 500 ASP 1 72 26.92 44.98
REMARK 500 LYS 1 91 44.12 -106.49
REMARK 500 PHE 1 94 70.32 -158.50
REMARK 500 ASP 1 106 -173.49 -63.06
REMARK 500 ALA 1 132 -67.26 -21.25
REMARK 500 ASP 1 191 -51.31 83.72
REMARK 500 ILE 2 -3 -74.53 -117.25
REMARK 500 THR 2 1 -142.05 -89.42
REMARK 500 ASN 2 18 46.24 -103.12
REMARK 500 ASN 2 40 12.15 -141.13
REMARK 500 ASP 2 69 49.91 38.04
REMARK 500 ALA 2 75 -119.32 -147.91
REMARK 500 SER 2 113 -34.25 -39.46
REMARK 500 ASP A 49 37.97 -147.31
REMARK 500 CYS A 114 -64.38 -20.53
REMARK 500 ASP B 3 96.36 -67.47
REMARK 500 TYR B 97 -70.66 -151.78
REMARK 500 GLN B 123 -34.78 -144.01
REMARK 500 SER B 199 7.20 -66.58
REMARK 500 VAL C 52 121.14 -39.57
REMARK 500 THR C 63 57.34 -151.31
REMARK 500 ASN C 70 162.70 176.19
REMARK 500 PRO C 130 164.06 -49.40
REMARK 500 TYR C 144 16.23 -143.11
REMARK 500 MET C 184 133.54 -34.73
REMARK 500 ALA C 220 -88.40 -108.94
REMARK 500 ASN D 40 58.04 -162.46
REMARK 500 GLN D 122 22.07 -144.11
REMARK 500 THR D 205 -71.97 -132.49
REMARK 500 GLU D 239 -40.49 159.35
REMARK 500 ARG E 10 138.00 -171.49
REMARK 500 SER E 35 171.83 -40.14
REMARK 500 ALA E 127 155.16 175.81
REMARK 500 SER E 128 -71.50 -95.20
REMARK 500 ALA E 179 -37.99 -35.82
REMARK 500 ALA E 249 105.12 152.79
REMARK 500 ASN F 4 69.70 79.17
REMARK 500 SER F 40 -153.42 -98.78
REMARK 500 LEU F 77 105.42 -58.34
REMARK 500 ASP F 138 -159.09 -129.42
REMARK 500 THR F 159 177.23 178.49
REMARK 500 GLN F 199 57.38 -65.53
REMARK 500 SER F 200 -7.67 -171.55
REMARK 500 ARG F 202 -81.82 -102.26
REMARK 500 GLU F 204 149.55 -177.21
REMARK 500 LYS F 232 -49.98 -28.47
REMARK 500 ASP G 43 19.10 -151.64
REMARK 500 GLN G 61 -13.49 79.41
REMARK 500
REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY I 181 LYS I 182 -149.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD 1 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 1 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 1 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD 2 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 2 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 2 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL I 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL J 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL K 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL M 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL M 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG M 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD N 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL N 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL O 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL O 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG P 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG R 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL S 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL T 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG T 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD V 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL V 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL V 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL W 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL Z 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL Z 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL Z 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 305
DBREF 4X6Z 1 -27 213 UNP P23724 PSB6_YEAST 1 241
DBREF 4X6Z 2 -40 225 UNP P30657 PSB7_YEAST 1 266
DBREF 4X6Z A 1 252 UNP P21243 PSA1_YEAST 1 252
DBREF 4X6Z B 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4X6Z C 1 258 UNP P23638 PSA3_YEAST 1 258
DBREF 4X6Z D 1 254 UNP P40303 PSA4_YEAST 1 254
DBREF 4X6Z E 1 260 UNP P32379 PSA5_YEAST 1 260
DBREF 4X6Z F 1 234 UNP P40302 PSA6_YEAST 1 234
DBREF 4X6Z G 0 287 UNP P21242 PSA7_YEAST 1 288
DBREF 4X6Z H -18 196 UNP P38624 PSB1_YEAST 1 215
DBREF 4X6Z I -28 232 UNP P25043 PSB2_YEAST 1 261
DBREF 4X6Z J -8 196 UNP P25451 PSB3_YEAST 1 205
DBREF 4X6Z K 0 197 UNP P22141 PSB4_YEAST 1 198
DBREF 4X6Z L -74 212 UNP P30656 PSB5_YEAST 1 287
DBREF 4X6Z M -27 213 UNP P23724 PSB6_YEAST 1 241
DBREF 4X6Z N -40 225 UNP P30657 PSB7_YEAST 1 266
DBREF 4X6Z O 1 252 UNP P21243 PSA1_YEAST 1 252
DBREF 4X6Z P 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4X6Z Q 1 258 UNP P23638 PSA3_YEAST 1 258
DBREF 4X6Z R 1 254 UNP P40303 PSA4_YEAST 1 254
DBREF 4X6Z S 1 260 UNP P32379 PSA5_YEAST 1 260
DBREF 4X6Z T 1 234 UNP P40302 PSA6_YEAST 1 234
DBREF 4X6Z U 0 287 UNP P21242 PSA7_YEAST 1 288
DBREF 4X6Z V -18 196 UNP P38624 PSB1_YEAST 1 215
DBREF 4X6Z W -28 232 UNP P25043 PSB2_YEAST 1 261
DBREF 4X6Z X -8 196 UNP P25451 PSB3_YEAST 1 205
DBREF 4X6Z Y 0 197 UNP P22141 PSB4_YEAST 1 198
DBREF 4X6Z Z -74 212 UNP P30656 PSB5_YEAST 1 287
DBREF 4X6Z a -9 3 PDB 4X6Z 4X6Z -9 3
DBREF 4X6Z e 1 13 PDB 4X6Z 4X6Z 1 13
SEQRES 1 1 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 1 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 1 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 1 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 1 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 1 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 1 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 1 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 1 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 1 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 1 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 1 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 1 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 1 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 1 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 1 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 1 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 1 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 1 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 2 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 2 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 2 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 2 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 2 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 2 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 2 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 2 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 2 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 2 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 2 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 2 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 2 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 2 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 2 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 2 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 2 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 2 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 2 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 2 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 2 266 TYR GLY THR GLN LYS ILE
SEQRES 1 A 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 A 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 A 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 A 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 A 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 A 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 A 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 A 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 A 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 A 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 A 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 A 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 A 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 A 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 A 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 A 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 A 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 A 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 A 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 A 252 ILE ALA GLU GLN ASP
SEQRES 1 B 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 B 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 B 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 B 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 B 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 B 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 B 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 B 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 B 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 B 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 B 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 B 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 B 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 B 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 B 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 B 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 B 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 B 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 B 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 B 250 GLU ALA LEU
SEQRES 1 C 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 C 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 C 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 C 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 C 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 C 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 C 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 C 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 C 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 C 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 C 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 C 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 C 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 C 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 C 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 C 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 C 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 C 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 C 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 C 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 D 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 D 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 D 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 D 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 D 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 D 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 D 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 D 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 D 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 D 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 D 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 D 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 D 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 D 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 D 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 D 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 D 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 D 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 D 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 D 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 E 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 E 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 E 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 E 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 E 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 E 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 E 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 E 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 E 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 E 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 E 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 E 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 E 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 E 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 E 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 E 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 E 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 E 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 E 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 E 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 F 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 F 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 F 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 F 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 F 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 F 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 F 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 F 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 F 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 F 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 F 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 F 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 F 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 F 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 F 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 F 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 F 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 F 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 G 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 G 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 G 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 G 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 G 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 G 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 G 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 G 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 G 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 G 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 G 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 G 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 G 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 G 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 G 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 G 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 G 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 G 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 G 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 G 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 G 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 G 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 G 288 LEU GLU
SEQRES 1 H 215 MET ASN GLY ILE GLN VAL ASP ILE ASN ARG LEU LYS LYS
SEQRES 2 H 215 GLY GLU VAL SER LEU GLY THR SER ILE MET ALA VAL THR
SEQRES 3 H 215 PHE LYS ASP GLY VAL ILE LEU GLY ALA ASP SER ARG THR
SEQRES 4 H 215 THR THR GLY ALA TYR ILE ALA ASN ARG VAL THR ASP LYS
SEQRES 5 H 215 LEU THR ARG VAL HIS ASP LYS ILE TRP CYS CYS ARG SER
SEQRES 6 H 215 GLY SER ALA ALA ASP THR GLN ALA ILE ALA ASP ILE VAL
SEQRES 7 H 215 GLN TYR HIS LEU GLU LEU TYR THR SER GLN TYR GLY THR
SEQRES 8 H 215 PRO SER THR GLU THR ALA ALA SER VAL PHE LYS GLU LEU
SEQRES 9 H 215 CYS TYR GLU ASN LYS ASP ASN LEU THR ALA GLY ILE ILE
SEQRES 10 H 215 VAL ALA GLY TYR ASP ASP LYS ASN LYS GLY GLU VAL TYR
SEQRES 11 H 215 THR ILE PRO LEU GLY GLY SER VAL HIS LYS LEU PRO TYR
SEQRES 12 H 215 ALA ILE ALA GLY SER GLY SER THR PHE ILE TYR GLY TYR
SEQRES 13 H 215 CYS ASP LYS ASN PHE ARG GLU ASN MET SER LYS GLU GLU
SEQRES 14 H 215 THR VAL ASP PHE ILE LYS HIS SER LEU SER GLN ALA ILE
SEQRES 15 H 215 LYS TRP ASP GLY SER SER GLY GLY VAL ILE ARG MET VAL
SEQRES 16 H 215 VAL LEU THR ALA ALA GLY VAL GLU ARG LEU ILE PHE TYR
SEQRES 17 H 215 PRO ASP GLU TYR GLU GLN LEU
SEQRES 1 I 261 MET ALA GLY LEU SER PHE ASP ASN TYR GLN ARG ASN ASN
SEQRES 2 I 261 PHE LEU ALA GLU ASN SER HIS THR GLN PRO LYS ALA THR
SEQRES 3 I 261 SER THR GLY THR THR ILE VAL GLY VAL LYS PHE ASN ASN
SEQRES 4 I 261 GLY VAL VAL ILE ALA ALA ASP THR ARG SER THR GLN GLY
SEQRES 5 I 261 PRO ILE VAL ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG
SEQRES 6 I 261 ILE SER PRO LYS ILE TRP CYS ALA GLY ALA GLY THR ALA
SEQRES 7 I 261 ALA ASP THR GLU ALA VAL THR GLN LEU ILE GLY SER ASN
SEQRES 8 I 261 ILE GLU LEU HIS SER LEU TYR THR SER ARG GLU PRO ARG
SEQRES 9 I 261 VAL VAL SER ALA LEU GLN MET LEU LYS GLN HIS LEU PHE
SEQRES 10 I 261 LYS TYR GLN GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA
SEQRES 11 I 261 GLY VAL ASP PRO THR GLY SER HIS LEU PHE SER ILE HIS
SEQRES 12 I 261 ALA HIS GLY SER THR ASP VAL GLY TYR TYR LEU SER LEU
SEQRES 13 I 261 GLY SER GLY SER LEU ALA ALA MET ALA VAL LEU GLU SER
SEQRES 14 I 261 HIS TRP LYS GLN ASP LEU THR LYS GLU GLU ALA ILE LYS
SEQRES 15 I 261 LEU ALA SER ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP
SEQRES 16 I 261 LEU GLY SER GLY SER ASN VAL ASP VAL CYS VAL MET GLU
SEQRES 17 I 261 ILE GLY LYS ASP ALA GLU TYR LEU ARG ASN TYR LEU THR
SEQRES 18 I 261 PRO ASN VAL ARG GLU GLU LYS GLN LYS SER TYR LYS PHE
SEQRES 19 I 261 PRO ARG GLY THR THR ALA VAL LEU LYS GLU SER ILE VAL
SEQRES 20 I 261 ASN ILE CYS ASP ILE GLN GLU GLU GLN VAL ASP ILE THR
SEQRES 21 I 261 ALA
SEQRES 1 J 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 J 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 J 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 J 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 J 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 J 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 J 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 J 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 J 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 J 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 J 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 J 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 J 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 J 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 J 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 J 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 K 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 K 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 K 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 K 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 K 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 K 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 K 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 K 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 K 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 K 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 K 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 K 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 K 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 K 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 K 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 K 198 GLN ALA GLN
SEQRES 1 L 287 MET GLN ALA ILE ALA ASP SER PHE SER VAL PRO ASN ARG
SEQRES 2 L 287 LEU VAL LYS GLU LEU GLN TYR ASP ASN GLU GLN ASN LEU
SEQRES 3 L 287 GLU SER ASP PHE VAL THR GLY ALA SER GLN PHE GLN ARG
SEQRES 4 L 287 LEU ALA PRO SER LEU THR VAL PRO PRO ILE ALA SER PRO
SEQRES 5 L 287 GLN GLN PHE LEU ARG ALA HIS THR ASP ASP SER ARG ASN
SEQRES 6 L 287 PRO ASP CYS LYS ILE LYS ILE ALA HIS GLY THR THR THR
SEQRES 7 L 287 LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE VAL ALA VAL
SEQRES 8 L 287 ASP SER ARG ALA THR ALA GLY ASN TRP VAL ALA SER GLN
SEQRES 9 L 287 THR VAL LYS LYS VAL ILE GLU ILE ASN PRO PHE LEU LEU
SEQRES 10 L 287 GLY THR MET ALA GLY GLY ALA ALA ASP CYS GLN PHE TRP
SEQRES 11 L 287 GLU THR TRP LEU GLY SER GLN CYS ARG LEU HIS GLU LEU
SEQRES 12 L 287 ARG GLU LYS GLU ARG ILE SER VAL ALA ALA ALA SER LYS
SEQRES 13 L 287 ILE LEU SER ASN LEU VAL TYR GLN TYR LYS GLY ALA GLY
SEQRES 14 L 287 LEU SER MET GLY THR MET ILE CYS GLY TYR THR ARG LYS
SEQRES 15 L 287 GLU GLY PRO THR ILE TYR TYR VAL ASP SER ASP GLY THR
SEQRES 16 L 287 ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY SER GLY GLN
SEQRES 17 L 287 THR PHE ALA TYR GLY VAL LEU ASP SER ASN TYR LYS TRP
SEQRES 18 L 287 ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY LYS ARG
SEQRES 19 L 287 SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR SER GLY
SEQRES 20 L 287 GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP GLY TRP
SEQRES 21 L 287 ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU PHE TRP
SEQRES 22 L 287 LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN VAL ILE
SEQRES 23 L 287 GLY
SEQRES 1 M 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 M 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 M 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 M 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 M 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 M 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 M 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 M 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 M 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 M 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 M 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 M 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 M 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 M 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 M 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 M 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 M 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 M 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 M 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 N 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 N 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 N 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 N 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 N 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 N 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 N 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 N 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 N 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 N 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 N 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 N 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 N 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 N 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 N 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 N 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 N 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 N 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 N 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 N 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 N 266 TYR GLY THR GLN LYS ILE
SEQRES 1 O 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 O 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 O 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 O 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 O 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 O 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 O 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 O 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 O 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 O 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 O 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 O 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 O 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 O 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 O 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 O 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 O 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 O 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 O 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 O 252 ILE ALA GLU GLN ASP
SEQRES 1 P 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 P 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 P 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 P 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 P 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 P 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 P 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 P 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 P 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 P 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 P 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 P 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 P 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 P 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 P 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 P 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 P 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 P 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 P 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 P 250 GLU ALA LEU
SEQRES 1 Q 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 Q 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 Q 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 Q 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 Q 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 Q 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 Q 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 Q 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 Q 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 Q 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 Q 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 Q 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 Q 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 Q 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 Q 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 Q 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 Q 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 Q 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 Q 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 Q 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 R 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 R 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 R 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 R 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 R 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 R 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 R 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 R 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 R 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 R 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 R 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 R 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 R 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 R 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 R 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 R 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 R 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 R 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 R 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 R 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 S 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 S 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 S 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 S 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 S 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 S 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 S 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 S 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 S 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 S 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 S 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 S 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 S 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 S 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 S 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 S 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 S 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 S 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 S 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 S 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 T 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 T 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 T 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 T 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 T 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 T 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 T 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 T 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 T 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 T 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 T 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 T 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 T 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 T 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 T 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 T 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 T 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 T 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 U 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 U 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 U 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 U 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 U 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 U 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 U 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 U 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 U 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 U 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 U 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 U 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 U 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 U 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 U 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 U 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 U 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 U 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 U 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 U 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 U 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 U 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 U 288 LEU GLU
SEQRES 1 V 215 MET ASN GLY ILE GLN VAL ASP ILE ASN ARG LEU LYS LYS
SEQRES 2 V 215 GLY GLU VAL SER LEU GLY THR SER ILE MET ALA VAL THR
SEQRES 3 V 215 PHE LYS ASP GLY VAL ILE LEU GLY ALA ASP SER ARG THR
SEQRES 4 V 215 THR THR GLY ALA TYR ILE ALA ASN ARG VAL THR ASP LYS
SEQRES 5 V 215 LEU THR ARG VAL HIS ASP LYS ILE TRP CYS CYS ARG SER
SEQRES 6 V 215 GLY SER ALA ALA ASP THR GLN ALA ILE ALA ASP ILE VAL
SEQRES 7 V 215 GLN TYR HIS LEU GLU LEU TYR THR SER GLN TYR GLY THR
SEQRES 8 V 215 PRO SER THR GLU THR ALA ALA SER VAL PHE LYS GLU LEU
SEQRES 9 V 215 CYS TYR GLU ASN LYS ASP ASN LEU THR ALA GLY ILE ILE
SEQRES 10 V 215 VAL ALA GLY TYR ASP ASP LYS ASN LYS GLY GLU VAL TYR
SEQRES 11 V 215 THR ILE PRO LEU GLY GLY SER VAL HIS LYS LEU PRO TYR
SEQRES 12 V 215 ALA ILE ALA GLY SER GLY SER THR PHE ILE TYR GLY TYR
SEQRES 13 V 215 CYS ASP LYS ASN PHE ARG GLU ASN MET SER LYS GLU GLU
SEQRES 14 V 215 THR VAL ASP PHE ILE LYS HIS SER LEU SER GLN ALA ILE
SEQRES 15 V 215 LYS TRP ASP GLY SER SER GLY GLY VAL ILE ARG MET VAL
SEQRES 16 V 215 VAL LEU THR ALA ALA GLY VAL GLU ARG LEU ILE PHE TYR
SEQRES 17 V 215 PRO ASP GLU TYR GLU GLN LEU
SEQRES 1 W 261 MET ALA GLY LEU SER PHE ASP ASN TYR GLN ARG ASN ASN
SEQRES 2 W 261 PHE LEU ALA GLU ASN SER HIS THR GLN PRO LYS ALA THR
SEQRES 3 W 261 SER THR GLY THR THR ILE VAL GLY VAL LYS PHE ASN ASN
SEQRES 4 W 261 GLY VAL VAL ILE ALA ALA ASP THR ARG SER THR GLN GLY
SEQRES 5 W 261 PRO ILE VAL ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG
SEQRES 6 W 261 ILE SER PRO LYS ILE TRP CYS ALA GLY ALA GLY THR ALA
SEQRES 7 W 261 ALA ASP THR GLU ALA VAL THR GLN LEU ILE GLY SER ASN
SEQRES 8 W 261 ILE GLU LEU HIS SER LEU TYR THR SER ARG GLU PRO ARG
SEQRES 9 W 261 VAL VAL SER ALA LEU GLN MET LEU LYS GLN HIS LEU PHE
SEQRES 10 W 261 LYS TYR GLN GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA
SEQRES 11 W 261 GLY VAL ASP PRO THR GLY SER HIS LEU PHE SER ILE HIS
SEQRES 12 W 261 ALA HIS GLY SER THR ASP VAL GLY TYR TYR LEU SER LEU
SEQRES 13 W 261 GLY SER GLY SER LEU ALA ALA MET ALA VAL LEU GLU SER
SEQRES 14 W 261 HIS TRP LYS GLN ASP LEU THR LYS GLU GLU ALA ILE LYS
SEQRES 15 W 261 LEU ALA SER ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP
SEQRES 16 W 261 LEU GLY SER GLY SER ASN VAL ASP VAL CYS VAL MET GLU
SEQRES 17 W 261 ILE GLY LYS ASP ALA GLU TYR LEU ARG ASN TYR LEU THR
SEQRES 18 W 261 PRO ASN VAL ARG GLU GLU LYS GLN LYS SER TYR LYS PHE
SEQRES 19 W 261 PRO ARG GLY THR THR ALA VAL LEU LYS GLU SER ILE VAL
SEQRES 20 W 261 ASN ILE CYS ASP ILE GLN GLU GLU GLN VAL ASP ILE THR
SEQRES 21 W 261 ALA
SEQRES 1 X 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 X 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 X 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 X 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 X 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 X 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 X 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 X 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 X 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 X 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 X 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 X 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 X 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 X 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 X 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 X 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 Y 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 Y 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 Y 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 Y 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 Y 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 Y 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 Y 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 Y 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 Y 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 Y 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 Y 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 Y 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 Y 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 Y 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 Y 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 Y 198 GLN ALA GLN
SEQRES 1 Z 287 MET GLN ALA ILE ALA ASP SER PHE SER VAL PRO ASN ARG
SEQRES 2 Z 287 LEU VAL LYS GLU LEU GLN TYR ASP ASN GLU GLN ASN LEU
SEQRES 3 Z 287 GLU SER ASP PHE VAL THR GLY ALA SER GLN PHE GLN ARG
SEQRES 4 Z 287 LEU ALA PRO SER LEU THR VAL PRO PRO ILE ALA SER PRO
SEQRES 5 Z 287 GLN GLN PHE LEU ARG ALA HIS THR ASP ASP SER ARG ASN
SEQRES 6 Z 287 PRO ASP CYS LYS ILE LYS ILE ALA HIS GLY THR THR THR
SEQRES 7 Z 287 LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE VAL ALA VAL
SEQRES 8 Z 287 ASP SER ARG ALA THR ALA GLY ASN TRP VAL ALA SER GLN
SEQRES 9 Z 287 THR VAL LYS LYS VAL ILE GLU ILE ASN PRO PHE LEU LEU
SEQRES 10 Z 287 GLY THR MET ALA GLY GLY ALA ALA ASP CYS GLN PHE TRP
SEQRES 11 Z 287 GLU THR TRP LEU GLY SER GLN CYS ARG LEU HIS GLU LEU
SEQRES 12 Z 287 ARG GLU LYS GLU ARG ILE SER VAL ALA ALA ALA SER LYS
SEQRES 13 Z 287 ILE LEU SER ASN LEU VAL TYR GLN TYR LYS GLY ALA GLY
SEQRES 14 Z 287 LEU SER MET GLY THR MET ILE CYS GLY TYR THR ARG LYS
SEQRES 15 Z 287 GLU GLY PRO THR ILE TYR TYR VAL ASP SER ASP GLY THR
SEQRES 16 Z 287 ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY SER GLY GLN
SEQRES 17 Z 287 THR PHE ALA TYR GLY VAL LEU ASP SER ASN TYR LYS TRP
SEQRES 18 Z 287 ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY LYS ARG
SEQRES 19 Z 287 SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR SER GLY
SEQRES 20 Z 287 GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP GLY TRP
SEQRES 21 Z 287 ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU PHE TRP
SEQRES 22 Z 287 LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN VAL ILE
SEQRES 23 Z 287 GLY
SEQRES 1 a 13 ARG ARG ARG PRO ARG PRO PRO TYR LEU PRO ARG PHE GLY
SEQRES 1 e 13 ARG ARG ARG PRO ARG PRO PRO TYR LEU PRO ARG PHE GLY
HET MPD 1 301 8
HET GOL 1 302 6
HET GOL 1 303 6
HET MG 1 304 1
HET MPD 2 301 8
HET GOL 2 302 6
HET GOL 2 303 6
HET MG 2 304 1
HET MG 2 305 1
HET MG 2 306 1
HET MG 2 307 1
HET MG 2 308 1
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET MG B 301 1
HET MG C 301 1
HET MG C 302 1
HET GOL D 301 6
HET MG D 302 1
HET GOL E 301 6
HET GOL F 301 6
HET GOL F 302 6
HET GOL F 303 6
HET GOL F 304 6
HET MG F 305 1
HET GOL G 301 6
HET GOL G 302 6
HET GOL H 201 6
HET MG H 202 1
HET MG H 203 1
HET MG H 204 1
HET MG H 205 1
HET GOL I 301 6
HET GOL I 302 6
HET MG J 201 1
HET GOL J 202 6
HET MG J 203 1
HET MG J 204 1
HET MG J 205 1
HET MG J 206 1
HET MG J 207 1
HET GOL K 201 6
HET MG K 202 1
HET MG K 203 1
HET MPD L 301 8
HET GOL L 302 6
HET GOL L 303 6
HET MG L 304 1
HET MG L 305 1
HET MPD M 301 8
HET GOL M 302 6
HET GOL M 303 6
HET MG M 304 1
HET MG M 305 1
HET MG M 306 1
HET MG M 307 1
HET MPD N 301 8
HET GOL N 302 6
HET GOL N 303 6
HET MG N 304 1
HET MG N 305 1
HET MG N 306 1
HET MG N 307 1
HET GOL O 301 6
HET GOL O 302 6
HET MG O 303 1
HET MG P 301 1
HET MG Q 301 1
HET MG Q 302 1
HET MG R 301 1
HET MG R 302 1
HET MG R 303 1
HET GOL S 301 6
HET MG S 302 1
HET MG S 303 1
HET MPD T 301 8
HET GOL T 302 6
HET MG T 303 1
HET MG T 304 1
HET MPD V 201 8
HET GOL V 202 6
HET GOL V 203 6
HET MG V 204 1
HET MG V 205 1
HET MG V 206 1
HET MG V 207 1
HET GOL W 301 6
HET MG W 302 1
HET MPD X 201 8
HET GOL X 202 6
HET MG X 203 1
HET MG X 204 1
HET MG X 205 1
HET MG Y 201 1
HET MG Y 202 1
HET MPD Z 301 8
HET GOL Z 302 6
HET GOL Z 303 6
HET GOL Z 304 6
HET MG Z 305 1
HET MG Z 306 1
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 31 MPD 9(C6 H14 O2)
FORMUL 32 GOL 38(C3 H8 O3)
FORMUL 34 MG 56(MG 2+)
FORMUL 34 HOH *359(H2 O)
HELIX 1 AA1 PHE 1 48 HIS 1 70 1 23
HELIX 2 AA2 SER 1 76 LYS 1 91 1 16
HELIX 3 AA3 ALA 1 133 VAL 1 145 1 13
HELIX 4 AA4 SER 1 167 HIS 1 186 1 20
HELIX 5 AA5 ILE 2 49 TYR 2 68 1 20
HELIX 6 AA6 GLU 2 80 SER 2 97 1 18
HELIX 7 AA7 GLY 2 137 LYS 2 149 1 13
HELIX 8 AA8 ARG 2 153 ILE 2 157 5 5
HELIX 9 AA9 THR 2 161 ASP 2 180 1 20
HELIX 10 AB1 TRP 2 211 ILE 2 217 5 7
HELIX 11 AB2 LEU A 25 THR A 35 1 11
HELIX 12 AB3 ASN A 36 ASN A 39 5 4
HELIX 13 AB4 ASP A 65 VAL A 69 5 5
HELIX 14 AB5 PRO A 86 GLY A 109 1 24
HELIX 15 AB6 PRO A 113 ARG A 131 1 19
HELIX 16 AB7 LYS A 174 LYS A 190 1 17
HELIX 17 AB8 SER A 198 GLY A 215 1 18
HELIX 18 AB9 SER A 237 GLU A 250 1 14
HELIX 19 AC1 LEU B 18 GLN B 30 1 13
HELIX 20 AC2 SER B 58 LEU B 61 5 4
HELIX 21 AC3 MET B 78 SER B 96 1 19
HELIX 22 AC4 TYR B 97 GLY B 102 1 6
HELIX 23 AC5 PRO B 106 ALA B 121 1 16
HELIX 24 AC6 GLY B 167 TRP B 179 1 13
HELIX 25 AC7 GLU B 184 SER B 199 1 16
HELIX 26 AC8 ASN B 218 LEU B 222 5 5
HELIX 27 AC9 THR B 239 LEU B 247 1 9
HELIX 28 AD1 LEU C 19 HIS C 31 1 13
HELIX 29 AD2 LEU C 80 ASN C 103 1 24
HELIX 30 AD3 PRO C 107 TYR C 122 1 16
HELIX 31 AD4 ASN C 168 TYR C 180 1 13
HELIX 32 AD5 LYS C 185 THR C 201 1 17
HELIX 33 AD6 THR C 207 ASP C 209 5 3
HELIX 34 AD7 LYS C 231 LYS C 241 1 11
HELIX 35 AD8 ILE D 17 GLY D 30 1 14
HELIX 36 AD9 LEU D 78 GLU D 101 1 24
HELIX 37 AE1 THR D 105 TYR D 120 1 16
HELIX 38 AE2 ASN D 167 TYR D 179 1 13
HELIX 39 AE3 THR D 187 GLU D 201 1 15
HELIX 40 AE4 SER D 225 GLN D 241 1 17
HELIX 41 AE5 LEU E 21 LEU E 33 1 13
HELIX 42 AE6 SER E 61 ILE E 64 5 4
HELIX 43 AE7 THR E 82 ASP E 84 5 3
HELIX 44 AE8 ALA E 85 ASP E 104 1 20
HELIX 45 AE9 ASN E 108 ASP E 118 1 11
HELIX 46 AF1 GLY E 175 TRP E 187 1 13
HELIX 47 AF2 THR E 192 MET E 208 1 17
HELIX 48 AF3 ASP E 232 ALA E 248 1 17
HELIX 49 AF4 LEU F 19 GLN F 31 1 13
HELIX 50 AF5 LEU F 77 ASN F 100 1 24
HELIX 51 AF6 ALA F 104 THR F 120 1 17
HELIX 52 AF7 ARG F 164 ILE F 180 1 17
HELIX 53 AF8 ASN F 185 GLN F 199 1 15
HELIX 54 AF9 GLY F 227 LYS F 232 1 6
HELIX 55 AG1 ASN G 20 ASN G 32 1 13
HELIX 56 AG2 LEU G 80 LYS G 103 1 24
HELIX 57 AG3 PRO G 107 ALA G 121 1 15
HELIX 58 AG4 HIS G 122 LEU G 124 5 3
HELIX 59 AG5 GLY G 167 HIS G 181 1 15
HELIX 60 AG6 SER G 187 HIS G 203 1 17
HELIX 61 AG7 GLU G 204 ASN G 206 5 3
HELIX 62 AG8 GLY G 232 ASN G 247 1 16
HELIX 63 AG9 SER H 48 GLY H 71 1 24
HELIX 64 AH1 SER H 74 ASN H 89 1 16
HELIX 65 AH2 LYS H 90 LEU H 93 5 4
HELIX 66 AH3 GLY H 128 PHE H 133 5 6
HELIX 67 AH4 ILE H 134 PHE H 142 1 9
HELIX 68 AH5 SER H 147 ASP H 166 1 20
HELIX 69 AH6 TYR H 189 GLU H 194 1 6
HELIX 70 AH7 THR I 48 SER I 71 1 24
HELIX 71 AH8 ARG I 75 TYR I 90 1 16
HELIX 72 AH9 GLY I 130 TRP I 142 1 13
HELIX 73 AI1 THR I 147 ASP I 166 1 20
HELIX 74 AI2 ASP J -6 ILE J -2 5 5
HELIX 75 AI3 LEU J 47 GLU J 70 1 24
HELIX 76 AI4 GLU J 74 GLU J 88 1 15
HELIX 77 AI5 ALA J 133 TYR J 145 1 13
HELIX 78 AI6 GLU J 150 ASP J 167 1 18
HELIX 79 AI7 GLY K 50 ASP K 71 1 22
HELIX 80 AI8 SER K 75 ARG K 92 1 18
HELIX 81 AI9 TYR K 134 TYR K 147 1 14
HELIX 82 AJ1 THR K 152 MET K 171 1 20
HELIX 83 AJ2 GLY L 48 LYS L 71 1 24
HELIX 84 AJ3 SER L 75 TYR L 90 1 16
HELIX 85 AJ4 GLY L 132 TYR L 144 1 13
HELIX 86 AJ5 SER L 149 ASP L 168 1 20
HELIX 87 AJ6 VAL L 193 GLY L 205 1 13
HELIX 88 AJ7 PHE M 48 HIS M 70 1 23
HELIX 89 AJ8 SER M 76 LYS M 91 1 16
HELIX 90 AJ9 ALA M 133 VAL M 145 1 13
HELIX 91 AK1 SER M 167 HIS M 186 1 20
HELIX 92 AK2 ILE N 49 TYR N 68 1 20
HELIX 93 AK3 GLU N 80 SER N 97 1 18
HELIX 94 AK4 GLY N 137 ARG N 148 1 12
HELIX 95 AK5 ARG N 153 ILE N 157 5 5
HELIX 96 AK6 THR N 161 ASP N 180 1 20
HELIX 97 AK7 TRP N 211 ILE N 217 5 7
HELIX 98 AK8 LEU O 25 THR O 35 1 11
HELIX 99 AK9 ASP O 65 VAL O 69 5 5
HELIX 100 AL1 PRO O 86 GLY O 109 1 24
HELIX 101 AL2 PRO O 113 ARG O 131 1 19
HELIX 102 AL3 LYS O 174 LYS O 190 1 17
HELIX 103 AL4 SER O 198 GLY O 215 1 18
HELIX 104 AL5 SER O 237 GLU O 250 1 14
HELIX 105 AL6 LEU P 18 GLN P 30 1 13
HELIX 106 AL7 SER P 58 LEU P 61 5 4
HELIX 107 AL8 MET P 78 SER P 96 1 19
HELIX 108 AL9 TYR P 97 GLY P 102 1 6
HELIX 109 AM1 PRO P 106 ALA P 121 1 16
HELIX 110 AM2 GLY P 167 TRP P 179 1 13
HELIX 111 AM3 GLU P 184 SER P 199 1 16
HELIX 112 AM4 ASN P 218 LEU P 222 5 5
HELIX 113 AM5 THR P 239 GLU P 248 1 10
HELIX 114 AM6 SER Q 3 ASP Q 7 5 5
HELIX 115 AM7 LEU Q 19 HIS Q 31 1 13
HELIX 116 AM8 LEU Q 80 ASN Q 103 1 24
HELIX 117 AM9 PRO Q 107 TYR Q 122 1 16
HELIX 118 AN1 ASN Q 168 TYR Q 180 1 13
HELIX 119 AN2 LYS Q 185 THR Q 201 1 17
HELIX 120 AN3 THR Q 207 ASP Q 209 5 3
HELIX 121 AN4 LYS Q 231 LYS Q 241 1 11
HELIX 122 AN5 ILE R 17 GLY R 30 1 14
HELIX 123 AN6 LEU R 78 GLU R 101 1 24
HELIX 124 AN7 THR R 105 TYR R 120 1 16
HELIX 125 AN8 ASN R 167 TYR R 179 1 13
HELIX 126 AN9 THR R 187 GLU R 201 1 15
HELIX 127 AO1 SER R 225 GLU R 237 1 13
HELIX 128 AO2 LEU S 21 LEU S 33 1 13
HELIX 129 AO3 GLU S 60 ILE S 64 5 5
HELIX 130 AO4 THR S 82 ASP S 84 5 3
HELIX 131 AO5 ALA S 85 ASP S 104 1 20
HELIX 132 AO6 ASN S 108 ASP S 118 1 11
HELIX 133 AO7 GLY S 175 TRP S 187 1 13
HELIX 134 AO8 THR S 192 MET S 208 1 17
HELIX 135 AO9 ASP S 232 GLU S 245 1 14
HELIX 136 AP1 LEU T 19 GLN T 31 1 13
HELIX 137 AP2 LEU T 77 ASN T 100 1 24
HELIX 138 AP3 ALA T 104 THR T 120 1 17
HELIX 139 AP4 ARG T 164 ILE T 180 1 17
HELIX 140 AP5 ASN T 185 GLN T 199 1 15
HELIX 141 AP6 GLY T 227 LYS T 232 1 6
HELIX 142 AP7 ASN U 20 ASN U 32 1 13
HELIX 143 AP8 LEU U 80 LYS U 103 1 24
HELIX 144 AP9 PRO U 107 HIS U 122 1 16
HELIX 145 AQ1 GLY U 167 HIS U 181 1 15
HELIX 146 AQ2 SER U 187 HIS U 203 1 17
HELIX 147 AQ3 GLU U 204 LYS U 207 5 4
HELIX 148 AQ4 GLY U 232 ASN U 247 1 16
HELIX 149 AQ5 SER V 48 GLY V 71 1 24
HELIX 150 AQ6 SER V 74 ASN V 89 1 16
HELIX 151 AQ7 LYS V 90 LEU V 93 5 4
HELIX 152 AQ8 GLY V 128 PHE V 133 5 6
HELIX 153 AQ9 ILE V 134 PHE V 142 1 9
HELIX 154 AR1 SER V 147 ASP V 166 1 20
HELIX 155 AR2 TYR V 189 GLU V 194 1 6
HELIX 156 AR3 THR W 48 SER W 71 1 24
HELIX 157 AR4 ARG W 75 TYR W 90 1 16
HELIX 158 AR5 GLY W 130 TRP W 142 1 13
HELIX 159 AR6 THR W 147 ASP W 166 1 20
HELIX 160 AR7 ASP X -6 ILE X -2 5 5
HELIX 161 AR8 LEU X 47 GLU X 70 1 24
HELIX 162 AR9 GLU X 74 GLU X 88 1 15
HELIX 163 AS1 ALA X 133 TYR X 145 1 13
HELIX 164 AS2 GLU X 150 ARG X 168 1 19
HELIX 165 AS3 GLY Y 50 ASP Y 71 1 22
HELIX 166 AS4 SER Y 75 ARG Y 92 1 18
HELIX 167 AS5 TYR Y 134 TYR Y 147 1 14
HELIX 168 AS6 THR Y 152 MET Y 171 1 20
HELIX 169 AS7 GLY Z 48 LYS Z 71 1 24
HELIX 170 AS8 SER Z 75 TYR Z 90 1 16
HELIX 171 AS9 GLY Z 132 TYR Z 144 1 13
HELIX 172 AT1 SER Z 149 ASP Z 168 1 20
HELIX 173 AT2 VAL Z 193 GLY Z 205 1 13
SHEET 1 AA1 5 CYS 1 127 GLY 1 131 0
SHEET 2 AA1 5 THR 1 2 ALA 1 7 -1 N ILE 1 3 O GLY 1 130
SHEET 3 AA1 5 PHE 1 11 ASP 1 17 -1 O ALA 1 15 N LEU 1 4
SHEET 4 AA1 5 GLY 1 192 THR 1 199 -1 O VAL 1 198 N ALA 1 12
SHEET 5 AA1 5 GLY 1 202 GLU 1 209 -1 O GLU 1 206 N ILE 1 195
SHEET 1 AA2 2 ASN 1 20 THR 1 22 0
SHEET 2 AA2 2 SER 1 25 SER 1 28 -1 O ASN 1 27 N ASN 1 20
SHEET 1 AA3 5 VAL 1 34 ASP 1 36 0
SHEET 2 AA3 5 ILE 1 41 GLY 1 47 -1 O MET 1 43 N PHE 1 35
SHEET 3 AA3 5 VAL 1 98 LEU 1 105 -1 O HIS 1 99 N ASN 1 46
SHEET 4 AA3 5 GLY 1 111 PHE 1 116 -1 O PHE 1 116 N THR 1 100
SHEET 5 AA3 5 TYR 1 122 GLU 1 125 -1 O GLU 1 125 N VAL 1 113
SHEET 1 AA4 5 LEU 2 25 PHE 2 28 0
SHEET 2 AA4 5 GLY 2 20 TYR 2 22 -1 N GLY 2 20 O PHE 2 28
SHEET 3 AA4 5 VAL 2 -2 GLY 2 0 -1 N THR 2 -1 O SER 2 21
SHEET 4 AA4 5 THR 2 41 ASP 2 48 -1 O GLY 2 47 N GLY 2 0
SHEET 5 AA4 5 LEU 2 34 PRO 2 36 -1 N ILE 2 35 O VAL 2 43
SHEET 1 AA5 7 LEU 2 25 PHE 2 28 0
SHEET 2 AA5 7 GLY 2 20 TYR 2 22 -1 N GLY 2 20 O PHE 2 28
SHEET 3 AA5 7 VAL 2 -2 GLY 2 0 -1 N THR 2 -1 O SER 2 21
SHEET 4 AA5 7 THR 2 41 ASP 2 48 -1 O GLY 2 47 N GLY 2 0
SHEET 5 AA5 7 ASN 2 104 VAL 2 111 -1 O ILE 2 107 N GLY 2 44
SHEET 6 AA5 7 GLN 2 117 ASN 2 123 -1 O PHE 2 118 N GLY 2 110
SHEET 7 AA5 7 THR 2 128 TYR 2 129 -1 O TYR 2 129 N TYR 2 121
SHEET 1 AA6 5 THR 2 133 ALA 2 135 0
SHEET 2 AA6 5 VAL 2 3 LYS 2 7 -1 N SER 2 5 O LEU 2 134
SHEET 3 AA6 5 GLY 2 11 ASP 2 17 -1 O ALA 2 15 N ILE 2 4
SHEET 4 AA6 5 ASN 2 186 ASP 2 193 -1 O ALA 2 190 N ILE 2 14
SHEET 5 AA6 5 GLY 2 197 GLN 2 205 -1 O THR 2 199 N ILE 2 191
SHEET 1 AA7 5 ALA A 168 THR A 171 0
SHEET 2 AA7 5 SER A 42 ARG A 46 -1 N SER A 42 O THR A 171
SHEET 3 AA7 5 CYS A 50 GLN A 56 -1 O ILE A 54 N LEU A 43
SHEET 4 AA7 5 LEU A 223 THR A 229 -1 O ALA A 228 N THR A 51
SHEET 5 AA7 5 LYS A 232 THR A 235 -1 O PHE A 234 N VAL A 227
SHEET 1 AA8 6 ILE A 72 CYS A 74 0
SHEET 2 AA8 6 GLY A 80 ASN A 84 -1 O MET A 81 N PHE A 73
SHEET 3 AA8 6 ILE A 140 ASP A 147 -1 O THR A 142 N VAL A 82
SHEET 4 AA8 6 GLY A 151 THR A 157 -1 O TYR A 155 N PHE A 143
SHEET 5 AA8 6 TYR A 163 TYR A 166 -1 O TYR A 166 N ILE A 154
SHEET 6 AA8 6 ALA B 56 MET B 57 -1 O MET B 57 N GLY A 165
SHEET 1 AA9 5 ALA B 161 ILE B 164 0
SHEET 2 AA9 5 SER B 34 LYS B 38 -1 N SER B 34 O ILE B 164
SHEET 3 AA9 5 VAL B 43 GLU B 48 -1 O ALA B 46 N LEU B 35
SHEET 4 AA9 5 ILE B 209 ILE B 214 -1 O ILE B 214 N VAL B 43
SHEET 5 AA9 5 PHE B 235 LYS B 237 -1 O ARG B 236 N ILE B 213
SHEET 1 AB1 5 SER B 65 THR B 68 0
SHEET 2 AB1 5 ILE B 71 GLY B 77 -1 O ILE B 71 N LEU B 67
SHEET 3 AB1 5 VAL B 132 ASP B 140 -1 O ALA B 137 N GLY B 72
SHEET 4 AB1 5 GLY B 144 VAL B 150 -1 O SER B 146 N GLY B 138
SHEET 5 AB1 5 TYR B 156 PRO B 158 -1 O PHE B 157 N GLN B 149
SHEET 1 AB2 6 TYR B 224 THR B 225 0
SHEET 2 AB2 6 ALA I 184 LEU I 191 1 O TYR I 186 N THR B 225
SHEET 3 AB2 6 VAL I 173 GLU I 179 -1 N VAL I 177 O GLU I 185
SHEET 4 AB2 6 GLY I 11 ALA I 16 -1 N VAL I 12 O MET I 178
SHEET 5 AB2 6 ILE I 3 PHE I 8 -1 N VAL I 6 O VAL I 13
SHEET 6 AB2 6 TYR I 124 LEU I 127 -1 O LEU I 127 N ILE I 3
SHEET 1 AB3 5 ALA C 162 VAL C 165 0
SHEET 2 AB3 5 ALA C 35 ALA C 40 -1 N GLY C 37 O ILE C 163
SHEET 3 AB3 5 GLY C 43 GLU C 49 -1 O ALA C 47 N ILE C 36
SHEET 4 AB3 5 LEU C 211 ARG C 217 -1 O ALA C 214 N LEU C 46
SHEET 5 AB3 5 TYR C 226 ILE C 229 -1 O LYS C 228 N THR C 215
SHEET 1 AB4 5 LEU C 66 LYS C 68 0
SHEET 2 AB4 5 ILE C 73 GLY C 79 -1 O VAL C 75 N TYR C 67
SHEET 3 AB4 5 VAL C 133 ASP C 141 -1 O ALA C 138 N ALA C 74
SHEET 4 AB4 5 GLY C 145 SER C 151 -1 O GLN C 147 N GLY C 139
SHEET 5 AB4 5 TYR C 157 GLY C 159 -1 O THR C 158 N THR C 150
SHEET 1 AB5 5 ALA D 161 ILE D 164 0
SHEET 2 AB5 5 ALA D 33 LYS D 37 -1 N GLY D 35 O GLN D 162
SHEET 3 AB5 5 VAL D 42 GLU D 47 -1 O GLY D 45 N VAL D 34
SHEET 4 AB5 5 ILE D 210 LYS D 216 -1 O THR D 213 N LEU D 44
SHEET 5 AB5 5 ASP D 220 ALA D 223 -1 O VAL D 222 N VAL D 214
SHEET 1 AB6 6 VAL D 64 ASP D 68 0
SHEET 2 AB6 6 VAL D 71 GLY D 77 -1 O VAL D 71 N ILE D 67
SHEET 3 AB6 6 VAL D 131 PHE D 138 -1 O LEU D 134 N SER D 74
SHEET 4 AB6 6 PRO D 145 THR D 150 -1 O TYR D 148 N ILE D 135
SHEET 5 AB6 6 TYR D 156 TRP D 159 -1 O SER D 157 N GLN D 149
SHEET 6 AB6 6 LEU E 59 GLU E 60 -1 O GLU E 60 N SER D 158
SHEET 1 AB7 5 ALA E 169 ILE E 172 0
SHEET 2 AB7 5 ALA E 37 ALA E 41 -1 N GLY E 39 O LYS E 170
SHEET 3 AB7 5 VAL E 46 GLU E 51 -1 O VAL E 47 N ILE E 40
SHEET 4 AB7 5 ALA E 217 THR E 223 -1 O SER E 220 N LEU E 48
SHEET 5 AB7 5 GLY E 227 ILE E 230 -1 O GLY E 227 N THR E 223
SHEET 1 AB8 5 ILE E 67 ASP E 71 0
SHEET 2 AB8 5 ILE E 74 GLY E 80 -1 O ILE E 74 N ILE E 70
SHEET 3 AB8 5 VAL E 140 ASP E 148 -1 O ALA E 145 N GLY E 75
SHEET 4 AB8 5 GLY E 152 ALA E 158 -1 O ALA E 158 N LEU E 142
SHEET 5 AB8 5 PHE E 164 ARG E 166 -1 O TYR E 165 N HIS E 157
SHEET 1 AB9 5 GLY F 158 ILE F 161 0
SHEET 2 AB9 5 THR F 35 ARG F 39 -1 N GLY F 37 O THR F 159
SHEET 3 AB9 5 HIS F 43 LEU F 49 -1 O VAL F 47 N VAL F 36
SHEET 4 AB9 5 LEU F 211 GLY F 217 -1 O SER F 212 N ALA F 48
SHEET 5 AB9 5 THR F 220 ASP F 226 -1 O TYR F 225 N ILE F 213
SHEET 1 AC1 5 ILE F 63 ASP F 67 0
SHEET 2 AC1 5 MET F 70 GLY F 76 -1 O LEU F 72 N ILE F 64
SHEET 3 AC1 5 VAL F 130 ASP F 138 -1 O LEU F 133 N SER F 73
SHEET 4 AC1 5 GLY F 141 PHE F 147 -1 O PHE F 147 N LEU F 132
SHEET 5 AC1 5 VAL F 153 LEU F 156 -1 O LEU F 156 N LEU F 144
SHEET 1 AC2 5 GLY G 161 THR G 164 0
SHEET 2 AC2 5 SER G 36 LYS G 40 -1 N GLY G 38 O ALA G 162
SHEET 3 AC2 5 GLY G 44 ILE G 53 -1 O ALA G 48 N ILE G 37
SHEET 4 AC2 5 ASP G 210 SER G 219 -1 O ASP G 210 N ILE G 53
SHEET 5 AC2 5 HIS G 227 PHE G 229 -1 O LYS G 228 N TRP G 217
SHEET 1 AC3 5 GLN G 67 VAL G 69 0
SHEET 2 AC3 5 ILE G 73 GLY G 79 -1 O ILE G 73 N VAL G 69
SHEET 3 AC3 5 VAL G 133 ASP G 141 -1 O ILE G 136 N VAL G 76
SHEET 4 AC3 5 GLY G 144 LEU G 150 -1 O TYR G 148 N PHE G 137
SHEET 5 AC3 5 TYR G 156 GLY G 158 -1 O TRP G 157 N MET G 149
SHEET 1 AC4 5 TYR H 124 ALA H 127 0
SHEET 2 AC4 5 ILE H 3 PHE H 8 -1 N ILE H 3 O ALA H 127
SHEET 3 AC4 5 GLY H 11 ALA H 16 -1 O ILE H 13 N VAL H 6
SHEET 4 AC4 5 ILE H 173 THR H 179 -1 O LEU H 178 N VAL H 12
SHEET 5 AC4 5 GLY H 182 PHE H 188 -1 O GLU H 184 N VAL H 177
SHEET 1 AC5 2 THR H 20 THR H 22 0
SHEET 2 AC5 2 TYR H 25 ASN H 28 -1 O TYR H 25 N THR H 22
SHEET 1 AC6 5 LEU H 34 HIS H 38 0
SHEET 2 AC6 5 ILE H 41 GLY H 47 -1 O ILE H 41 N VAL H 37
SHEET 3 AC6 5 ALA H 95 ASP H 103 -1 O ALA H 100 N TRP H 42
SHEET 4 AC6 5 LYS H 107 ILE H 113 -1 O ILE H 113 N ILE H 97
SHEET 5 AC6 5 HIS H 120 LEU H 122 -1 O HIS H 120 N THR H 112
SHEET 1 AC7 2 SER I 20 GLN I 22 0
SHEET 2 AC7 2 ILE I 25 ASP I 28 -1 O ILE I 25 N GLN I 22
SHEET 1 AC8 5 LEU I 34 SER I 38 0
SHEET 2 AC8 5 ILE I 41 GLY I 47 -1 O CYS I 43 N HIS I 35
SHEET 3 AC8 5 ALA I 96 ASP I 104 -1 O ILE I 99 N ALA I 44
SHEET 4 AC8 5 GLY I 107 ILE I 113 -1 O HIS I 109 N GLY I 102
SHEET 5 AC8 5 THR I 119 VAL I 121 -1 O ASP I 120 N SER I 112
SHEET 1 AC9 6 VAL I 212 ILE I 217 0
SHEET 2 AC9 6 VAL J 186 LEU J 191 -1 O TYR J 190 N LEU I 213
SHEET 3 AC9 6 ALA J 176 LYS J 182 -1 N VAL J 178 O ARG J 189
SHEET 4 AC9 6 CYS J 11 ASP J 17 -1 N ILE J 14 O TYR J 179
SHEET 5 AC9 6 ILE J 2 GLY J 8 -1 N MET J 6 O ALA J 13
SHEET 6 AC9 6 PHE J 127 GLY J 131 -1 O ILE J 128 N ALA J 5
SHEET 1 AD1 2 LEU J 20 SER J 22 0
SHEET 2 AD1 2 LEU J 25 SER J 28 -1 O SER J 28 N LEU J 20
SHEET 1 AD2 5 ILE J 34 TYR J 37 0
SHEET 2 AD2 5 VAL J 40 GLY J 46 -1 O LEU J 42 N PHE J 35
SHEET 3 AD2 5 VAL J 96 ILE J 103 -1 O ALA J 101 N PHE J 41
SHEET 4 AD2 5 PRO J 110 PHE J 115 -1 O ALA J 113 N VAL J 100
SHEET 5 AD2 5 ILE J 121 GLU J 123 -1 O ASP J 122 N GLY J 114
SHEET 1 AD3 5 TYR K 129 ALA K 131 0
SHEET 2 AD3 5 ILE K 3 ARG K 7 -1 N GLY K 5 O GLY K 130
SHEET 3 AD3 5 SER K 11 SER K 17 -1 O ILE K 13 N ILE K 6
SHEET 4 AD3 5 VAL K 178 ASP K 184 -1 O LYS K 181 N LEU K 14
SHEET 5 AD3 5 GLY K 187 GLN K 190 -1 O ARG K 189 N ILE K 182
SHEET 1 AD4 2 ALA K 19 ARG K 22 0
SHEET 2 AD4 2 SER K 25 ASP K 29 -1 O LYS K 28 N VAL K 20
SHEET 1 AD5 5 THR K 34 SER K 38 0
SHEET 2 AD5 5 THR K 41 GLY K 47 -1 O THR K 41 N SER K 38
SHEET 3 AD5 5 VAL K 99 TYR K 106 -1 O GLY K 104 N LEU K 42
SHEET 4 AD5 5 PRO K 113 ILE K 118 -1 O GLU K 114 N GLY K 105
SHEET 5 AD5 5 LYS K 124 GLU K 126 -1 O VAL K 125 N GLN K 117
SHEET 1 AD6 5 ILE L 126 VAL L 129 0
SHEET 2 AD6 5 THR L 3 PHE L 8 -1 N THR L 3 O VAL L 129
SHEET 3 AD6 5 GLY L 11 VAL L 16 -1 O ILE L 13 N PHE L 6
SHEET 4 AD6 5 SER L 174 THR L 181 -1 O VAL L 180 N ILE L 12
SHEET 5 AD6 5 GLY L 184 ASP L 192 -1 O ILE L 186 N HIS L 179
SHEET 1 AD7 2 ALA L 20 ALA L 22 0
SHEET 2 AD7 2 TRP L 25 SER L 28 -1 O TRP L 25 N ALA L 22
SHEET 1 AD8 5 VAL L 34 ASN L 38 0
SHEET 2 AD8 5 LEU L 41 THR L 44 -1 O GLY L 43 N ILE L 35
SHEET 3 AD8 5 GLY L 98 THR L 105 -1 O CYS L 102 N LEU L 42
SHEET 4 AD8 5 GLY L 109 ASP L 116 -1 O TYR L 113 N ILE L 101
SHEET 5 AD8 5 ARG L 121 GLY L 124 -1 O LEU L 122 N TYR L 114
SHEET 1 AD9 5 CYS M 127 GLY M 131 0
SHEET 2 AD9 5 THR M 2 ALA M 7 -1 N ILE M 3 O GLY M 130
SHEET 3 AD9 5 PHE M 11 ASP M 17 -1 O ALA M 15 N LEU M 4
SHEET 4 AD9 5 GLY M 192 THR M 199 -1 O VAL M 198 N ALA M 12
SHEET 5 AD9 5 GLY M 202 GLU M 209 -1 O ARG M 204 N ILE M 197
SHEET 1 AE1 2 ASN M 20 THR M 22 0
SHEET 2 AE1 2 SER M 25 SER M 28 -1 O ASN M 27 N ASN M 20
SHEET 1 AE2 5 VAL M 34 ASP M 36 0
SHEET 2 AE2 5 ILE M 41 GLY M 47 -1 O MET M 43 N PHE M 35
SHEET 3 AE2 5 VAL M 98 LEU M 105 -1 O HIS M 99 N ASN M 46
SHEET 4 AE2 5 GLY M 111 PHE M 116 -1 O ALA M 112 N GLY M 104
SHEET 5 AE2 5 TYR M 122 GLU M 125 -1 O GLU M 125 N VAL M 113
SHEET 1 AE3 5 LEU N 25 PHE N 28 0
SHEET 2 AE3 5 GLY N 20 TYR N 22 -1 N TYR N 22 O LEU N 25
SHEET 3 AE3 5 VAL N -2 GLY N 0 -1 N THR N -1 O SER N 21
SHEET 4 AE3 5 THR N 41 ASP N 48 -1 O GLY N 47 N GLY N 0
SHEET 5 AE3 5 LEU N 34 PRO N 36 -1 N ILE N 35 O VAL N 43
SHEET 1 AE4 7 LEU N 25 PHE N 28 0
SHEET 2 AE4 7 GLY N 20 TYR N 22 -1 N TYR N 22 O LEU N 25
SHEET 3 AE4 7 VAL N -2 GLY N 0 -1 N THR N -1 O SER N 21
SHEET 4 AE4 7 THR N 41 ASP N 48 -1 O GLY N 47 N GLY N 0
SHEET 5 AE4 7 ASN N 104 VAL N 111 -1 O ILE N 107 N GLY N 44
SHEET 6 AE4 7 GLN N 117 ASN N 123 -1 O VAL N 122 N ILE N 106
SHEET 7 AE4 7 THR N 128 TYR N 129 -1 O TYR N 129 N TYR N 121
SHEET 1 AE5 5 THR N 133 ALA N 135 0
SHEET 2 AE5 5 VAL N 3 LYS N 7 -1 N SER N 5 O LEU N 134
SHEET 3 AE5 5 GLY N 11 ASP N 17 -1 O ALA N 15 N ILE N 4
SHEET 4 AE5 5 ASN N 186 ASP N 193 -1 O ALA N 190 N ILE N 14
SHEET 5 AE5 5 GLY N 197 GLN N 205 -1 O THR N 199 N ILE N 191
SHEET 1 AE6 5 ALA O 168 THR O 171 0
SHEET 2 AE6 5 SER O 42 ARG O 46 -1 N SER O 42 O THR O 171
SHEET 3 AE6 5 CYS O 50 GLN O 56 -1 O ILE O 54 N LEU O 43
SHEET 4 AE6 5 LEU O 223 THR O 229 -1 O ALA O 228 N THR O 51
SHEET 5 AE6 5 PHE O 233 THR O 235 -1 O PHE O 234 N VAL O 227
SHEET 1 AE7 6 ILE O 72 CYS O 74 0
SHEET 2 AE7 6 GLY O 80 ASN O 84 -1 O MET O 81 N PHE O 73
SHEET 3 AE7 6 ILE O 140 ASP O 147 -1 O THR O 142 N VAL O 82
SHEET 4 AE7 6 GLY O 151 THR O 157 -1 O TYR O 155 N PHE O 143
SHEET 5 AE7 6 TYR O 163 TYR O 166 -1 O TYR O 166 N ILE O 154
SHEET 6 AE7 6 ALA P 56 MET P 57 -1 O MET P 57 N GLY O 165
SHEET 1 AE8 5 ALA P 161 ILE P 164 0
SHEET 2 AE8 5 SER P 34 LYS P 38 -1 N SER P 34 O ILE P 164
SHEET 3 AE8 5 VAL P 43 GLU P 48 -1 O VAL P 44 N ILE P 37
SHEET 4 AE8 5 ILE P 209 ILE P 214 -1 O ILE P 214 N VAL P 43
SHEET 5 AE8 5 PHE P 235 LYS P 237 -1 O ARG P 236 N ILE P 213
SHEET 1 AE9 5 SER P 65 THR P 68 0
SHEET 2 AE9 5 ILE P 71 GLY P 77 -1 O ILE P 71 N LEU P 67
SHEET 3 AE9 5 VAL P 132 ASP P 140 -1 O ALA P 137 N GLY P 72
SHEET 4 AE9 5 GLY P 144 VAL P 150 -1 O VAL P 150 N LEU P 134
SHEET 5 AE9 5 TYR P 156 PRO P 158 -1 O PHE P 157 N GLN P 149
SHEET 1 AF1 6 TYR P 224 THR P 225 0
SHEET 2 AF1 6 ALA W 184 LEU W 191 1 O TYR W 186 N THR P 225
SHEET 3 AF1 6 VAL W 173 GLU W 179 -1 N VAL W 177 O GLU W 185
SHEET 4 AF1 6 GLY W 11 ALA W 16 -1 N VAL W 12 O MET W 178
SHEET 5 AF1 6 ILE W 3 PHE W 8 -1 N VAL W 6 O VAL W 13
SHEET 6 AF1 6 TYR W 124 LEU W 127 -1 O LEU W 127 N ILE W 3
SHEET 1 AF2 5 ALA Q 162 VAL Q 165 0
SHEET 2 AF2 5 ALA Q 35 ALA Q 40 -1 N GLY Q 37 O ILE Q 163
SHEET 3 AF2 5 GLY Q 43 GLU Q 49 -1 O ALA Q 47 N ILE Q 36
SHEET 4 AF2 5 LEU Q 211 LYS Q 218 -1 O ALA Q 214 N LEU Q 46
SHEET 5 AF2 5 VAL Q 225 ILE Q 229 -1 O LYS Q 228 N THR Q 215
SHEET 1 AF3 5 LEU Q 66 LYS Q 68 0
SHEET 2 AF3 5 ILE Q 73 GLY Q 79 -1 O VAL Q 75 N TYR Q 67
SHEET 3 AF3 5 VAL Q 133 ASP Q 141 -1 O ALA Q 138 N ALA Q 74
SHEET 4 AF3 5 GLY Q 145 SER Q 151 -1 O GLN Q 147 N GLY Q 139
SHEET 5 AF3 5 TYR Q 157 GLY Q 159 -1 O THR Q 158 N THR Q 150
SHEET 1 AF4 5 ALA R 161 ILE R 164 0
SHEET 2 AF4 5 ALA R 33 LYS R 37 -1 N GLY R 35 O GLN R 162
SHEET 3 AF4 5 VAL R 42 GLU R 47 -1 O GLY R 45 N VAL R 34
SHEET 4 AF4 5 ILE R 210 LYS R 216 -1 O THR R 213 N LEU R 44
SHEET 5 AF4 5 ASP R 220 ALA R 223 -1 O VAL R 222 N VAL R 214
SHEET 1 AF5 5 VAL R 64 ASP R 68 0
SHEET 2 AF5 5 VAL R 71 GLY R 77 -1 O VAL R 71 N ILE R 67
SHEET 3 AF5 5 VAL R 131 PHE R 138 -1 O LEU R 134 N SER R 74
SHEET 4 AF5 5 PRO R 145 THR R 150 -1 O TYR R 148 N ILE R 135
SHEET 5 AF5 5 TYR R 156 SER R 158 -1 O SER R 157 N GLN R 149
SHEET 1 AF6 5 ALA S 169 ILE S 172 0
SHEET 2 AF6 5 ALA S 37 ALA S 41 -1 N GLY S 39 O LYS S 170
SHEET 3 AF6 5 VAL S 46 GLU S 51 -1 O VAL S 47 N ILE S 40
SHEET 4 AF6 5 ALA S 217 THR S 223 -1 O SER S 220 N LEU S 48
SHEET 5 AF6 5 GLY S 227 ILE S 230 -1 O GLY S 227 N THR S 223
SHEET 1 AF7 5 ILE S 67 ASP S 71 0
SHEET 2 AF7 5 ILE S 74 GLY S 80 -1 O ILE S 74 N ILE S 70
SHEET 3 AF7 5 VAL S 140 ASP S 148 -1 O ALA S 145 N GLY S 75
SHEET 4 AF7 5 GLY S 152 ALA S 158 -1 O ALA S 158 N LEU S 142
SHEET 5 AF7 5 PHE S 164 ARG S 166 -1 O TYR S 165 N HIS S 157
SHEET 1 AF8 5 GLY T 158 ILE T 161 0
SHEET 2 AF8 5 THR T 35 ARG T 39 -1 N GLY T 37 O THR T 159
SHEET 3 AF8 5 HIS T 43 LEU T 49 -1 O VAL T 47 N VAL T 36
SHEET 4 AF8 5 LEU T 211 GLY T 217 -1 O SER T 212 N ALA T 48
SHEET 5 AF8 5 THR T 220 ASP T 226 -1 O TYR T 225 N ILE T 213
SHEET 1 AF9 5 ILE T 63 ASP T 67 0
SHEET 2 AF9 5 MET T 70 GLY T 76 -1 O LEU T 72 N ILE T 64
SHEET 3 AF9 5 VAL T 130 ASP T 138 -1 O ILE T 135 N GLY T 71
SHEET 4 AF9 5 GLY T 141 PHE T 147 -1 O PHE T 147 N LEU T 132
SHEET 5 AF9 5 VAL T 153 LEU T 156 -1 O LEU T 156 N LEU T 144
SHEET 1 AG1 5 GLY U 161 THR U 164 0
SHEET 2 AG1 5 SER U 36 LYS U 40 -1 N GLY U 38 O ALA U 162
SHEET 3 AG1 5 GLY U 44 ILE U 53 -1 O ALA U 48 N ILE U 37
SHEET 4 AG1 5 ASP U 210 SER U 219 -1 O ASP U 210 N ILE U 53
SHEET 5 AG1 5 HIS U 227 PHE U 229 -1 O LYS U 228 N TRP U 217
SHEET 1 AG2 5 GLN U 67 VAL U 69 0
SHEET 2 AG2 5 ILE U 73 GLY U 79 -1 O ILE U 73 N VAL U 69
SHEET 3 AG2 5 VAL U 133 ASP U 141 -1 O ILE U 136 N VAL U 76
SHEET 4 AG2 5 GLY U 144 LEU U 150 -1 O TYR U 148 N PHE U 137
SHEET 5 AG2 5 TYR U 156 GLY U 158 -1 O TRP U 157 N MET U 149
SHEET 1 AG3 5 TYR V 124 ALA V 127 0
SHEET 2 AG3 5 ILE V 3 PHE V 8 -1 N ILE V 3 O ALA V 127
SHEET 3 AG3 5 GLY V 11 ALA V 16 -1 O ILE V 13 N VAL V 6
SHEET 4 AG3 5 ILE V 173 THR V 179 -1 O ARG V 174 N ALA V 16
SHEET 5 AG3 5 GLY V 182 PHE V 188 -1 O GLU V 184 N VAL V 177
SHEET 1 AG4 2 THR V 20 THR V 22 0
SHEET 2 AG4 2 TYR V 25 ASN V 28 -1 O TYR V 25 N THR V 22
SHEET 1 AG5 5 LEU V 34 HIS V 38 0
SHEET 2 AG5 5 ILE V 41 GLY V 47 -1 O CYS V 43 N THR V 35
SHEET 3 AG5 5 ALA V 95 ASP V 103 -1 O ALA V 100 N TRP V 42
SHEET 4 AG5 5 LYS V 107 ILE V 113 -1 O ILE V 113 N ILE V 97
SHEET 5 AG5 5 HIS V 120 LEU V 122 -1 O HIS V 120 N THR V 112
SHEET 1 AG6 2 SER W 20 GLN W 22 0
SHEET 2 AG6 2 ILE W 25 ASP W 28 -1 O ILE W 25 N GLN W 22
SHEET 1 AG7 5 LEU W 34 SER W 38 0
SHEET 2 AG7 5 ILE W 41 GLY W 47 -1 O CYS W 43 N HIS W 35
SHEET 3 AG7 5 ALA W 96 ASP W 104 -1 O ILE W 99 N ALA W 44
SHEET 4 AG7 5 GLY W 107 ILE W 113 -1 O HIS W 109 N GLY W 102
SHEET 5 AG7 5 THR W 119 VAL W 121 -1 O ASP W 120 N SER W 112
SHEET 1 AG8 6 VAL W 212 ILE W 217 0
SHEET 2 AG8 6 VAL X 186 LEU X 191 -1 O LYS X 188 N SER W 216
SHEET 3 AG8 6 ALA X 176 LYS X 182 -1 N ILE X 180 O VAL X 187
SHEET 4 AG8 6 CYS X 11 ASP X 17 -1 N ILE X 14 O TYR X 179
SHEET 5 AG8 6 ILE X 2 GLY X 8 -1 N MET X 6 O ALA X 13
SHEET 6 AG8 6 PHE X 127 GLY X 131 -1 O ILE X 128 N ALA X 5
SHEET 1 AG9 2 LEU X 20 SER X 22 0
SHEET 2 AG9 2 LEU X 25 SER X 28 -1 O SER X 28 N LEU X 20
SHEET 1 AH1 5 ILE X 34 TYR X 37 0
SHEET 2 AH1 5 VAL X 40 GLY X 46 -1 O LEU X 42 N PHE X 35
SHEET 3 AH1 5 VAL X 96 ILE X 103 -1 O ALA X 101 N PHE X 41
SHEET 4 AH1 5 PRO X 110 PHE X 115 -1 O ALA X 113 N VAL X 100
SHEET 5 AH1 5 ILE X 121 GLU X 123 -1 O ASP X 122 N GLY X 114
SHEET 1 AH2 5 TYR Y 129 HIS Y 132 0
SHEET 2 AH2 5 ILE Y 3 ARG Y 7 -1 N GLY Y 5 O GLY Y 130
SHEET 3 AH2 5 SER Y 11 SER Y 17 -1 O ILE Y 13 N ILE Y 6
SHEET 4 AH2 5 VAL Y 178 ASP Y 184 -1 O LYS Y 181 N LEU Y 14
SHEET 5 AH2 5 GLY Y 187 GLN Y 190 -1 O ARG Y 189 N ILE Y 182
SHEET 1 AH3 2 ALA Y 19 ARG Y 22 0
SHEET 2 AH3 2 SER Y 25 ASP Y 29 -1 O LYS Y 28 N VAL Y 20
SHEET 1 AH4 5 THR Y 34 SER Y 38 0
SHEET 2 AH4 5 THR Y 41 GLY Y 47 -1 O THR Y 41 N SER Y 38
SHEET 3 AH4 5 VAL Y 99 TYR Y 106 -1 O GLY Y 104 N LEU Y 42
SHEET 4 AH4 5 PRO Y 113 ILE Y 118 -1 O GLU Y 114 N GLY Y 105
SHEET 5 AH4 5 LYS Y 124 GLU Y 126 -1 O VAL Y 125 N GLN Y 117
SHEET 1 AH5 5 ILE Z 126 VAL Z 129 0
SHEET 2 AH5 5 THR Z 3 PHE Z 8 -1 N THR Z 3 O VAL Z 129
SHEET 3 AH5 5 GLY Z 11 VAL Z 16 -1 O ALA Z 15 N LEU Z 4
SHEET 4 AH5 5 SER Z 174 THR Z 181 -1 O VAL Z 180 N ILE Z 12
SHEET 5 AH5 5 GLY Z 184 ASP Z 192 -1 O ILE Z 186 N HIS Z 179
SHEET 1 AH6 2 ALA Z 20 ALA Z 22 0
SHEET 2 AH6 2 TRP Z 25 SER Z 28 -1 O TRP Z 25 N ALA Z 22
SHEET 1 AH7 5 VAL Z 34 ASN Z 38 0
SHEET 2 AH7 5 LEU Z 41 THR Z 44 -1 O GLY Z 43 N ILE Z 35
SHEET 3 AH7 5 GLY Z 98 THR Z 105 -1 O CYS Z 102 N LEU Z 42
SHEET 4 AH7 5 GLY Z 109 ASP Z 116 -1 O TYR Z 113 N ILE Z 101
SHEET 5 AH7 5 ARG Z 121 GLY Z 124 -1 O LEU Z 122 N TYR Z 114
LINK OE2 GLU J 123 MG MG J 201 1555 1555 2.81
CISPEP 1 GLY 1 0 GLY 1 1 0 -9.10
CISPEP 2 PRO 1 153 GLY 1 154 0 4.65
CISPEP 3 GLY C 219 ALA C 220 0 4.40
CISPEP 4 ALA E 127 SER E 128 0 -17.99
CISPEP 5 GLY E 129 GLU E 130 0 -0.12
CISPEP 6 SER I 169 GLY I 170 0 3.73
CISPEP 7 GLY M 0 GLY M 1 0 -9.03
CISPEP 8 TYR N 220 GLY N 221 0 13.24
CISPEP 9 ALA S 127 SER S 128 0 -20.22
CISPEP 10 GLU S 247 ALA S 248 0 -15.70
CISPEP 11 ARG T 3 ASN T 4 0 -17.90
CISPEP 12 GLN X 195 ASP X 196 0 16.52
CISPEP 13 PHE a 2 GLY a 3 0 13.05
CISPEP 14 PHE e 12 GLY e 13 0 26.35
SITE 1 AC1 1 TYR 1 -4
SITE 1 AC2 1 TYR 1 97
SITE 1 AC3 1 ARG 1 92
SITE 1 AC4 2 ARG 2 153 GLU 2 154
SITE 1 AC5 1 ASP 2 193
SITE 1 AC6 1 ILE 2 -3
SITE 1 AC7 1 ASP 2 152
SITE 1 AC8 1 GLN 2 94
SITE 1 AC9 3 ARG A 46 GLY A 47 LYS A 48
SITE 1 AD1 3 TYR A 108 HIS I 66 TYR I 69
SITE 1 AD2 4 PHE A 73 LYS A 98 ASP G 113 GLN H 69
SITE 1 AD3 4 ARG D 111 GLY D 115 HOH D 401 ARG E 86
SITE 1 AD4 3 TYR E 167 ASN E 168 SER F 58
SITE 1 AD5 2 ASN F 41 HOH F 406
SITE 1 AD6 2 ARG E 122 ASN F 86
SITE 1 AD7 4 PHE F 99 ARG F 101 ARG F 107 GLU N 65
SITE 1 AD8 1 GLU F 27
SITE 1 AD9 1 TYR G 125
SITE 1 AE1 3 GLU G 93 GLU G 94 SER G 97
SITE 1 AE2 11 THR H 1 ARG H 19 THR H 20 LYS H 33
SITE 2 AE2 11 ARG H 45 SER H 46 GLY H 47 SER H 48
SITE 3 AE2 11 ALA H 49 THR H 52 HOH H 307
SITE 1 AE3 4 THR H 22 ALA H 27 SER I 118 ASP I 120
SITE 1 AE4 1 TYR I 97
SITE 1 AE5 4 CYS I 31 ALA I 32 ILE J 121 GLU J 123
SITE 1 AE6 4 ARG B 99 GLN I 57 GLN J 80 SER J 83
SITE 1 AE7 1 PHE J 91
SITE 1 AE8 1 TYR J 94
SITE 1 AE9 4 MET K 0 GLN K 98 ASN K 100 TYR K 120
SITE 1 AF1 4 ARG K 22 GLY L 98 ASP L 116 ASP L 118
SITE 1 AF2 4 ASP L 141 LEU Y 162 GLU Y 166 LYS Y 169
SITE 1 AF3 2 ASN L 143 TYR L 155
SITE 1 AF4 1 THR L 1
SITE 1 AF5 1 GLN L 62
SITE 1 AF6 3 TYR L 90 TYR M 89 GLY M 90
SITE 1 AF7 4 ASN M 46 GLY M 47 TYR M 97 HOH M 407
SITE 1 AF8 1 TYR M 97
SITE 1 AF9 2 HOH M 405 GLU N 154
SITE 1 AG1 2 ASP N 39 GLY N 197
SITE 1 AG2 2 TYR O 108 HIS W 66
SITE 1 AG3 4 PHE O 73 LYS O 98 ASP U 113 GLN V 69
SITE 1 AG4 1 LEU P 250
SITE 1 AG5 1 GLU R 189
SITE 1 AG6 2 ASN S 168 SER T 58
SITE 1 AG7 5 HIS T 69 LYS T 102 GLY T 217 ASP T 219
SITE 2 AG7 5 PRO T 221
SITE 1 AG8 1 ASN T 93
SITE 1 AG9 5 THR V 1 GLY V 47 GLY V 128 SER V 129
SITE 2 AG9 5 MG V 206
SITE 1 AH1 2 GLN 2 -6 ASP V 91
SITE 1 AH2 6 THR V 20 THR V 31 ARG V 45 GLY V 47
SITE 2 AH2 6 ALA V 49 THR V 52
SITE 1 AH3 2 LEU V 115 MPD V 201
SITE 1 AH4 2 LEU V 93 THR V 94
SITE 1 AH5 1 GLY W 128
SITE 1 AH6 3 ALA W 54 GLN W 57 GLN X 80
SITE 1 AH7 2 LYS X 30 VAL Y 125
SITE 1 AH8 1 MET Y 173
SITE 1 AH9 6 THR Z 1 GLY Z 47 GLY Z 130 SER Z 131
SITE 2 AH9 6 GOL Z 302 HOH Z 402
SITE 1 AI1 2 ASP Z 116 MPD Z 301
SITE 1 AI2 1 TYR Z 90
SITE 1 AI3 2 ASN Z 143 TYR Z 155
SITE 1 AI4 1 GLN Z 62
CRYST1 133.350 300.790 144.580 90.00 112.11 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007499 0.000000 0.003047 0.00000
SCALE2 0.000000 0.003325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007466 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
