HEADER IMMUNE SYSTEM 09-MAR-18 6FXN
TITLE CRYSTAL STRUCTURE OF HUMAN BAFF IN COMPLEX WITH FAB FRAGMENT OF ANTI-
TITLE 2 BAFF ANTIBODY BELIMUMAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B;
COMPND 3 CHAIN: A, B, C, J, K, L;
COMPND 4 SYNONYM: B LYMPHOCYTE STIMULATOR,BLYS,B-CELL-ACTIVATING FACTOR,BAFF,
COMPND 5 DENDRITIC CELL-DERIVED TNF-LIKE MOLECULE,TNF- AND APOL-RELATED
COMPND 6 LEUKOCYTE EXPRESSED LIGAND 1,TALL-1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: BELIMUMAB HEAVY CHAIN;
COMPND 11 CHAIN: D, F, H, M, O, Q;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: BELIMUMAB LIGHT CHAIN;
COMPND 15 CHAIN: E, G, I, N, P, R;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TNFSF13B, BAFF, BLYS, TALL1, TNFSF20, ZTNF4, UNQ401/PRO738;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10090
KEYWDS IMMUNOLOGY, B CELL, CYTOKINE, BAFF, ANTIBODY, PROTEROS, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LAMMENS,K.MASKOS,L.WILLEN,X.JIANG,P.SCHNEIDER
REVDAT 2 17-JAN-24 6FXN 1 REMARK
REVDAT 1 04-APR-18 6FXN 0
SPRSDE 04-APR-18 6FXN 6ERX
JRNL AUTH M.VIGOLO,M.G.CHAMBERS,L.WILLEN,D.CHEVALLEY,K.MASKOS,
JRNL AUTH 2 A.LAMMENS,A.TARDIVEL,D.DAS,C.KOWALCZYK-QUINTAS,
JRNL AUTH 3 S.SCHUEPBACH-MALLEPELL,C.R.SMULSKI,M.ESLAMI,A.ROLINK,
JRNL AUTH 4 E.HUMMLER,E.SAMY,Y.FOMEKONG NANFACK,F.MACKAY,M.LIAO,H.HESS,
JRNL AUTH 5 X.JIANG,P.SCHNEIDER
JRNL TITL A LOOP REGION OF BAFF CONTROLS B CELL SURVIVAL AND REGULATES
JRNL TITL 2 RECOGNITION BY DIFFERENT INHIBITORS.
JRNL REF NAT COMMUN V. 9 1199 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29572442
JRNL DOI 10.1038/S41467-018-03323-8
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 138.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 108711
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.600
REMARK 3 FREE R VALUE TEST SET COUNT : 654
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7410
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 34
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 25879
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : 0.29000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.56000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.328
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.269
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.652
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25944 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 23679 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 35416 ; 1.524 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 54474 ; 1.197 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3402 ; 7.616 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 980 ;38.688 ;24.684
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3851 ;13.846 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 87 ;16.333 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4063 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 29817 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5746 ; 0.002 ; 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): 13668 ; 2.222 ; 3.904
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 13667 ; 2.222 ; 3.904
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17050 ; 3.571 ; 6.582
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 17051 ; 3.571 ; 6.582
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12276 ; 3.125 ; 4.170
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 12277 ; 3.125 ; 4.170
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 18367 ; 4.689 ; 6.903
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 25075 ; 6.105 ;34.152
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 25070 ; 6.104 ;34.150
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
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 : A 1 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0330 108.3120 17.1730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0872 T22: 0.0351
REMARK 3 T33: 0.1163 T12: -0.0543
REMARK 3 T13: -0.0625 T23: 0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 3.1552 L22: 4.7333
REMARK 3 L33: 3.4542 L12: -2.0008
REMARK 3 L13: -0.6585 L23: 0.8792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: 0.0778 S13: -0.2636
REMARK 3 S21: 0.0676 S22: -0.0645 S23: 0.1232
REMARK 3 S31: 0.3489 S32: -0.2119 S33: 0.0954
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 : B 1 B 500
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1160 126.3610 4.2560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0999 T22: 0.0869
REMARK 3 T33: 0.1794 T12: -0.0050
REMARK 3 T13: -0.0407 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 2.4586 L22: 2.9261
REMARK 3 L33: 4.6579 L12: -1.1542
REMARK 3 L13: -0.2845 L23: 1.3933
REMARK 3 S TENSOR
REMARK 3 S11: 0.0822 S12: 0.3539 S13: 0.0555
REMARK 3 S21: -0.4577 S22: -0.0335 S23: -0.0731
REMARK 3 S31: -0.1621 S32: 0.0821 S33: -0.0487
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 : C 1 C 500
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9600 120.4550 23.5110
REMARK 3 T TENSOR
REMARK 3 T11: 0.0720 T22: 0.0203
REMARK 3 T33: 0.2028 T12: 0.0021
REMARK 3 T13: -0.1066 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 5.0213 L22: 2.6641
REMARK 3 L33: 3.5972 L12: -0.6495
REMARK 3 L13: -1.8999 L23: 1.0263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0032 S12: -0.1666 S13: -0.0605
REMARK 3 S21: 0.0862 S22: 0.0896 S23: -0.4355
REMARK 3 S31: -0.0657 S32: 0.2643 S33: -0.0928
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 : D 1 D 123
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5170 109.7240 47.1980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1923 T22: 0.6701
REMARK 3 T33: 0.4430 T12: 0.0020
REMARK 3 T13: 0.0102 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 4.2387 L22: 2.4528
REMARK 3 L33: 7.4298 L12: -0.1116
REMARK 3 L13: -4.1775 L23: -2.5572
REMARK 3 S TENSOR
REMARK 3 S11: -0.1322 S12: -0.2313 S13: -0.0997
REMARK 3 S21: 0.3515 S22: 0.4186 S23: 0.5631
REMARK 3 S31: -0.1697 S32: -0.6154 S33: -0.2865
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 : D 124 D 300
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2390 107.6650 79.5930
REMARK 3 T TENSOR
REMARK 3 T11: 0.6790 T22: 0.2652
REMARK 3 T33: 0.9290 T12: 0.1080
REMARK 3 T13: 0.1851 T23: 0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 3.8261 L22: 2.2669
REMARK 3 L33: 3.1006 L12: 0.6670
REMARK 3 L13: 0.7732 L23: -0.5611
REMARK 3 S TENSOR
REMARK 3 S11: -0.1122 S12: -0.0425 S13: 1.0220
REMARK 3 S21: 0.4231 S22: -0.0776 S23: 0.3213
REMARK 3 S31: -0.4362 S32: -0.1222 S33: 0.1899
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 : E 1 E 109
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0690 96.8070 49.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.2127 T22: 0.5117
REMARK 3 T33: 0.3090 T12: 0.0049
REMARK 3 T13: 0.0334 T23: 0.1705
REMARK 3 L TENSOR
REMARK 3 L11: 5.0477 L22: 3.5814
REMARK 3 L33: 5.3103 L12: -1.8835
REMARK 3 L13: 2.0258 L23: -2.1504
REMARK 3 S TENSOR
REMARK 3 S11: -0.2615 S12: -1.0162 S13: -0.6094
REMARK 3 S21: 0.2168 S22: 0.1509 S23: -0.0192
REMARK 3 S31: 0.4118 S32: -0.0202 S33: 0.1107
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 : E 110 E 300
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8550 91.6770 84.4500
REMARK 3 T TENSOR
REMARK 3 T11: 0.4361 T22: 0.1011
REMARK 3 T33: 0.4415 T12: -0.1172
REMARK 3 T13: 0.0802 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 8.7956 L22: 2.5810
REMARK 3 L33: 5.6888 L12: -1.5481
REMARK 3 L13: -1.9352 L23: 0.0835
REMARK 3 S TENSOR
REMARK 3 S11: 0.4118 S12: -0.2078 S13: 0.3365
REMARK 3 S21: 0.4630 S22: -0.2071 S23: 0.3346
REMARK 3 S31: -0.3202 S32: -0.4029 S33: -0.2048
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 : F 1 F 123
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6420 143.0570 2.7390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0340 T22: 0.0819
REMARK 3 T33: 0.1583 T12: 0.0158
REMARK 3 T13: -0.0426 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 5.6694 L22: 6.3067
REMARK 3 L33: 2.0698 L12: -3.6891
REMARK 3 L13: 2.8016 L23: -1.7951
REMARK 3 S TENSOR
REMARK 3 S11: -0.1064 S12: -0.4526 S13: 0.1950
REMARK 3 S21: 0.1170 S22: 0.0676 S23: 0.0781
REMARK 3 S31: -0.1037 S32: -0.1619 S33: 0.0387
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 : F 124 F 300
REMARK 3 ORIGIN FOR THE GROUP (A): -42.4970 142.0230 4.0010
REMARK 3 T TENSOR
REMARK 3 T11: 0.4598 T22: 0.1856
REMARK 3 T33: 0.1887 T12: 0.0935
REMARK 3 T13: -0.1257 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 7.1538 L22: 7.4220
REMARK 3 L33: 2.1776 L12: 3.5347
REMARK 3 L13: -1.0295 L23: 0.3391
REMARK 3 S TENSOR
REMARK 3 S11: 0.1109 S12: -0.5082 S13: -0.1444
REMARK 3 S21: 1.3711 S22: 0.0949 S23: -0.3181
REMARK 3 S31: 0.5238 S32: 0.1737 S33: -0.2058
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 : G 1 G 109
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8860 124.0050 -8.0690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2002 T22: 0.0423
REMARK 3 T33: 0.1999 T12: 0.0788
REMARK 3 T13: -0.0619 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 6.3150 L22: 2.1373
REMARK 3 L33: 5.1456 L12: 0.3589
REMARK 3 L13: 2.5987 L23: 1.1609
REMARK 3 S TENSOR
REMARK 3 S11: 0.2393 S12: 0.1447 S13: -0.4961
REMARK 3 S21: -0.2809 S22: -0.1019 S23: -0.2217
REMARK 3 S31: 0.1950 S32: 0.1238 S33: -0.1374
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 : G 110 G 300
REMARK 3 ORIGIN FOR THE GROUP (A): -49.9910 137.5200 -10.6900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0984 T22: 0.0775
REMARK 3 T33: 0.1487 T12: -0.0600
REMARK 3 T13: -0.0815 T23: 0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 5.6898 L22: 8.1789
REMARK 3 L33: 3.8524 L12: -2.9782
REMARK 3 L13: -1.3468 L23: 2.8281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: 0.0973 S13: 0.1085
REMARK 3 S21: 0.0857 S22: 0.0421 S23: 0.2969
REMARK 3 S31: -0.1083 S32: -0.1641 S33: -0.0421
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 : H 1 H 123
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9750 150.9430 38.6480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1683 T22: 0.0710
REMARK 3 T33: 0.1318 T12: 0.0577
REMARK 3 T13: -0.0588 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 2.4306 L22: 4.8147
REMARK 3 L33: 6.4176 L12: 2.7661
REMARK 3 L13: 2.1112 L23: 3.7152
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: -0.2124 S13: 0.1703
REMARK 3 S21: 0.2059 S22: -0.1549 S23: 0.2598
REMARK 3 S31: -0.0343 S32: -0.2597 S33: 0.0547
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 : H 124 H 300
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1100 181.8480 37.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.3848 T22: 0.5571
REMARK 3 T33: 0.4819 T12: -0.3322
REMARK 3 T13: 0.1812 T23: -0.2637
REMARK 3 L TENSOR
REMARK 3 L11: 2.1544 L22: 4.3683
REMARK 3 L33: 8.3764 L12: -1.1088
REMARK 3 L13: -1.6177 L23: -1.4484
REMARK 3 S TENSOR
REMARK 3 S11: -0.4703 S12: 0.2678 S13: -0.3493
REMARK 3 S21: 0.3928 S22: -0.1060 S23: 0.5815
REMARK 3 S31: 1.0177 S32: -1.6955 S33: 0.5764
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 : I 1 I 109
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8410 151.1670 20.1730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1725 T22: 0.1149
REMARK 3 T33: 0.1350 T12: 0.0186
REMARK 3 T13: -0.0539 T23: -0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 3.7620 L22: 6.2620
REMARK 3 L33: 2.8900 L12: 1.9018
REMARK 3 L13: -1.1907 L23: 0.6026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: 0.1994 S13: -0.1017
REMARK 3 S21: -0.4521 S22: 0.2361 S23: -0.3637
REMARK 3 S31: -0.0458 S32: 0.2675 S33: -0.2034
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 : I 110 I 300
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6780 187.3740 32.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.1727 T22: 0.1144
REMARK 3 T33: 0.1680 T12: -0.0597
REMARK 3 T13: -0.0916 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 3.4110 L22: 4.7915
REMARK 3 L33: 8.6207 L12: -0.3038
REMARK 3 L13: -2.4496 L23: 3.6028
REMARK 3 S TENSOR
REMARK 3 S11: -0.2606 S12: -0.2019 S13: 0.1044
REMARK 3 S21: 0.2746 S22: -0.0633 S23: 0.1322
REMARK 3 S31: 0.1872 S32: 0.2580 S33: 0.3238
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 : J 1 J 500
REMARK 3 ORIGIN FOR THE GROUP (A): 54.6570 166.7830 84.9920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1001 T22: 0.0240
REMARK 3 T33: 0.1008 T12: -0.0268
REMARK 3 T13: -0.0638 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 2.0854 L22: 3.6194
REMARK 3 L33: 3.4119 L12: -1.3355
REMARK 3 L13: 0.8008 L23: -0.5903
REMARK 3 S TENSOR
REMARK 3 S11: -0.0565 S12: 0.0343 S13: 0.2289
REMARK 3 S21: -0.0322 S22: 0.0324 S23: -0.0512
REMARK 3 S31: -0.3778 S32: 0.0468 S33: 0.0240
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 : K 1 K 500
REMARK 3 ORIGIN FOR THE GROUP (A): 49.0500 148.0760 71.9870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0624 T22: 0.0371
REMARK 3 T33: 0.1492 T12: 0.0244
REMARK 3 T13: -0.0799 T23: -0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 2.7146 L22: 2.9180
REMARK 3 L33: 4.5510 L12: -1.2258
REMARK 3 L13: 0.7418 L23: -1.6305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: 0.2752 S13: -0.0161
REMARK 3 S21: -0.2417 S22: -0.1008 S23: 0.0676
REMARK 3 S31: 0.2490 S32: 0.0138 S33: 0.0034
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 : L 1 L 500
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8970 153.9720 90.4200
REMARK 3 T TENSOR
REMARK 3 T11: 0.1144 T22: 0.1093
REMARK 3 T33: 0.1697 T12: 0.0390
REMARK 3 T13: 0.0119 T23: 0.0536
REMARK 3 L TENSOR
REMARK 3 L11: 3.7404 L22: 2.8758
REMARK 3 L33: 2.6095 L12: 0.0529
REMARK 3 L13: 0.8683 L23: -0.9919
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: -0.0577 S13: 0.1070
REMARK 3 S21: 0.1076 S22: 0.2142 S23: 0.5545
REMARK 3 S31: -0.1307 S32: -0.5075 S33: -0.1550
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 : M 1 M 123
REMARK 3 ORIGIN FOR THE GROUP (A): 69.6520 167.1810 115.5800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1021 T22: 0.2143
REMARK 3 T33: 0.2113 T12: 0.0312
REMARK 3 T13: -0.0505 T23: 0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 5.3876 L22: 1.9719
REMARK 3 L33: 5.9106 L12: 1.8583
REMARK 3 L13: 4.0947 L23: 3.2039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0988 S12: -0.0666 S13: -0.2025
REMARK 3 S21: 0.2669 S22: 0.0460 S23: -0.1940
REMARK 3 S31: 0.4293 S32: 0.2949 S33: -0.1448
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 : M 124 M 300
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8060 167.6770 147.1780
REMARK 3 T TENSOR
REMARK 3 T11: 0.2884 T22: 0.0957
REMARK 3 T33: 0.4900 T12: 0.0853
REMARK 3 T13: -0.0634 T23: -0.1039
REMARK 3 L TENSOR
REMARK 3 L11: 6.9041 L22: 2.3888
REMARK 3 L33: 3.7016 L12: 0.0702
REMARK 3 L13: -2.2216 L23: -0.0998
REMARK 3 S TENSOR
REMARK 3 S11: -0.1210 S12: 0.2219 S13: -1.1698
REMARK 3 S21: 0.1419 S22: -0.1593 S23: -0.0250
REMARK 3 S31: 0.5655 S32: 0.2102 S33: 0.2802
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 : N 1 N 109
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9070 178.4170 116.1030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1116 T22: 0.2480
REMARK 3 T33: 0.1753 T12: -0.0129
REMARK 3 T13: -0.1181 T23: -0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 1.9401 L22: 5.0186
REMARK 3 L33: 7.0772 L12: -1.6591
REMARK 3 L13: -0.3519 L23: 2.8961
REMARK 3 S TENSOR
REMARK 3 S11: -0.1142 S12: -0.2088 S13: 0.2152
REMARK 3 S21: 0.0213 S22: -0.1671 S23: 0.1139
REMARK 3 S31: -0.4575 S32: -0.3049 S33: 0.2812
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 : N 110 N 300
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5140 183.3070 152.4640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0771 T22: 0.0266
REMARK 3 T33: 0.1858 T12: -0.0037
REMARK 3 T13: -0.0064 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 7.2402 L22: 2.3599
REMARK 3 L33: 5.6037 L12: -1.3168
REMARK 3 L13: 1.9515 L23: 0.2083
REMARK 3 S TENSOR
REMARK 3 S11: 0.0811 S12: -0.1996 S13: 0.0679
REMARK 3 S21: 0.1927 S22: -0.0706 S23: -0.1422
REMARK 3 S31: 0.1566 S32: 0.1925 S33: -0.0106
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 : O 1 O 123
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3190 124.0780 106.6660
REMARK 3 T TENSOR
REMARK 3 T11: 0.3785 T22: 0.2124
REMARK 3 T33: 0.1946 T12: -0.0281
REMARK 3 T13: -0.1049 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 4.0154 L22: 5.8451
REMARK 3 L33: 5.2751 L12: 3.1478
REMARK 3 L13: -1.7948 L23: -3.4573
REMARK 3 S TENSOR
REMARK 3 S11: 0.2641 S12: -0.5258 S13: -0.2927
REMARK 3 S21: 0.4625 S22: -0.2098 S23: -0.0840
REMARK 3 S31: 0.1743 S32: -0.1509 S33: -0.0542
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 : O 124 O 300
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7350 92.2970 106.5870
REMARK 3 T TENSOR
REMARK 3 T11: 0.5204 T22: 0.7513
REMARK 3 T33: 0.6491 T12: -0.3587
REMARK 3 T13: -0.0563 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 1.1811 L22: 2.9304
REMARK 3 L33: 6.3914 L12: -0.9482
REMARK 3 L13: 0.0413 L23: 2.1498
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.3425 S13: -0.0109
REMARK 3 S21: -0.0206 S22: 0.2253 S23: -0.5201
REMARK 3 S31: -0.3408 S32: 1.1149 S33: -0.2245
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 : P 1 P 109
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6740 122.7790 88.0580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2023 T22: 0.2959
REMARK 3 T33: 0.1763 T12: -0.0258
REMARK 3 T13: -0.0858 T23: 0.1284
REMARK 3 L TENSOR
REMARK 3 L11: 4.6003 L22: 6.6589
REMARK 3 L33: 2.7031 L12: 1.6827
REMARK 3 L13: 0.7394 L23: 0.3023
REMARK 3 S TENSOR
REMARK 3 S11: 0.0501 S12: 0.1876 S13: 0.0434
REMARK 3 S21: -0.2035 S22: 0.0793 S23: 0.3001
REMARK 3 S31: 0.1354 S32: -0.5450 S33: -0.1293
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 : P 110 P 300
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9600 86.9280 102.6950
REMARK 3 T TENSOR
REMARK 3 T11: 0.4578 T22: 0.4739
REMARK 3 T33: 0.3588 T12: -0.3217
REMARK 3 T13: -0.0160 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 3.4416 L22: 4.5673
REMARK 3 L33: 5.8153 L12: -0.2207
REMARK 3 L13: 0.8576 L23: -1.9353
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.6972 S13: -0.1673
REMARK 3 S21: 0.3237 S22: -0.1137 S23: -0.1249
REMARK 3 S31: 0.0474 S32: -0.0060 S33: 0.1246
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 : Q 1 Q 123
REMARK 3 ORIGIN FOR THE GROUP (A): 79.1320 132.3790 72.3160
REMARK 3 T TENSOR
REMARK 3 T11: 0.1337 T22: 0.0435
REMARK 3 T33: 0.1805 T12: 0.0013
REMARK 3 T13: -0.1340 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 5.7791 L22: 5.7101
REMARK 3 L33: 2.0873 L12: -3.8437
REMARK 3 L13: -2.9483 L23: 1.0330
REMARK 3 S TENSOR
REMARK 3 S11: -0.1436 S12: -0.4438 S13: -0.1815
REMARK 3 S21: 0.1425 S22: 0.1474 S23: 0.0553
REMARK 3 S31: 0.0820 S32: 0.2935 S33: -0.0037
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 : Q 124 Q 300
REMARK 3 ORIGIN FOR THE GROUP (A): 109.4840 133.4580 73.2270
REMARK 3 T TENSOR
REMARK 3 T11: 0.4761 T22: 0.2263
REMARK 3 T33: 0.3428 T12: 0.0331
REMARK 3 T13: 0.0656 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 5.5246 L22: 6.9833
REMARK 3 L33: 2.1032 L12: 3.5709
REMARK 3 L13: 0.4465 L23: -0.2882
REMARK 3 S TENSOR
REMARK 3 S11: 0.5080 S12: -0.4867 S13: 0.1102
REMARK 3 S21: 1.1579 S22: -0.2375 S23: 0.4289
REMARK 3 S31: -0.2669 S32: 0.1239 S33: -0.2704
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 : R 1 R 109
REMARK 3 ORIGIN FOR THE GROUP (A): 80.3630 150.9000 60.5640
REMARK 3 T TENSOR
REMARK 3 T11: 0.2254 T22: 0.0694
REMARK 3 T33: 0.1723 T12: 0.1019
REMARK 3 T13: -0.0147 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 7.0389 L22: 3.1360
REMARK 3 L33: 3.7637 L12: 0.6155
REMARK 3 L13: -1.9261 L23: -1.0610
REMARK 3 S TENSOR
REMARK 3 S11: 0.2483 S12: 0.3707 S13: 0.3357
REMARK 3 S21: -0.2653 S22: -0.1801 S23: -0.1511
REMARK 3 S31: -0.2224 S32: 0.0298 S33: -0.0682
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 : R 110 R 300
REMARK 3 ORIGIN FOR THE GROUP (A): 116.4670 137.0680 58.1270
REMARK 3 T TENSOR
REMARK 3 T11: 0.2375 T22: 0.0963
REMARK 3 T33: 0.2953 T12: 0.0122
REMARK 3 T13: -0.0212 T23: -0.1128
REMARK 3 L TENSOR
REMARK 3 L11: 5.0203 L22: 6.9419
REMARK 3 L33: 3.7033 L12: -2.3890
REMARK 3 L13: 0.5782 L23: -2.5176
REMARK 3 S TENSOR
REMARK 3 S11: 0.1246 S12: 0.0823 S13: -0.0356
REMARK 3 S21: -0.1969 S22: -0.0340 S23: -0.1696
REMARK 3 S31: 0.0724 S32: 0.1467 S33: -0.0907
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6FXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009070.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109365
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 138.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.360
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1KD7 , 7FAB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% (W/V) PEG4000, 0.1 M MGCL2, 0.1 M
REMARK 280 HEPES PH 7.5, VAPOR DIFFUSION, 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 67.74950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, M, N, O, P, Q, R
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 A 122
REMARK 465 ARG A 123
REMARK 465 GLY A 124
REMARK 465 SER A 125
REMARK 465 HIS A 126
REMARK 465 HIS A 127
REMARK 465 HIS A 128
REMARK 465 HIS A 129
REMARK 465 HIS A 130
REMARK 465 HIS A 131
REMARK 465 GLY A 132
REMARK 465 SER A 133
REMARK 465 ALA A 134
REMARK 465 VAL A 135
REMARK 465 GLN A 136
REMARK 465 GLY A 137
REMARK 465 PRO A 138
REMARK 465 GLU A 139
REMARK 465 GLU A 140
REMARK 465 THR A 141
REMARK 465 MET B 122
REMARK 465 ARG B 123
REMARK 465 GLY B 124
REMARK 465 SER B 125
REMARK 465 HIS B 126
REMARK 465 HIS B 127
REMARK 465 HIS B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 GLY B 132
REMARK 465 SER B 133
REMARK 465 ALA B 134
REMARK 465 VAL B 135
REMARK 465 GLN B 136
REMARK 465 GLY B 137
REMARK 465 PRO B 138
REMARK 465 GLU B 139
REMARK 465 GLU B 140
REMARK 465 THR B 141
REMARK 465 MET C 122
REMARK 465 ARG C 123
REMARK 465 GLY C 124
REMARK 465 SER C 125
REMARK 465 HIS C 126
REMARK 465 HIS C 127
REMARK 465 HIS C 128
REMARK 465 HIS C 129
REMARK 465 HIS C 130
REMARK 465 HIS C 131
REMARK 465 GLY C 132
REMARK 465 SER C 133
REMARK 465 ALA C 134
REMARK 465 VAL C 135
REMARK 465 GLN C 136
REMARK 465 GLY C 137
REMARK 465 PRO C 138
REMARK 465 GLU C 139
REMARK 465 GLU C 140
REMARK 465 THR C 141
REMARK 465 SER D 138
REMARK 465 LYS D 139
REMARK 465 SER D 140
REMARK 465 THR D 141
REMARK 465 SER D 142
REMARK 465 GLY D 143
REMARK 465 GLY D 144
REMARK 465 PRO D 223
REMARK 465 LYS D 224
REMARK 465 SER D 225
REMARK 465 SER E 1
REMARK 465 SER E 2
REMARK 465 GLU E 212
REMARK 465 CYS E 213
REMARK 465 SER E 214
REMARK 465 GLN F 1
REMARK 465 SER F 138
REMARK 465 LYS F 139
REMARK 465 SER F 140
REMARK 465 SER F 225
REMARK 465 SER G 1
REMARK 465 GLU G 212
REMARK 465 CYS G 213
REMARK 465 SER G 214
REMARK 465 GLN H 1
REMARK 465 SER H 138
REMARK 465 LYS H 139
REMARK 465 SER H 140
REMARK 465 THR H 141
REMARK 465 SER H 142
REMARK 465 GLY H 143
REMARK 465 GLY H 144
REMARK 465 SER H 225
REMARK 465 SER I 1
REMARK 465 GLU I 212
REMARK 465 CYS I 213
REMARK 465 SER I 214
REMARK 465 MET J 122
REMARK 465 ARG J 123
REMARK 465 GLY J 124
REMARK 465 SER J 125
REMARK 465 HIS J 126
REMARK 465 HIS J 127
REMARK 465 HIS J 128
REMARK 465 HIS J 129
REMARK 465 HIS J 130
REMARK 465 HIS J 131
REMARK 465 GLY J 132
REMARK 465 SER J 133
REMARK 465 ALA J 134
REMARK 465 VAL J 135
REMARK 465 GLN J 136
REMARK 465 GLY J 137
REMARK 465 PRO J 138
REMARK 465 GLU J 139
REMARK 465 GLU J 140
REMARK 465 THR J 141
REMARK 465 MET K 122
REMARK 465 ARG K 123
REMARK 465 GLY K 124
REMARK 465 SER K 125
REMARK 465 HIS K 126
REMARK 465 HIS K 127
REMARK 465 HIS K 128
REMARK 465 HIS K 129
REMARK 465 HIS K 130
REMARK 465 HIS K 131
REMARK 465 GLY K 132
REMARK 465 SER K 133
REMARK 465 ALA K 134
REMARK 465 VAL K 135
REMARK 465 GLN K 136
REMARK 465 GLY K 137
REMARK 465 PRO K 138
REMARK 465 GLU K 139
REMARK 465 GLU K 140
REMARK 465 THR K 141
REMARK 465 MET L 122
REMARK 465 ARG L 123
REMARK 465 GLY L 124
REMARK 465 SER L 125
REMARK 465 HIS L 126
REMARK 465 HIS L 127
REMARK 465 HIS L 128
REMARK 465 HIS L 129
REMARK 465 HIS L 130
REMARK 465 HIS L 131
REMARK 465 GLY L 132
REMARK 465 SER L 133
REMARK 465 ALA L 134
REMARK 465 VAL L 135
REMARK 465 GLN L 136
REMARK 465 GLY L 137
REMARK 465 PRO L 138
REMARK 465 GLU L 139
REMARK 465 GLU L 140
REMARK 465 THR L 141
REMARK 465 GLN M 1
REMARK 465 SER M 138
REMARK 465 LYS M 139
REMARK 465 SER M 140
REMARK 465 THR M 141
REMARK 465 SER M 142
REMARK 465 GLY M 143
REMARK 465 GLY M 144
REMARK 465 LYS M 224
REMARK 465 SER M 225
REMARK 465 SER N 1
REMARK 465 GLU N 212
REMARK 465 CYS N 213
REMARK 465 SER N 214
REMARK 465 SER O 137
REMARK 465 SER O 138
REMARK 465 LYS O 139
REMARK 465 SER O 140
REMARK 465 THR O 141
REMARK 465 SER O 142
REMARK 465 GLY O 143
REMARK 465 GLY O 144
REMARK 465 LYS O 224
REMARK 465 SER O 225
REMARK 465 SER P 1
REMARK 465 GLU P 212
REMARK 465 CYS P 213
REMARK 465 SER P 214
REMARK 465 GLN Q 1
REMARK 465 SER Q 138
REMARK 465 LYS Q 139
REMARK 465 SER Q 140
REMARK 465 THR Q 141
REMARK 465 SER Q 142
REMARK 465 GLY Q 143
REMARK 465 GLY Q 144
REMARK 465 LYS Q 224
REMARK 465 SER Q 225
REMARK 465 SER R 1
REMARK 465 THR R 211
REMARK 465 GLU R 212
REMARK 465 CYS R 213
REMARK 465 SER R 214
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 142 CG1 CG2
REMARK 480 LYS A 160 CE NZ
REMARK 480 LYS A 181 CD CE NZ
REMARK 480 GLU A 182 CD OE1 OE2
REMARK 480 LYS A 184 NZ
REMARK 480 LYS A 204 CE NZ
REMARK 480 ILE A 212 CD1
REMARK 480 LYS A 215 CD CE NZ
REMARK 480 LEU A 285 CD1 CD2
REMARK 480 VAL B 142 CG1 CG2
REMARK 480 GLU B 154 CD OE1 OE2
REMARK 480 LYS B 160 CD CE NZ
REMARK 480 LYS B 181 CD CE NZ
REMARK 480 LYS B 184 NZ
REMARK 480 LYS B 188 CE NZ
REMARK 480 LYS B 204 CD CE NZ
REMARK 480 LYS B 215 CD CE NZ
REMARK 480 GLU B 254 CD OE1 OE2
REMARK 480 LEU B 285 CD1 CD2
REMARK 480 VAL C 142 CG1 CG2
REMARK 480 GLU C 154 CD OE1 OE2
REMARK 480 LYS C 160 CD CE NZ
REMARK 480 LYS C 181 CG CD CE NZ
REMARK 480 LYS C 184 CE NZ
REMARK 480 LYS C 204 CE NZ
REMARK 480 LYS C 215 NZ
REMARK 480 LYS C 252 CE NZ
REMARK 480 LEU C 285 CD1 CD2
REMARK 480 GLN D 1 CG CD OE1 NE2
REMARK 480 VAL D 2 CG1 CG2
REMARK 480 GLN D 3 CD OE1 NE2
REMARK 480 GLN D 5 CD OE1 NE2
REMARK 480 LYS D 12 NZ
REMARK 480 LYS D 13 CD CE NZ
REMARK 480 LYS D 23 CD CE NZ
REMARK 480 SER D 25 OG
REMARK 480 ILE D 34 CD1
REMARK 480 LYS D 59 NZ
REMARK 480 GLN D 62 CD OE1 NE2
REMARK 480 LEU D 83 CD1 CD2
REMARK 480 SER D 84 OG
REMARK 480 SER D 85 OG
REMARK 480 ARG D 87 CZ NH1 NH2
REMARK 480 ARG D 115 CD NE CZ NH1 NH2
REMARK 480 SER D 125 OG
REMARK 480 LYS D 127 CG CD CE NZ
REMARK 480 SER D 130 OG
REMARK 480 LEU D 148 CD1 CD2
REMARK 480 LYS D 153 CD CE NZ
REMARK 480 SER D 182 OG
REMARK 480 LEU D 185 CD1 CD2
REMARK 480 LEU D 199 CD1 CD2
REMARK 480 THR D 201 OG1 CG2
REMARK 480 ILE D 205 CD1
REMARK 480 VAL D 208 CG1 CG2
REMARK 480 LYS D 211 CE NZ
REMARK 480 LYS D 216 CE NZ
REMARK 480 LYS D 219 CE NZ
REMARK 480 LYS D 220 NZ
REMARK 480 VAL D 221 CG1 CG2
REMARK 480 GLU D 222 CG CD OE1 OE2
REMARK 480 GLU E 3 CD OE1 OE2
REMARK 480 LEU E 14 CD1 CD2
REMARK 480 LYS E 50 CE NZ
REMARK 480 ASP E 59 CG OD1 OD2
REMARK 480 LEU E 108 CD1 CD2
REMARK 480 LYS E 112 NZ
REMARK 480 SER E 124 OG
REMARK 480 GLU E 125 CD OE1 OE2
REMARK 480 GLN E 128 CG CD OE1 NE2
REMARK 480 LYS E 131 CE NZ
REMARK 480 LYS E 158 CD CE NZ
REMARK 480 LYS E 168 CE NZ
REMARK 480 GLU E 185 CD OE1 OE2
REMARK 480 LYS E 188 CD CE NZ
REMARK 480 ARG E 191 CG CD NE CZ NH1 NH2
REMARK 480 LYS E 206 NZ
REMARK 480 LYS F 13 NZ
REMARK 480 ARG F 19 CZ NH1 NH2
REMARK 480 LYS F 23 CD CE NZ
REMARK 480 GLN F 62 CD OE1 NE2
REMARK 480 GLU F 82 CD OE1 OE2
REMARK 480 ARG F 115 CD NE CZ NH1 NH2
REMARK 480 SER F 137 OG
REMARK 480 THR F 141 OG1 CG2
REMARK 480 SER F 142 OG
REMARK 480 THR F 201 OG1 CG2
REMARK 480 ILE F 205 CD1
REMARK 480 LYS F 211 NZ
REMARK 480 LYS F 216 CD CE NZ
REMARK 480 LYS F 219 NZ
REMARK 480 LYS F 220 CE NZ
REMARK 480 LYS F 224 CD CE NZ
REMARK 480 LYS G 50 CE NZ
REMARK 480 LYS G 131 CD CE NZ
REMARK 480 LYS G 151 CE NZ
REMARK 480 LYS G 158 CD CE NZ
REMARK 480 LYS G 173 NZ
REMARK 480 LYS G 188 CE NZ
REMARK 480 ARG G 191 CD NE CZ NH1 NH2
REMARK 480 THR G 211 OG1 CG2
REMARK 480 LYS H 13 CE NZ
REMARK 480 LYS H 23 NZ
REMARK 480 GLN H 43 CD OE1 NE2
REMARK 480 LYS H 59 NZ
REMARK 480 GLU H 89 CD OE1 OE2
REMARK 480 ARG H 115 CG CD NE CZ NH1 NH2
REMARK 480 SER H 125 OG
REMARK 480 LYS H 127 CG CD CE NZ
REMARK 480 LYS H 153 CE NZ
REMARK 480 LEU H 169 CD1 CD2
REMARK 480 SER H 182 OG
REMARK 480 ILE H 205 CD1
REMARK 480 LYS H 211 CG CD CE NZ
REMARK 480 ASN H 214 CG OD1 ND2
REMARK 480 LYS H 216 CD CE NZ
REMARK 480 LYS H 220 CD CE NZ
REMARK 480 GLU H 222 CG CD OE1 OE2
REMARK 480 LYS H 224 CG CD CE NZ
REMARK 480 GLU I 3 CD OE1 OE2
REMARK 480 ASP I 25 CG OD1 OD2
REMARK 480 LYS I 112 CG CD CE NZ
REMARK 480 LYS I 131 CE NZ
REMARK 480 LYS I 151 NZ
REMARK 480 LYS I 158 CD CE NZ
REMARK 480 LYS I 168 CE NZ
REMARK 480 LYS I 188 CE NZ
REMARK 480 ARG I 191 CZ NH1 NH2
REMARK 480 VAL J 142 CG1 CG2
REMARK 480 GLU J 154 CD OE1 OE2
REMARK 480 LYS J 160 CG CD CE NZ
REMARK 480 LYS J 181 CE NZ
REMARK 480 GLU J 182 CD OE1 OE2
REMARK 480 LYS J 184 NZ
REMARK 480 LYS J 188 NZ
REMARK 480 LYS J 215 NZ
REMARK 480 PHE J 220 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 LYS J 252 CD CE NZ
REMARK 480 LEU J 285 CD1 CD2
REMARK 480 VAL K 142 CG1 CG2
REMARK 480 GLU K 154 CD OE1 OE2
REMARK 480 LYS K 160 NZ
REMARK 480 LYS K 181 CG CD CE NZ
REMARK 480 LYS K 184 NZ
REMARK 480 LYS K 204 CE NZ
REMARK 480 LYS K 215 NZ
REMARK 480 LYS K 252 CE NZ
REMARK 480 LEU K 285 CD1 CD2
REMARK 480 VAL L 142 CG1 CG2
REMARK 480 GLU L 154 CD OE1 OE2
REMARK 480 LYS L 160 CD CE NZ
REMARK 480 SER L 176 OG
REMARK 480 LYS L 181 CD CE NZ
REMARK 480 GLU L 182 CD OE1 OE2
REMARK 480 LYS L 184 CE NZ
REMARK 480 LYS L 188 CE NZ
REMARK 480 LYS L 204 NZ
REMARK 480 LYS L 215 CE NZ
REMARK 480 LYS L 252 CD CE NZ
REMARK 480 GLU L 254 CD OE1 OE2
REMARK 480 LEU L 285 CD1 CD2
REMARK 480 VAL M 2 CG1 CG2
REMARK 480 GLU M 10 CD OE1 OE2
REMARK 480 LYS M 13 CE NZ
REMARK 480 LYS M 23 CE NZ
REMARK 480 GLU M 89 CD OE1 OE2
REMARK 480 ARG M 115 CD NE CZ NH1 NH2
REMARK 480 ILE M 205 CD1
REMARK 480 LYS M 211 CE NZ
REMARK 480 LYS M 216 CD CE NZ
REMARK 480 LYS M 219 CE NZ
REMARK 480 GLU M 222 CG CD OE1 OE2
REMARK 480 GLU N 3 CD OE1 OE2
REMARK 480 LYS N 50 NZ
REMARK 480 GLU N 80 CD OE1 OE2
REMARK 480 LYS N 112 NZ
REMARK 480 GLU N 125 CD OE1 OE2
REMARK 480 LYS N 131 NZ
REMARK 480 LYS N 158 CD CE NZ
REMARK 480 GLU N 185 CG CD OE1 OE2
REMARK 480 LYS N 188 CD CE NZ
REMARK 480 ARG N 191 CZ NH1 NH2
REMARK 480 THR N 211 OG1 CG2
REMARK 480 GLN O 1 CG CD OE1 NE2
REMARK 480 VAL O 2 CG1 CG2
REMARK 480 ARG O 19 CZ NH1 NH2
REMARK 480 LYS O 23 NZ
REMARK 480 SER O 25 OG
REMARK 480 LYS O 59 CE NZ
REMARK 480 GLU O 82 CD OE1 OE2
REMARK 480 SER O 88 OG
REMARK 480 ARG O 115 CG CD NE CZ NH1 NH2
REMARK 480 LYS O 127 CE NZ
REMARK 480 LEU O 148 CD1 CD2
REMARK 480 LYS O 153 NZ
REMARK 480 SER O 163 OG
REMARK 480 LEU O 169 CG CD1 CD2
REMARK 480 ILE O 205 CD1
REMARK 480 VAL O 208 CG1 CG2
REMARK 480 LYS O 211 CE NZ
REMARK 480 LYS O 216 CE NZ
REMARK 480 VAL O 217 CG1 CG2
REMARK 480 LYS O 219 CE NZ
REMARK 480 LYS O 220 CD CE NZ
REMARK 480 GLU O 222 CD OE1 OE2
REMARK 480 GLU P 3 CG CD OE1 OE2
REMARK 480 LYS P 50 CG CD CE NZ
REMARK 480 LYS P 112 CE NZ
REMARK 480 GLU P 125 CD OE1 OE2
REMARK 480 GLN P 128 CD OE1 NE2
REMARK 480 LYS P 131 CD CE NZ
REMARK 480 LYS P 151 CE NZ
REMARK 480 SER P 154 OG
REMARK 480 LYS P 158 CG CD CE NZ
REMARK 480 LYS P 168 NZ
REMARK 480 LYS P 173 NZ
REMARK 480 LYS P 188 CD CE NZ
REMARK 480 ARG P 191 CD NE CZ NH1 NH2
REMARK 480 LYS P 206 NZ
REMARK 480 THR P 211 OG1 CG2
REMARK 480 LYS Q 13 CE NZ
REMARK 480 LYS Q 23 CD CE NZ
REMARK 480 LYS Q 59 NZ
REMARK 480 ARG Q 115 CD NE CZ NH1 NH2
REMARK 480 LYS Q 127 NZ
REMARK 480 THR Q 170 OG1 CG2
REMARK 480 SER Q 182 OG
REMARK 480 SER Q 197 OG
REMARK 480 ILE Q 205 CD1
REMARK 480 LYS Q 211 CD CE NZ
REMARK 480 LYS Q 216 CE NZ
REMARK 480 LYS Q 219 NZ
REMARK 480 LYS Q 220 CD CE NZ
REMARK 480 GLU Q 222 CG CD OE1 OE2
REMARK 480 GLU R 3 CD OE1 OE2
REMARK 480 GLU R 80 CD OE1 OE2
REMARK 480 LYS R 131 CE NZ
REMARK 480 LYS R 151 CD CE NZ
REMARK 480 LYS R 158 CD CE NZ
REMARK 480 LYS R 188 CE NZ
REMARK 480 ARG R 191 NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG N 191 NE ARG N 191 CZ 0.082
REMARK 500
REMARK 500 REMARK: NULL
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 LEU D 83 CB - CG - CD1 ANGL. DEV. = 17.4 DEGREES
REMARK 500 LEU D 83 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG D 87 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG F 19 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 VAL L 142 CA - CB - CG2 ANGL. DEV. = 9.1 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 GLU A 182 58.12 38.48
REMARK 500 ASN A 242 91.61 -165.16
REMARK 500 LEU B 272 51.02 -105.22
REMARK 500 ASN C 242 89.72 -168.77
REMARK 500 ASN D 30 -138.70 59.12
REMARK 500 GLN D 62 44.32 -82.02
REMARK 500 ASN D 63 34.90 -141.11
REMARK 500 SER D 85 60.24 60.00
REMARK 500 ALA D 109 -155.82 -100.49
REMARK 500 HIS E 96 -167.16 62.18
REMARK 500 ALA E 145 108.67 -160.54
REMARK 500 ASP E 153 -119.49 62.27
REMARK 500 LYS E 158 -71.12 -67.41
REMARK 500 ASN F 30 -125.02 57.63
REMARK 500 GLN F 62 41.92 -101.93
REMARK 500 ASN F 63 42.42 -149.00
REMARK 500 ALA F 109 -163.81 -108.32
REMARK 500 SER F 142 95.01 -161.15
REMARK 500 ASP F 154 71.25 57.83
REMARK 500 THR F 170 -60.15 -97.70
REMARK 500 SER G 66 103.01 -161.15
REMARK 500 ALA G 83 -179.06 -171.72
REMARK 500 HIS G 96 -165.71 60.28
REMARK 500 ASP G 153 -130.55 56.51
REMARK 500 ASN H 30 -121.80 53.31
REMARK 500 ALA H 109 -163.25 -115.89
REMARK 500 ASP H 154 74.40 50.55
REMARK 500 THR H 201 -60.91 -145.23
REMARK 500 SER I 64 144.31 -175.76
REMARK 500 SER I 66 112.79 -162.12
REMARK 500 HIS I 96 -155.85 -90.25
REMARK 500 ASP I 153 -113.28 52.45
REMARK 500 LYS I 158 -78.94 -65.71
REMARK 500 ASN J 242 91.46 -160.54
REMARK 500 ASN K 242 88.92 -160.06
REMARK 500 ASN M 30 -137.25 60.57
REMARK 500 ASP M 154 77.33 59.56
REMARK 500 SER N 66 96.23 -162.64
REMARK 500 HIS N 96 -165.63 65.34
REMARK 500 ASP N 153 -111.89 53.01
REMARK 500 LYS N 158 -73.94 -69.61
REMARK 500 ASN N 172 -2.37 69.27
REMARK 500 ASN O 30 -121.41 50.73
REMARK 500 ALA O 109 -165.40 -103.15
REMARK 500 SER O 111 139.14 -175.12
REMARK 500 ASP O 154 72.54 60.42
REMARK 500 GLU P 82 103.20 -51.33
REMARK 500 HIS P 96 -169.43 65.53
REMARK 500 ASP P 153 -117.14 56.85
REMARK 500 LYS P 158 -73.31 -74.36
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6FXN A 134 285 UNP Q9Y275 TN13B_HUMAN 134 285
DBREF 6FXN B 134 285 UNP Q9Y275 TN13B_HUMAN 134 285
DBREF 6FXN C 134 285 UNP Q9Y275 TN13B_HUMAN 134 285
DBREF 6FXN D 1 225 PDB 6FXN 6FXN 1 225
DBREF 6FXN E 1 214 PDB 6FXN 6FXN 1 214
DBREF 6FXN F 1 225 PDB 6FXN 6FXN 1 225
DBREF 6FXN G 1 214 PDB 6FXN 6FXN 1 214
DBREF 6FXN H 1 225 PDB 6FXN 6FXN 1 225
DBREF 6FXN I 1 214 PDB 6FXN 6FXN 1 214
DBREF 6FXN J 134 285 UNP Q9Y275 TN13B_HUMAN 134 285
DBREF 6FXN K 134 285 UNP Q9Y275 TN13B_HUMAN 134 285
DBREF 6FXN L 134 285 UNP Q9Y275 TN13B_HUMAN 134 285
DBREF 6FXN M 1 225 PDB 6FXN 6FXN 1 225
DBREF 6FXN N 1 214 PDB 6FXN 6FXN 1 214
DBREF 6FXN O 1 225 PDB 6FXN 6FXN 1 225
DBREF 6FXN P 1 214 PDB 6FXN 6FXN 1 214
DBREF 6FXN Q 1 225 PDB 6FXN 6FXN 1 225
DBREF 6FXN R 1 214 PDB 6FXN 6FXN 1 214
SEQADV 6FXN MET A 122 UNP Q9Y275 INITIATING METHIONINE
SEQADV 6FXN ARG A 123 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY A 124 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER A 125 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS A 126 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS A 127 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS A 128 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS A 129 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS A 130 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS A 131 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY A 132 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER A 133 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN ALA A 218 UNP Q9Y275 HIS 218 ENGINEERED MUTATION
SEQADV 6FXN MET B 122 UNP Q9Y275 INITIATING METHIONINE
SEQADV 6FXN ARG B 123 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY B 124 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER B 125 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS B 126 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS B 127 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS B 128 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS B 129 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS B 130 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS B 131 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY B 132 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER B 133 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN ALA B 218 UNP Q9Y275 HIS 218 ENGINEERED MUTATION
SEQADV 6FXN MET C 122 UNP Q9Y275 INITIATING METHIONINE
SEQADV 6FXN ARG C 123 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY C 124 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER C 125 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS C 126 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS C 127 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS C 128 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS C 129 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS C 130 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS C 131 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY C 132 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER C 133 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN ALA C 218 UNP Q9Y275 HIS 218 ENGINEERED MUTATION
SEQADV 6FXN MET J 122 UNP Q9Y275 INITIATING METHIONINE
SEQADV 6FXN ARG J 123 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY J 124 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER J 125 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS J 126 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS J 127 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS J 128 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS J 129 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS J 130 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS J 131 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY J 132 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER J 133 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN ALA J 218 UNP Q9Y275 HIS 218 ENGINEERED MUTATION
SEQADV 6FXN MET K 122 UNP Q9Y275 INITIATING METHIONINE
SEQADV 6FXN ARG K 123 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY K 124 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER K 125 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS K 126 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS K 127 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS K 128 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS K 129 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS K 130 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS K 131 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY K 132 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER K 133 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN ALA K 218 UNP Q9Y275 HIS 218 ENGINEERED MUTATION
SEQADV 6FXN MET L 122 UNP Q9Y275 INITIATING METHIONINE
SEQADV 6FXN ARG L 123 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY L 124 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER L 125 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS L 126 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS L 127 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS L 128 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS L 129 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS L 130 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN HIS L 131 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN GLY L 132 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN SER L 133 UNP Q9Y275 EXPRESSION TAG
SEQADV 6FXN ALA L 218 UNP Q9Y275 HIS 218 ENGINEERED MUTATION
SEQRES 1 A 164 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 A 164 VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU
SEQRES 3 A 164 GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS
SEQRES 4 A 164 GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS
SEQRES 5 A 164 ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU
SEQRES 6 A 164 VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL
SEQRES 7 A 164 LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE
SEQRES 8 A 164 GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER
SEQRES 9 A 164 LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU
SEQRES 10 A 164 THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA
SEQRES 11 A 164 LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO
SEQRES 12 A 164 ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR
SEQRES 13 A 164 PHE PHE GLY ALA LEU LYS LEU LEU
SEQRES 1 B 164 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 B 164 VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU
SEQRES 3 B 164 GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS
SEQRES 4 B 164 GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS
SEQRES 5 B 164 ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU
SEQRES 6 B 164 VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL
SEQRES 7 B 164 LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE
SEQRES 8 B 164 GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER
SEQRES 9 B 164 LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU
SEQRES 10 B 164 THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA
SEQRES 11 B 164 LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO
SEQRES 12 B 164 ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR
SEQRES 13 B 164 PHE PHE GLY ALA LEU LYS LEU LEU
SEQRES 1 C 164 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 C 164 VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU
SEQRES 3 C 164 GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS
SEQRES 4 C 164 GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS
SEQRES 5 C 164 ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU
SEQRES 6 C 164 VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL
SEQRES 7 C 164 LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE
SEQRES 8 C 164 GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER
SEQRES 9 C 164 LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU
SEQRES 10 C 164 THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA
SEQRES 11 C 164 LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO
SEQRES 12 C 164 ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR
SEQRES 13 C 164 PHE PHE GLY ALA LEU LYS LEU LEU
SEQRES 1 D 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 D 225 PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY
SEQRES 3 D 225 GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 D 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 D 225 PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN
SEQRES 6 D 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR
SEQRES 7 D 225 ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 D 225 ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU
SEQRES 9 D 225 PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR
SEQRES 10 D 225 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 D 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 D 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 D 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 D 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 D 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 D 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 D 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 D 225 GLU PRO LYS SER
SEQRES 1 E 214 SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA
SEQRES 2 E 214 LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER
SEQRES 3 E 214 LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 E 214 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN
SEQRES 5 E 214 ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER
SEQRES 6 E 214 SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN
SEQRES 7 E 214 ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP
SEQRES 8 E 214 SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU
SEQRES 9 E 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 E 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 E 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 E 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 E 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 E 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 E 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 E 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 E 214 ALA PRO THR GLU CYS SER
SEQRES 1 F 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 F 225 PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY
SEQRES 3 F 225 GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 F 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 F 225 PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN
SEQRES 6 F 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR
SEQRES 7 F 225 ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 F 225 ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU
SEQRES 9 F 225 PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR
SEQRES 10 F 225 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 F 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 F 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 F 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 F 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 F 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 F 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 F 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 F 225 GLU PRO LYS SER
SEQRES 1 G 214 SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA
SEQRES 2 G 214 LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER
SEQRES 3 G 214 LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 G 214 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN
SEQRES 5 G 214 ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER
SEQRES 6 G 214 SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN
SEQRES 7 G 214 ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP
SEQRES 8 G 214 SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU
SEQRES 9 G 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 G 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 G 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 G 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 G 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 G 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 G 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 G 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 G 214 ALA PRO THR GLU CYS SER
SEQRES 1 H 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 225 PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 225 GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 H 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 H 225 PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN
SEQRES 6 H 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR
SEQRES 7 H 225 ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU
SEQRES 9 H 225 PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR
SEQRES 10 H 225 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 H 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 H 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 H 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 H 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 H 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 H 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 H 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 H 225 GLU PRO LYS SER
SEQRES 1 I 214 SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA
SEQRES 2 I 214 LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER
SEQRES 3 I 214 LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 I 214 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN
SEQRES 5 I 214 ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER
SEQRES 6 I 214 SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN
SEQRES 7 I 214 ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP
SEQRES 8 I 214 SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU
SEQRES 9 I 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 I 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 I 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 I 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 I 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 I 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 I 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 I 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 I 214 ALA PRO THR GLU CYS SER
SEQRES 1 J 164 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 J 164 VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU
SEQRES 3 J 164 GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS
SEQRES 4 J 164 GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS
SEQRES 5 J 164 ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU
SEQRES 6 J 164 VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL
SEQRES 7 J 164 LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE
SEQRES 8 J 164 GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER
SEQRES 9 J 164 LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU
SEQRES 10 J 164 THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA
SEQRES 11 J 164 LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO
SEQRES 12 J 164 ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR
SEQRES 13 J 164 PHE PHE GLY ALA LEU LYS LEU LEU
SEQRES 1 K 164 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 K 164 VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU
SEQRES 3 K 164 GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS
SEQRES 4 K 164 GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS
SEQRES 5 K 164 ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU
SEQRES 6 K 164 VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL
SEQRES 7 K 164 LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE
SEQRES 8 K 164 GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER
SEQRES 9 K 164 LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU
SEQRES 10 K 164 THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA
SEQRES 11 K 164 LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO
SEQRES 12 K 164 ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR
SEQRES 13 K 164 PHE PHE GLY ALA LEU LYS LEU LEU
SEQRES 1 L 164 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 L 164 VAL GLN GLY PRO GLU GLU THR VAL THR GLN ASP CYS LEU
SEQRES 3 L 164 GLN LEU ILE ALA ASP SER GLU THR PRO THR ILE GLN LYS
SEQRES 4 L 164 GLY SER TYR THR PHE VAL PRO TRP LEU LEU SER PHE LYS
SEQRES 5 L 164 ARG GLY SER ALA LEU GLU GLU LYS GLU ASN LYS ILE LEU
SEQRES 6 L 164 VAL LYS GLU THR GLY TYR PHE PHE ILE TYR GLY GLN VAL
SEQRES 7 L 164 LEU TYR THR ASP LYS THR TYR ALA MET GLY HIS LEU ILE
SEQRES 8 L 164 GLN ARG LYS LYS VAL ALA VAL PHE GLY ASP GLU LEU SER
SEQRES 9 L 164 LEU VAL THR LEU PHE ARG CYS ILE GLN ASN MET PRO GLU
SEQRES 10 L 164 THR LEU PRO ASN ASN SER CYS TYR SER ALA GLY ILE ALA
SEQRES 11 L 164 LYS LEU GLU GLU GLY ASP GLU LEU GLN LEU ALA ILE PRO
SEQRES 12 L 164 ARG GLU ASN ALA GLN ILE SER LEU ASP GLY ASP VAL THR
SEQRES 13 L 164 PHE PHE GLY ALA LEU LYS LEU LEU
SEQRES 1 M 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 M 225 PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY
SEQRES 3 M 225 GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 M 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 M 225 PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN
SEQRES 6 M 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR
SEQRES 7 M 225 ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 M 225 ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU
SEQRES 9 M 225 PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR
SEQRES 10 M 225 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 M 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 M 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 M 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 M 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 M 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 M 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 M 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 M 225 GLU PRO LYS SER
SEQRES 1 N 214 SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA
SEQRES 2 N 214 LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER
SEQRES 3 N 214 LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 N 214 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN
SEQRES 5 N 214 ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER
SEQRES 6 N 214 SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN
SEQRES 7 N 214 ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP
SEQRES 8 N 214 SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU
SEQRES 9 N 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 N 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 N 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 N 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 N 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 N 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 N 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 N 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 N 214 ALA PRO THR GLU CYS SER
SEQRES 1 O 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 O 225 PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY
SEQRES 3 O 225 GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 O 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 O 225 PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN
SEQRES 6 O 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR
SEQRES 7 O 225 ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 O 225 ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU
SEQRES 9 O 225 PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR
SEQRES 10 O 225 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 O 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 O 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 O 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 O 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 O 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 O 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 O 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 O 225 GLU PRO LYS SER
SEQRES 1 P 214 SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA
SEQRES 2 P 214 LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER
SEQRES 3 P 214 LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 P 214 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN
SEQRES 5 P 214 ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER
SEQRES 6 P 214 SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN
SEQRES 7 P 214 ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP
SEQRES 8 P 214 SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU
SEQRES 9 P 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 P 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 P 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 P 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 P 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 P 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 P 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 P 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 P 214 ALA PRO THR GLU CYS SER
SEQRES 1 Q 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 Q 225 PRO GLY SER SER VAL ARG VAL SER CYS LYS ALA SER GLY
SEQRES 3 Q 225 GLY THR PHE ASN ASN ASN ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 Q 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 Q 225 PRO MET PHE GLY THR ALA LYS TYR SER GLN ASN PHE GLN
SEQRES 6 Q 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR GLY THR
SEQRES 7 Q 225 ALA SER MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 Q 225 ALA VAL TYR TYR CYS ALA ARG SER ARG ASP LEU LEU LEU
SEQRES 9 Q 225 PHE PRO HIS HIS ALA LEU SER PRO TRP GLY ARG GLY THR
SEQRES 10 Q 225 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 Q 225 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 Q 225 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 Q 225 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 Q 225 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 Q 225 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 Q 225 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 Q 225 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 Q 225 GLU PRO LYS SER
SEQRES 1 R 214 SER SER GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA
SEQRES 2 R 214 LEU GLY GLN THR VAL ARG VAL THR CYS GLN GLY ASP SER
SEQRES 3 R 214 LEU ARG SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 R 214 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN
SEQRES 5 R 214 ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SER SER
SEQRES 6 R 214 SER GLY ASN THR ALA SER LEU THR ILE THR GLY ALA GLN
SEQRES 7 R 214 ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER ARG ASP
SEQRES 8 R 214 SER SER GLY ASN HIS TRP VAL PHE GLY GLY GLY THR GLU
SEQRES 9 R 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 R 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 R 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 R 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 R 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 R 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 R 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 R 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 R 214 ALA PRO THR GLU CYS SER
FORMUL 19 HOH *270(H2 O)
HELIX 1 AA1 ARG D 87 THR D 91 5 5
HELIX 2 AA2 SER D 166 ALA D 168 5 3
HELIX 3 AA3 ASP E 25 SER E 29 5 5
HELIX 4 AA4 GLN E 78 GLU E 82 5 5
HELIX 5 AA5 SER E 123 ALA E 129 1 7
HELIX 6 AA6 THR E 183 HIS E 190 1 8
HELIX 7 AA7 ARG F 87 THR F 91 5 5
HELIX 8 AA8 SER F 197 LEU F 199 5 3
HELIX 9 AA9 ASP G 25 SER G 29 5 5
HELIX 10 AB1 GLN G 78 GLU G 82 5 5
HELIX 11 AB2 SER G 123 ALA G 129 1 7
HELIX 12 AB3 THR G 183 HIS G 190 1 8
HELIX 13 AB4 GLN H 62 GLN H 65 5 4
HELIX 14 AB5 ARG H 87 THR H 91 5 5
HELIX 15 AB6 LYS H 211 ASN H 214 5 4
HELIX 16 AB7 ASP I 25 SER I 29 5 5
HELIX 17 AB8 GLN I 78 GLU I 82 5 5
HELIX 18 AB9 SER I 123 ALA I 129 1 7
HELIX 19 AC1 THR I 183 SER I 189 1 7
HELIX 20 AC2 ARG M 87 THR M 91 5 5
HELIX 21 AC3 PRO M 195 LEU M 199 5 5
HELIX 22 AC4 ASP N 25 SER N 29 5 5
HELIX 23 AC5 GLN N 78 GLU N 82 5 5
HELIX 24 AC6 SER N 123 ALA N 129 1 7
HELIX 25 AC7 THR N 183 HIS N 190 1 8
HELIX 26 AC8 GLN O 62 GLN O 65 5 4
HELIX 27 AC9 ARG O 87 THR O 91 5 5
HELIX 28 AD1 ASP P 25 SER P 29 5 5
HELIX 29 AD2 GLN P 78 GLU P 82 5 5
HELIX 30 AD3 SER P 123 ALA P 129 1 7
HELIX 31 AD4 THR P 183 HIS P 190 1 8
HELIX 32 AD5 ARG Q 87 THR Q 91 5 5
HELIX 33 AD6 ASP R 25 SER R 29 5 5
HELIX 34 AD7 GLN R 78 GLU R 82 5 5
HELIX 35 AD8 SER R 123 ALA R 129 1 7
HELIX 36 AD9 THR R 183 HIS R 190 1 8
SHEET 1 AA1 5 TRP A 168 ARG A 174 0
SHEET 2 AA1 5 CYS A 146 ALA A 151 -1 N CYS A 146 O ARG A 174
SHEET 3 AA1 5 PHE A 278 LYS A 283 -1 O PHE A 279 N LEU A 149
SHEET 4 AA1 5 GLY A 191 TYR A 201 -1 N TYR A 196 O GLY A 280
SHEET 5 AA1 5 ASN A 243 LEU A 253 -1 O ALA A 251 N PHE A 193
SHEET 1 AA2 5 TRP A 168 ARG A 174 0
SHEET 2 AA2 5 CYS A 146 ALA A 151 -1 N CYS A 146 O ARG A 174
SHEET 3 AA2 5 PHE A 278 LYS A 283 -1 O PHE A 279 N LEU A 149
SHEET 4 AA2 5 GLY A 191 TYR A 201 -1 N TYR A 196 O GLY A 280
SHEET 5 AA2 5 ILE A 270 SER A 271 -1 O SER A 271 N LEU A 200
SHEET 1 AA3 5 ILE A 158 LYS A 160 0
SHEET 2 AA3 5 TYR A 163 PHE A 165 -1 O PHE A 165 N ILE A 158
SHEET 3 AA3 5 GLU A 258 ILE A 263 -1 O ILE A 263 N THR A 164
SHEET 4 AA3 5 LYS A 184 VAL A 187 -1 N ILE A 185 O LEU A 259
SHEET 5 AA3 5 LEU A 178 LYS A 181 -1 N GLU A 179 O LEU A 186
SHEET 1 AA4 5 ILE A 158 LYS A 160 0
SHEET 2 AA4 5 TYR A 163 PHE A 165 -1 O PHE A 165 N ILE A 158
SHEET 3 AA4 5 GLU A 258 ILE A 263 -1 O ILE A 263 N THR A 164
SHEET 4 AA4 5 ALA A 207 LYS A 215 -1 N LEU A 211 O ALA A 262
SHEET 5 AA4 5 LEU A 226 ASN A 235 -1 O VAL A 227 N ARG A 214
SHEET 1 AA5 5 TRP B 168 ARG B 174 0
SHEET 2 AA5 5 CYS B 146 ALA B 151 -1 N ILE B 150 O LEU B 169
SHEET 3 AA5 5 PHE B 278 LYS B 283 -1 O PHE B 279 N LEU B 149
SHEET 4 AA5 5 GLY B 191 TYR B 201 -1 N TYR B 196 O GLY B 280
SHEET 5 AA5 5 ASN B 243 LEU B 253 -1 O GLY B 249 N ILE B 195
SHEET 1 AA6 5 ILE B 158 LYS B 160 0
SHEET 2 AA6 5 TYR B 163 PHE B 165 -1 O PHE B 165 N ILE B 158
SHEET 3 AA6 5 GLU B 258 ILE B 263 -1 O ILE B 263 N THR B 164
SHEET 4 AA6 5 LYS B 184 VAL B 187 -1 N ILE B 185 O LEU B 259
SHEET 5 AA6 5 LEU B 178 LYS B 181 -1 N GLU B 179 O LEU B 186
SHEET 1 AA7 5 ILE B 158 LYS B 160 0
SHEET 2 AA7 5 TYR B 163 PHE B 165 -1 O PHE B 165 N ILE B 158
SHEET 3 AA7 5 GLU B 258 ILE B 263 -1 O ILE B 263 N THR B 164
SHEET 4 AA7 5 ALA B 207 LYS B 215 -1 N LYS B 215 O GLU B 258
SHEET 5 AA7 5 LEU B 226 ASN B 235 -1 O LEU B 229 N ILE B 212
SHEET 1 AA8 5 TRP C 168 ARG C 174 0
SHEET 2 AA8 5 CYS C 146 ALA C 151 -1 N CYS C 146 O ARG C 174
SHEET 3 AA8 5 PHE C 278 LYS C 283 -1 O PHE C 279 N LEU C 149
SHEET 4 AA8 5 GLY C 191 TYR C 201 -1 N PHE C 194 O LEU C 282
SHEET 5 AA8 5 ASN C 243 LEU C 253 -1 O GLY C 249 N ILE C 195
SHEET 1 AA9 5 ILE C 158 LYS C 160 0
SHEET 2 AA9 5 TYR C 163 PHE C 165 -1 O PHE C 165 N ILE C 158
SHEET 3 AA9 5 GLU C 258 ILE C 263 -1 O ILE C 263 N THR C 164
SHEET 4 AA9 5 LYS C 184 VAL C 187 -1 N ILE C 185 O LEU C 259
SHEET 5 AA9 5 LEU C 178 LYS C 181 -1 N GLU C 179 O LEU C 186
SHEET 1 AB1 5 ILE C 158 LYS C 160 0
SHEET 2 AB1 5 TYR C 163 PHE C 165 -1 O PHE C 165 N ILE C 158
SHEET 3 AB1 5 GLU C 258 ILE C 263 -1 O ILE C 263 N THR C 164
SHEET 4 AB1 5 ALA C 207 LYS C 215 -1 N LEU C 211 O ALA C 262
SHEET 5 AB1 5 LEU C 226 ASN C 235 -1 O VAL C 227 N ARG C 214
SHEET 1 AB2 4 GLN D 3 GLN D 6 0
SHEET 2 AB2 4 VAL D 18 SER D 25 -1 O LYS D 23 N GLN D 5
SHEET 3 AB2 4 THR D 78 LEU D 83 -1 O MET D 81 N VAL D 20
SHEET 4 AB2 4 VAL D 68 ASP D 73 -1 N ASP D 73 O THR D 78
SHEET 1 AB3 6 GLU D 10 LYS D 12 0
SHEET 2 AB3 6 THR D 117 VAL D 121 1 O THR D 120 N LYS D 12
SHEET 3 AB3 6 ALA D 92 ALA D 97 -1 N ALA D 92 O VAL D 119
SHEET 4 AB3 6 ILE D 34 GLN D 39 -1 N VAL D 37 O TYR D 95
SHEET 5 AB3 6 LEU D 45 ILE D 51 -1 O GLY D 49 N TRP D 36
SHEET 6 AB3 6 LYS D 59 TYR D 60 -1 O LYS D 59 N GLY D 50
SHEET 1 AB4 4 SER D 130 LEU D 134 0
SHEET 2 AB4 4 ALA D 146 TYR D 155 -1 O LEU D 151 N PHE D 132
SHEET 3 AB4 4 TYR D 186 VAL D 194 -1 O TYR D 186 N TYR D 155
SHEET 4 AB4 4 VAL D 173 THR D 175 -1 N HIS D 174 O VAL D 191
SHEET 1 AB5 4 SER D 130 LEU D 134 0
SHEET 2 AB5 4 ALA D 146 TYR D 155 -1 O LEU D 151 N PHE D 132
SHEET 3 AB5 4 TYR D 186 VAL D 194 -1 O TYR D 186 N TYR D 155
SHEET 4 AB5 4 VAL D 179 LEU D 180 -1 N VAL D 179 O SER D 187
SHEET 1 AB6 3 THR D 161 TRP D 164 0
SHEET 2 AB6 3 ILE D 205 HIS D 210 -1 O ASN D 207 N SER D 163
SHEET 3 AB6 3 THR D 215 LYS D 220 -1 O VAL D 217 N VAL D 208
SHEET 1 AB7 4 THR E 5 GLN E 6 0
SHEET 2 AB7 4 VAL E 18 GLN E 23 -1 O GLN E 23 N THR E 5
SHEET 3 AB7 4 THR E 69 ILE E 74 -1 O ALA E 70 N CYS E 22
SHEET 4 AB7 4 PHE E 61 SER E 66 -1 N SER E 62 O THR E 73
SHEET 1 AB8 5 ALA E 9 ALA E 13 0
SHEET 2 AB8 5 THR E 103 LEU E 108 1 O GLU E 104 N VAL E 10
SHEET 3 AB8 5 ASP E 84 SER E 89 -1 N TYR E 85 O THR E 103
SHEET 4 AB8 5 SER E 33 GLN E 37 -1 N SER E 33 O SER E 88
SHEET 5 AB8 5 VAL E 44 TYR E 48 -1 O VAL E 44 N GLN E 36
SHEET 1 AB9 4 ALA E 9 ALA E 13 0
SHEET 2 AB9 4 THR E 103 LEU E 108 1 O GLU E 104 N VAL E 10
SHEET 3 AB9 4 ASP E 84 SER E 89 -1 N TYR E 85 O THR E 103
SHEET 4 AB9 4 VAL E 98 PHE E 99 -1 O VAL E 98 N SER E 89
SHEET 1 AC1 4 SER E 116 PHE E 120 0
SHEET 2 AC1 4 ALA E 132 PHE E 141 -1 O LEU E 137 N THR E 118
SHEET 3 AC1 4 TYR E 174 LEU E 182 -1 O LEU E 182 N ALA E 132
SHEET 4 AC1 4 VAL E 161 THR E 163 -1 N GLU E 162 O TYR E 179
SHEET 1 AC2 4 SER E 116 PHE E 120 0
SHEET 2 AC2 4 ALA E 132 PHE E 141 -1 O LEU E 137 N THR E 118
SHEET 3 AC2 4 TYR E 174 LEU E 182 -1 O LEU E 182 N ALA E 132
SHEET 4 AC2 4 SER E 167 LYS E 168 -1 N SER E 167 O ALA E 175
SHEET 1 AC3 4 SER E 155 PRO E 156 0
SHEET 2 AC3 4 THR E 147 ALA E 152 -1 N ALA E 152 O SER E 155
SHEET 3 AC3 4 TYR E 193 HIS E 199 -1 O GLN E 196 N ALA E 149
SHEET 4 AC3 4 SER E 202 VAL E 208 -1 O VAL E 204 N VAL E 197
SHEET 1 AC4 4 LEU F 4 GLN F 6 0
SHEET 2 AC4 4 VAL F 18 ALA F 24 -1 O LYS F 23 N GLN F 5
SHEET 3 AC4 4 THR F 78 LEU F 83 -1 O ALA F 79 N CYS F 22
SHEET 4 AC4 4 VAL F 68 ASP F 73 -1 N ALA F 69 O GLU F 82
SHEET 1 AC5 6 GLU F 10 LYS F 12 0
SHEET 2 AC5 6 THR F 117 VAL F 121 1 O THR F 120 N LYS F 12
SHEET 3 AC5 6 ALA F 92 SER F 99 -1 N ALA F 92 O VAL F 119
SHEET 4 AC5 6 ALA F 33 GLN F 39 -1 N ALA F 33 O SER F 99
SHEET 5 AC5 6 GLU F 46 ILE F 51 -1 O ILE F 51 N ILE F 34
SHEET 6 AC5 6 LYS F 59 TYR F 60 -1 O LYS F 59 N GLY F 50
SHEET 1 AC6 4 SER F 130 LEU F 134 0
SHEET 2 AC6 4 THR F 145 TYR F 155 -1 O LEU F 151 N PHE F 132
SHEET 3 AC6 4 TYR F 186 PRO F 195 -1 O LEU F 188 N VAL F 152
SHEET 4 AC6 4 VAL F 173 THR F 175 -1 N HIS F 174 O VAL F 191
SHEET 1 AC7 4 SER F 130 LEU F 134 0
SHEET 2 AC7 4 THR F 145 TYR F 155 -1 O LEU F 151 N PHE F 132
SHEET 3 AC7 4 TYR F 186 PRO F 195 -1 O LEU F 188 N VAL F 152
SHEET 4 AC7 4 VAL F 179 LEU F 180 -1 N VAL F 179 O SER F 187
SHEET 1 AC8 3 THR F 161 TRP F 164 0
SHEET 2 AC8 3 TYR F 204 HIS F 210 -1 O ASN F 207 N SER F 163
SHEET 3 AC8 3 THR F 215 VAL F 221 -1 O VAL F 221 N TYR F 204
SHEET 1 AC9 4 THR G 5 GLN G 6 0
SHEET 2 AC9 4 VAL G 18 GLN G 23 -1 O GLN G 23 N THR G 5
SHEET 3 AC9 4 THR G 69 ILE G 74 -1 O ALA G 70 N CYS G 22
SHEET 4 AC9 4 PHE G 61 SER G 66 -1 N SER G 62 O THR G 73
SHEET 1 AD1 5 ALA G 9 ALA G 13 0
SHEET 2 AD1 5 THR G 103 LEU G 108 1 O LEU G 108 N VAL G 12
SHEET 3 AD1 5 ASP G 84 SER G 89 -1 N TYR G 85 O THR G 103
SHEET 4 AD1 5 SER G 33 GLN G 37 -1 N GLN G 37 O ASP G 84
SHEET 5 AD1 5 VAL G 44 ILE G 47 -1 O VAL G 46 N TRP G 34
SHEET 1 AD2 4 ALA G 9 ALA G 13 0
SHEET 2 AD2 4 THR G 103 LEU G 108 1 O LEU G 108 N VAL G 12
SHEET 3 AD2 4 ASP G 84 SER G 89 -1 N TYR G 85 O THR G 103
SHEET 4 AD2 4 VAL G 98 PHE G 99 -1 O VAL G 98 N SER G 89
SHEET 1 AD3 4 SER G 116 PHE G 120 0
SHEET 2 AD3 4 ALA G 132 PHE G 141 -1 O LEU G 137 N THR G 118
SHEET 3 AD3 4 TYR G 174 LEU G 182 -1 O LEU G 182 N ALA G 132
SHEET 4 AD3 4 VAL G 161 THR G 163 -1 N GLU G 162 O TYR G 179
SHEET 1 AD4 4 SER G 116 PHE G 120 0
SHEET 2 AD4 4 ALA G 132 PHE G 141 -1 O LEU G 137 N THR G 118
SHEET 3 AD4 4 TYR G 174 LEU G 182 -1 O LEU G 182 N ALA G 132
SHEET 4 AD4 4 SER G 167 LYS G 168 -1 N SER G 167 O ALA G 175
SHEET 1 AD5 4 SER G 155 PRO G 156 0
SHEET 2 AD5 4 THR G 147 ALA G 152 -1 N ALA G 152 O SER G 155
SHEET 3 AD5 4 TYR G 193 HIS G 199 -1 O THR G 198 N THR G 147
SHEET 4 AD5 4 SER G 202 VAL G 208 -1 O VAL G 208 N TYR G 193
SHEET 1 AD6 4 LEU H 4 GLN H 6 0
SHEET 2 AD6 4 CYS H 22 ALA H 24 -1 O LYS H 23 N GLN H 5
SHEET 3 AD6 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22
SHEET 4 AD6 4 VAL H 18 ARG H 19 -1 N VAL H 18 O LEU H 83
SHEET 1 AD7 4 LEU H 4 GLN H 6 0
SHEET 2 AD7 4 CYS H 22 ALA H 24 -1 O LYS H 23 N GLN H 5
SHEET 3 AD7 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22
SHEET 4 AD7 4 VAL H 68 ASP H 73 -1 N ALA H 69 O GLU H 82
SHEET 1 AD8 6 GLU H 10 LYS H 12 0
SHEET 2 AD8 6 THR H 117 VAL H 121 1 O THR H 120 N LYS H 12
SHEET 3 AD8 6 ALA H 92 ARG H 100 -1 N TYR H 94 O THR H 117
SHEET 4 AD8 6 ASN H 32 GLN H 39 -1 N VAL H 37 O TYR H 95
SHEET 5 AD8 6 LEU H 45 ILE H 51 -1 O ILE H 51 N ILE H 34
SHEET 6 AD8 6 LYS H 59 TYR H 60 -1 O LYS H 59 N GLY H 50
SHEET 1 AD9 4 SER H 130 LEU H 134 0
SHEET 2 AD9 4 ALA H 146 TYR H 155 -1 O LYS H 153 N SER H 130
SHEET 3 AD9 4 TYR H 186 VAL H 194 -1 O TYR H 186 N TYR H 155
SHEET 4 AD9 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191
SHEET 1 AE1 4 SER H 130 LEU H 134 0
SHEET 2 AE1 4 ALA H 146 TYR H 155 -1 O LYS H 153 N SER H 130
SHEET 3 AE1 4 TYR H 186 VAL H 194 -1 O TYR H 186 N TYR H 155
SHEET 4 AE1 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187
SHEET 1 AE2 3 THR H 161 TRP H 164 0
SHEET 2 AE2 3 TYR H 204 HIS H 210 -1 O ASN H 209 N THR H 161
SHEET 3 AE2 3 THR H 215 VAL H 221 -1 O VAL H 221 N TYR H 204
SHEET 1 AE3 4 THR I 5 GLN I 6 0
SHEET 2 AE3 4 VAL I 18 GLN I 23 -1 O GLN I 23 N THR I 5
SHEET 3 AE3 4 THR I 69 ILE I 74 -1 O ALA I 70 N CYS I 22
SHEET 4 AE3 4 PHE I 61 SER I 62 -1 N SER I 62 O THR I 73
SHEET 1 AE4 4 THR I 5 GLN I 6 0
SHEET 2 AE4 4 VAL I 18 GLN I 23 -1 O GLN I 23 N THR I 5
SHEET 3 AE4 4 THR I 69 ILE I 74 -1 O ALA I 70 N CYS I 22
SHEET 4 AE4 4 SER I 65 SER I 66 -1 N SER I 66 O THR I 69
SHEET 1 AE5 5 ALA I 9 ALA I 13 0
SHEET 2 AE5 5 THR I 103 LEU I 108 1 O LEU I 108 N VAL I 12
SHEET 3 AE5 5 ASP I 84 SER I 89 -1 N TYR I 85 O THR I 103
SHEET 4 AE5 5 SER I 33 GLN I 37 -1 N GLN I 37 O ASP I 84
SHEET 5 AE5 5 VAL I 44 ILE I 47 -1 O VAL I 44 N GLN I 36
SHEET 1 AE6 4 ALA I 9 ALA I 13 0
SHEET 2 AE6 4 THR I 103 LEU I 108 1 O LEU I 108 N VAL I 12
SHEET 3 AE6 4 ASP I 84 SER I 89 -1 N TYR I 85 O THR I 103
SHEET 4 AE6 4 VAL I 98 PHE I 99 -1 O VAL I 98 N SER I 89
SHEET 1 AE7 4 SER I 116 PHE I 120 0
SHEET 2 AE7 4 ALA I 132 PHE I 141 -1 O LEU I 137 N THR I 118
SHEET 3 AE7 4 TYR I 174 LEU I 182 -1 O ALA I 176 N ILE I 138
SHEET 4 AE7 4 VAL I 161 THR I 163 -1 N GLU I 162 O TYR I 179
SHEET 1 AE8 4 SER I 116 PHE I 120 0
SHEET 2 AE8 4 ALA I 132 PHE I 141 -1 O LEU I 137 N THR I 118
SHEET 3 AE8 4 TYR I 174 LEU I 182 -1 O ALA I 176 N ILE I 138
SHEET 4 AE8 4 SER I 167 LYS I 168 -1 N SER I 167 O ALA I 175
SHEET 1 AE9 4 SER I 155 PRO I 156 0
SHEET 2 AE9 4 THR I 147 ALA I 152 -1 N ALA I 152 O SER I 155
SHEET 3 AE9 4 TYR I 193 HIS I 199 -1 O THR I 198 N THR I 147
SHEET 4 AE9 4 SER I 202 VAL I 208 -1 O SER I 202 N HIS I 199
SHEET 1 AF1 5 TRP J 168 ARG J 174 0
SHEET 2 AF1 5 CYS J 146 ALA J 151 -1 N ILE J 150 O LEU J 169
SHEET 3 AF1 5 PHE J 278 LYS J 283 -1 O PHE J 279 N LEU J 149
SHEET 4 AF1 5 GLY J 191 TYR J 201 -1 N GLN J 198 O PHE J 278
SHEET 5 AF1 5 ASN J 243 LEU J 253 -1 O ASN J 243 N TYR J 201
SHEET 1 AF2 2 ILE J 158 LYS J 160 0
SHEET 2 AF2 2 TYR J 163 PHE J 165 -1 O PHE J 165 N ILE J 158
SHEET 1 AF3 5 LEU J 178 LYS J 181 0
SHEET 2 AF3 5 LYS J 184 VAL J 187 -1 O LEU J 186 N GLU J 179
SHEET 3 AF3 5 GLU J 258 ALA J 262 -1 O LEU J 259 N ILE J 185
SHEET 4 AF3 5 ALA J 207 LYS J 215 -1 N LEU J 211 O ALA J 262
SHEET 5 AF3 5 LEU J 226 ASN J 235 -1 O VAL J 227 N ARG J 214
SHEET 1 AF4 5 TRP K 168 ARG K 174 0
SHEET 2 AF4 5 CYS K 146 ALA K 151 -1 N CYS K 146 O ARG K 174
SHEET 3 AF4 5 PHE K 278 LYS K 283 -1 O PHE K 279 N LEU K 149
SHEET 4 AF4 5 GLY K 191 TYR K 201 -1 N TYR K 196 O GLY K 280
SHEET 5 AF4 5 ASN K 243 LEU K 253 -1 O ALA K 251 N PHE K 193
SHEET 1 AF5 2 ILE K 158 LYS K 160 0
SHEET 2 AF5 2 TYR K 163 PHE K 165 -1 O PHE K 165 N ILE K 158
SHEET 1 AF6 5 LEU K 178 LYS K 181 0
SHEET 2 AF6 5 LYS K 184 VAL K 187 -1 O LEU K 186 N GLU K 179
SHEET 3 AF6 5 GLU K 258 ALA K 262 -1 O LEU K 259 N ILE K 185
SHEET 4 AF6 5 ALA K 207 LYS K 215 -1 N LYS K 215 O GLU K 258
SHEET 5 AF6 5 LEU K 226 ASN K 235 -1 O VAL K 227 N ARG K 214
SHEET 1 AF7 5 TRP L 168 ARG L 174 0
SHEET 2 AF7 5 CYS L 146 ALA L 151 -1 N ILE L 150 O LEU L 169
SHEET 3 AF7 5 PHE L 278 LYS L 283 -1 O PHE L 279 N LEU L 149
SHEET 4 AF7 5 GLY L 191 TYR L 201 -1 N PHE L 194 O LEU L 282
SHEET 5 AF7 5 ASN L 243 LEU L 253 -1 O GLY L 249 N ILE L 195
SHEET 1 AF8 2 ILE L 158 LYS L 160 0
SHEET 2 AF8 2 TYR L 163 PHE L 165 -1 O PHE L 165 N ILE L 158
SHEET 1 AF9 5 LEU L 178 GLU L 180 0
SHEET 2 AF9 5 ILE L 185 VAL L 187 -1 O LEU L 186 N GLU L 179
SHEET 3 AF9 5 GLU L 258 ALA L 262 -1 O LEU L 259 N ILE L 185
SHEET 4 AF9 5 ALA L 207 LYS L 215 -1 N LEU L 211 O ALA L 262
SHEET 5 AF9 5 LEU L 226 ASN L 235 -1 O VAL L 227 N ARG L 214
SHEET 1 AG1 4 LEU M 4 GLN M 6 0
SHEET 2 AG1 4 VAL M 18 ALA M 24 -1 O LYS M 23 N GLN M 5
SHEET 3 AG1 4 THR M 78 LEU M 83 -1 O MET M 81 N VAL M 20
SHEET 4 AG1 4 VAL M 68 ASP M 73 -1 N ALA M 69 O GLU M 82
SHEET 1 AG2 6 VAL M 11 LYS M 12 0
SHEET 2 AG2 6 THR M 117 VAL M 121 1 O THR M 120 N LYS M 12
SHEET 3 AG2 6 ALA M 92 SER M 99 -1 N TYR M 94 O THR M 117
SHEET 4 AG2 6 ALA M 33 GLN M 39 -1 N ALA M 33 O SER M 99
SHEET 5 AG2 6 GLU M 46 ILE M 51 -1 O ILE M 51 N ILE M 34
SHEET 6 AG2 6 LYS M 59 TYR M 60 -1 O LYS M 59 N GLY M 50
SHEET 1 AG3 4 VAL M 11 LYS M 12 0
SHEET 2 AG3 4 THR M 117 VAL M 121 1 O THR M 120 N LYS M 12
SHEET 3 AG3 4 ALA M 92 SER M 99 -1 N TYR M 94 O THR M 117
SHEET 4 AG3 4 LEU M 110 TRP M 113 -1 O SER M 111 N ARG M 98
SHEET 1 AG4 4 SER M 130 LEU M 134 0
SHEET 2 AG4 4 ALA M 146 TYR M 155 -1 O LYS M 153 N SER M 130
SHEET 3 AG4 4 TYR M 186 VAL M 194 -1 O TYR M 186 N TYR M 155
SHEET 4 AG4 4 VAL M 173 THR M 175 -1 N HIS M 174 O VAL M 191
SHEET 1 AG5 4 SER M 130 LEU M 134 0
SHEET 2 AG5 4 ALA M 146 TYR M 155 -1 O LYS M 153 N SER M 130
SHEET 3 AG5 4 TYR M 186 VAL M 194 -1 O TYR M 186 N TYR M 155
SHEET 4 AG5 4 VAL M 179 LEU M 180 -1 N VAL M 179 O SER M 187
SHEET 1 AG6 3 THR M 161 TRP M 164 0
SHEET 2 AG6 3 TYR M 204 HIS M 210 -1 O ASN M 209 N THR M 161
SHEET 3 AG6 3 THR M 215 VAL M 221 -1 O THR M 215 N HIS M 210
SHEET 1 AG7 4 THR N 5 GLN N 6 0
SHEET 2 AG7 4 VAL N 18 GLN N 23 -1 O GLN N 23 N THR N 5
SHEET 3 AG7 4 THR N 69 ILE N 74 -1 O LEU N 72 N VAL N 20
SHEET 4 AG7 4 PHE N 61 SER N 66 -1 N SER N 66 O THR N 69
SHEET 1 AG8 5 ALA N 9 ALA N 13 0
SHEET 2 AG8 5 THR N 103 LEU N 108 1 O GLU N 104 N VAL N 10
SHEET 3 AG8 5 ALA N 83 SER N 89 -1 N ALA N 83 O LEU N 105
SHEET 4 AG8 5 SER N 33 GLN N 37 -1 N GLN N 37 O ASP N 84
SHEET 5 AG8 5 VAL N 44 TYR N 48 -1 O ILE N 47 N TRP N 34
SHEET 1 AG9 4 ALA N 9 ALA N 13 0
SHEET 2 AG9 4 THR N 103 LEU N 108 1 O GLU N 104 N VAL N 10
SHEET 3 AG9 4 ALA N 83 SER N 89 -1 N ALA N 83 O LEU N 105
SHEET 4 AG9 4 VAL N 98 PHE N 99 -1 O VAL N 98 N SER N 89
SHEET 1 AH1 4 SER N 116 PHE N 120 0
SHEET 2 AH1 4 ALA N 132 PHE N 141 -1 O LEU N 137 N THR N 118
SHEET 3 AH1 4 TYR N 174 LEU N 182 -1 O TYR N 174 N PHE N 141
SHEET 4 AH1 4 VAL N 161 THR N 163 -1 N GLU N 162 O TYR N 179
SHEET 1 AH2 4 SER N 116 PHE N 120 0
SHEET 2 AH2 4 ALA N 132 PHE N 141 -1 O LEU N 137 N THR N 118
SHEET 3 AH2 4 TYR N 174 LEU N 182 -1 O TYR N 174 N PHE N 141
SHEET 4 AH2 4 SER N 167 LYS N 168 -1 N SER N 167 O ALA N 175
SHEET 1 AH3 4 SER N 155 PRO N 156 0
SHEET 2 AH3 4 THR N 147 ALA N 152 -1 N ALA N 152 O SER N 155
SHEET 3 AH3 4 TYR N 193 HIS N 199 -1 O GLN N 196 N ALA N 149
SHEET 4 AH3 4 SER N 202 VAL N 208 -1 O VAL N 204 N VAL N 197
SHEET 1 AH4 4 GLN O 3 GLN O 6 0
SHEET 2 AH4 4 VAL O 18 SER O 25 -1 O LYS O 23 N GLN O 5
SHEET 3 AH4 4 THR O 78 LEU O 83 -1 O LEU O 83 N VAL O 18
SHEET 4 AH4 4 VAL O 68 ASP O 73 -1 N THR O 71 O SER O 80
SHEET 1 AH5 6 GLU O 10 LYS O 12 0
SHEET 2 AH5 6 THR O 117 VAL O 121 1 O THR O 120 N LYS O 12
SHEET 3 AH5 6 ALA O 92 SER O 99 -1 N TYR O 94 O THR O 117
SHEET 4 AH5 6 ALA O 33 GLN O 39 -1 N ALA O 33 O SER O 99
SHEET 5 AH5 6 LEU O 45 ILE O 51 -1 O GLY O 49 N TRP O 36
SHEET 6 AH5 6 LYS O 59 TYR O 60 -1 O LYS O 59 N GLY O 50
SHEET 1 AH6 4 SER O 130 LEU O 134 0
SHEET 2 AH6 4 ALA O 146 TYR O 155 -1 O GLY O 149 N LEU O 134
SHEET 3 AH6 4 TYR O 186 VAL O 194 -1 O LEU O 188 N VAL O 152
SHEET 4 AH6 4 VAL O 173 THR O 175 -1 N HIS O 174 O VAL O 191
SHEET 1 AH7 4 SER O 130 LEU O 134 0
SHEET 2 AH7 4 ALA O 146 TYR O 155 -1 O GLY O 149 N LEU O 134
SHEET 3 AH7 4 TYR O 186 VAL O 194 -1 O LEU O 188 N VAL O 152
SHEET 4 AH7 4 VAL O 179 LEU O 180 -1 N VAL O 179 O SER O 187
SHEET 1 AH8 3 THR O 161 TRP O 164 0
SHEET 2 AH8 3 ILE O 205 HIS O 210 -1 O ASN O 207 N SER O 163
SHEET 3 AH8 3 THR O 215 LYS O 220 -1 O THR O 215 N HIS O 210
SHEET 1 AH9 4 THR P 5 GLN P 6 0
SHEET 2 AH9 4 VAL P 18 GLN P 23 -1 O GLN P 23 N THR P 5
SHEET 3 AH9 4 THR P 69 ILE P 74 -1 O ALA P 70 N CYS P 22
SHEET 4 AH9 4 PHE P 61 SER P 66 -1 N SER P 64 O SER P 71
SHEET 1 AI1 5 ALA P 9 ALA P 13 0
SHEET 2 AI1 5 THR P 103 LEU P 108 1 O LEU P 108 N VAL P 12
SHEET 3 AI1 5 ASP P 84 SER P 89 -1 N TYR P 85 O THR P 103
SHEET 4 AI1 5 SER P 33 GLN P 37 -1 N GLN P 37 O ASP P 84
SHEET 5 AI1 5 VAL P 44 ILE P 47 -1 O ILE P 47 N TRP P 34
SHEET 1 AI2 4 ALA P 9 ALA P 13 0
SHEET 2 AI2 4 THR P 103 LEU P 108 1 O LEU P 108 N VAL P 12
SHEET 3 AI2 4 ASP P 84 SER P 89 -1 N TYR P 85 O THR P 103
SHEET 4 AI2 4 VAL P 98 PHE P 99 -1 O VAL P 98 N SER P 89
SHEET 1 AI3 4 SER P 116 PHE P 120 0
SHEET 2 AI3 4 ALA P 132 PHE P 141 -1 O LEU P 137 N THR P 118
SHEET 3 AI3 4 TYR P 174 LEU P 182 -1 O ALA P 176 N ILE P 138
SHEET 4 AI3 4 VAL P 161 THR P 163 -1 N GLU P 162 O TYR P 179
SHEET 1 AI4 4 SER P 116 PHE P 120 0
SHEET 2 AI4 4 ALA P 132 PHE P 141 -1 O LEU P 137 N THR P 118
SHEET 3 AI4 4 TYR P 174 LEU P 182 -1 O ALA P 176 N ILE P 138
SHEET 4 AI4 4 SER P 167 LYS P 168 -1 N SER P 167 O ALA P 175
SHEET 1 AI5 4 SER P 155 PRO P 156 0
SHEET 2 AI5 4 THR P 147 ALA P 152 -1 N ALA P 152 O SER P 155
SHEET 3 AI5 4 TYR P 193 HIS P 199 -1 O GLN P 196 N ALA P 149
SHEET 4 AI5 4 SER P 202 VAL P 208 -1 O VAL P 204 N VAL P 197
SHEET 1 AI6 4 LEU Q 4 GLN Q 6 0
SHEET 2 AI6 4 VAL Q 18 ALA Q 24 -1 O LYS Q 23 N GLN Q 5
SHEET 3 AI6 4 THR Q 78 LEU Q 83 -1 O MET Q 81 N VAL Q 20
SHEET 4 AI6 4 VAL Q 68 ASP Q 73 -1 N THR Q 71 O SER Q 80
SHEET 1 AI7 6 GLU Q 10 LYS Q 12 0
SHEET 2 AI7 6 THR Q 117 VAL Q 121 1 O THR Q 120 N GLU Q 10
SHEET 3 AI7 6 ALA Q 92 SER Q 99 -1 N ALA Q 92 O VAL Q 119
SHEET 4 AI7 6 ALA Q 33 GLN Q 39 -1 N ALA Q 33 O SER Q 99
SHEET 5 AI7 6 LEU Q 45 ILE Q 51 -1 O ILE Q 51 N ILE Q 34
SHEET 6 AI7 6 LYS Q 59 TYR Q 60 -1 O LYS Q 59 N GLY Q 50
SHEET 1 AI8 4 SER Q 130 LEU Q 134 0
SHEET 2 AI8 4 ALA Q 146 TYR Q 155 -1 O GLY Q 149 N LEU Q 134
SHEET 3 AI8 4 TYR Q 186 VAL Q 194 -1 O TYR Q 186 N TYR Q 155
SHEET 4 AI8 4 VAL Q 173 THR Q 175 -1 N HIS Q 174 O VAL Q 191
SHEET 1 AI9 4 SER Q 130 LEU Q 134 0
SHEET 2 AI9 4 ALA Q 146 TYR Q 155 -1 O GLY Q 149 N LEU Q 134
SHEET 3 AI9 4 TYR Q 186 VAL Q 194 -1 O TYR Q 186 N TYR Q 155
SHEET 4 AI9 4 VAL Q 179 LEU Q 180 -1 N VAL Q 179 O SER Q 187
SHEET 1 AJ1 3 THR Q 161 TRP Q 164 0
SHEET 2 AJ1 3 ILE Q 205 HIS Q 210 -1 O ASN Q 207 N SER Q 163
SHEET 3 AJ1 3 THR Q 215 LYS Q 220 -1 O VAL Q 217 N VAL Q 208
SHEET 1 AJ2 4 THR R 5 GLN R 6 0
SHEET 2 AJ2 4 VAL R 18 GLN R 23 -1 O GLN R 23 N THR R 5
SHEET 3 AJ2 4 THR R 69 ILE R 74 -1 O ALA R 70 N CYS R 22
SHEET 4 AJ2 4 PHE R 61 SER R 66 -1 N SER R 64 O SER R 71
SHEET 1 AJ3 5 ALA R 9 ALA R 13 0
SHEET 2 AJ3 5 THR R 103 LEU R 108 1 O LEU R 108 N VAL R 12
SHEET 3 AJ3 5 ASP R 84 SER R 89 -1 N TYR R 85 O THR R 103
SHEET 4 AJ3 5 SER R 33 GLN R 37 -1 N GLN R 37 O ASP R 84
SHEET 5 AJ3 5 VAL R 44 ILE R 47 -1 O VAL R 46 N TRP R 34
SHEET 1 AJ4 4 ALA R 9 ALA R 13 0
SHEET 2 AJ4 4 THR R 103 LEU R 108 1 O LEU R 108 N VAL R 12
SHEET 3 AJ4 4 ASP R 84 SER R 89 -1 N TYR R 85 O THR R 103
SHEET 4 AJ4 4 VAL R 98 PHE R 99 -1 O VAL R 98 N SER R 89
SHEET 1 AJ5 4 SER R 116 PHE R 120 0
SHEET 2 AJ5 4 ALA R 132 PHE R 141 -1 O LEU R 137 N THR R 118
SHEET 3 AJ5 4 TYR R 174 LEU R 182 -1 O LEU R 182 N ALA R 132
SHEET 4 AJ5 4 VAL R 161 THR R 163 -1 N GLU R 162 O TYR R 179
SHEET 1 AJ6 4 SER R 116 PHE R 120 0
SHEET 2 AJ6 4 ALA R 132 PHE R 141 -1 O LEU R 137 N THR R 118
SHEET 3 AJ6 4 TYR R 174 LEU R 182 -1 O LEU R 182 N ALA R 132
SHEET 4 AJ6 4 SER R 167 LYS R 168 -1 N SER R 167 O ALA R 175
SHEET 1 AJ7 4 SER R 155 PRO R 156 0
SHEET 2 AJ7 4 THR R 147 ALA R 152 -1 N ALA R 152 O SER R 155
SHEET 3 AJ7 4 TYR R 193 HIS R 199 -1 O GLN R 196 N ALA R 149
SHEET 4 AJ7 4 SER R 202 VAL R 208 -1 O SER R 202 N HIS R 199
SSBOND 1 CYS A 232 CYS A 245 1555 1555 2.07
SSBOND 2 CYS B 232 CYS B 245 1555 1555 2.06
SSBOND 3 CYS C 232 CYS C 245 1555 1555 2.07
SSBOND 4 CYS D 22 CYS D 96 1555 1555 2.04
SSBOND 5 CYS D 150 CYS D 206 1555 1555 2.03
SSBOND 6 CYS E 22 CYS E 87 1555 1555 2.04
SSBOND 7 CYS E 136 CYS E 195 1555 1555 2.05
SSBOND 8 CYS F 22 CYS F 96 1555 1555 2.03
SSBOND 9 CYS F 150 CYS F 206 1555 1555 2.03
SSBOND 10 CYS G 22 CYS G 87 1555 1555 2.03
SSBOND 11 CYS G 136 CYS G 195 1555 1555 2.05
SSBOND 12 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 13 CYS H 150 CYS H 206 1555 1555 2.04
SSBOND 14 CYS I 22 CYS I 87 1555 1555 2.05
SSBOND 15 CYS I 136 CYS I 195 1555 1555 2.05
SSBOND 16 CYS J 232 CYS J 245 1555 1555 2.06
SSBOND 17 CYS K 232 CYS K 245 1555 1555 2.06
SSBOND 18 CYS L 232 CYS L 245 1555 1555 2.06
SSBOND 19 CYS M 22 CYS M 96 1555 1555 2.03
SSBOND 20 CYS M 150 CYS M 206 1555 1555 2.02
SSBOND 21 CYS N 22 CYS N 87 1555 1555 2.04
SSBOND 22 CYS N 136 CYS N 195 1555 1555 2.05
SSBOND 23 CYS O 22 CYS O 96 1555 1555 2.04
SSBOND 24 CYS O 150 CYS O 206 1555 1555 2.05
SSBOND 25 CYS P 22 CYS P 87 1555 1555 2.04
SSBOND 26 CYS P 136 CYS P 195 1555 1555 2.04
SSBOND 27 CYS Q 22 CYS Q 96 1555 1555 2.05
SSBOND 28 CYS Q 150 CYS Q 206 1555 1555 2.02
SSBOND 29 CYS R 22 CYS R 87 1555 1555 2.04
SSBOND 30 CYS R 136 CYS R 195 1555 1555 2.04
CISPEP 1 SER D 111 PRO D 112 0 -3.39
CISPEP 2 PHE D 156 PRO D 157 0 -5.57
CISPEP 3 GLU D 158 PRO D 159 0 -5.21
CISPEP 4 TYR E 142 PRO E 143 0 -1.39
CISPEP 5 SER F 111 PRO F 112 0 1.08
CISPEP 6 PHE F 156 PRO F 157 0 -5.50
CISPEP 7 GLU F 158 PRO F 159 0 1.72
CISPEP 8 TYR G 142 PRO G 143 0 -1.64
CISPEP 9 SER H 111 PRO H 112 0 -3.55
CISPEP 10 PHE H 156 PRO H 157 0 -17.59
CISPEP 11 GLU H 158 PRO H 159 0 -1.13
CISPEP 12 TYR I 142 PRO I 143 0 -2.60
CISPEP 13 SER M 111 PRO M 112 0 -1.16
CISPEP 14 PHE M 156 PRO M 157 0 -4.67
CISPEP 15 GLU M 158 PRO M 159 0 -2.71
CISPEP 16 TYR N 142 PRO N 143 0 -0.95
CISPEP 17 SER O 111 PRO O 112 0 -5.33
CISPEP 18 PHE O 156 PRO O 157 0 -0.51
CISPEP 19 GLU O 158 PRO O 159 0 -5.95
CISPEP 20 TYR P 142 PRO P 143 0 -2.00
CISPEP 21 SER Q 111 PRO Q 112 0 -6.16
CISPEP 22 PHE Q 156 PRO Q 157 0 -1.93
CISPEP 23 GLU Q 158 PRO Q 159 0 4.43
CISPEP 24 TYR R 142 PRO R 143 0 -4.01
CRYST1 135.687 135.499 138.180 90.00 91.88 90.00 P 1 21 1 12
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 0.007370 0.000000 0.000242 0.00000
SCALE2 0.000000 0.007380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007241 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
