HEADER HYDROLASE 18-AUG-10 2XOK
TITLE REFINED STRUCTURE OF YEAST F1C10 ATPASE COMPLEX TO 3 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL;
COMPND 6 CHAIN: D, E, F;
COMPND 7 EC: 3.6.1.34;
COMPND 8 MOL_ID: 3;
COMPND 9 MOLECULE: ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL;
COMPND 10 CHAIN: G;
COMPND 11 SYNONYM: F-ATPASE GAMMA SUBUNIT;
COMPND 12 MOL_ID: 4;
COMPND 13 MOLECULE: ATP SYNTHASE;
COMPND 14 CHAIN: H;
COMPND 15 MOL_ID: 5;
COMPND 16 MOLECULE: ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT;
COMPND 17 CHAIN: I;
COMPND 18 FRAGMENT: RESIDUES 2-62;
COMPND 19 MOL_ID: 6;
COMPND 20 MOLECULE: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL;
COMPND 21 CHAIN: K, L, M, N, O, P, Q, R, S, T;
COMPND 22 SYNONYM: LIPID-BINDING PROTEIN, OLIGOMYCIN RESISTANCE PROTEIN 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 ORGANELLE: MITOCHONDRION;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 9 ORGANISM_TAXID: 4932;
SOURCE 10 ORGANELLE: MITOCHONDRION;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 ORGANELLE: MITOCHONDRION;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 19 ORGANISM_TAXID: 4932;
SOURCE 20 OTHER_DETAILS: MITOCHONDRION;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 ORGANELLE: MITOCHONDRION;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 4932;
SOURCE 30 ORGANELLE: MITOCHONDRION
KEYWDS HYDROLASE, ATP-BINDING, F(O), F(1), ATP SYNTHASE, MITOCHONDRIA, INNER
KEYWDS 2 MEMBRANE, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.STOCK,A.G.W LESLIE,J.E.WALKER
REVDAT 4 20-DEC-23 2XOK 1 REMARK LINK
REVDAT 3 09-OCT-19 2XOK 1 JRNL
REVDAT 2 08-MAY-19 2XOK 1 REMARK
REVDAT 1 22-SEP-10 2XOK 0
JRNL AUTH D.STOCK,A.G.LESLIE,J.E.WALKER
JRNL TITL MOLECULAR ARCHITECTURE OF THE ROTARY MOTOR IN ATP SYNTHASE.
JRNL REF SCIENCE V. 286 1700 1999
JRNL REFN ISSN 0036-8075
JRNL PMID 10576729
JRNL DOI 10.1126/SCIENCE.286.5445.1700
REMARK 2
REMARK 2 RESOLUTION. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.8
REMARK 3 NUMBER OF REFLECTIONS : 91603
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2352
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) : 3.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.09
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4867
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 29953
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 116.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.54000
REMARK 3 B22 (A**2) : -6.25000
REMARK 3 B33 (A**2) : 2.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.94000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.486
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.357
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.376
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 30557 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 41439 ; 1.368 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3986 ; 6.010 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1147 ;37.576 ;24.368
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5190 ;20.207 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 173 ;17.071 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4952 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22461 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 15595 ; 0.227 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 21201 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1049 ; 0.150 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.197 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 19 ; 0.223 ; 0.200
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): 20196 ; 1.197 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31745 ; 2.265 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11270 ; 3.642 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9694 ; 6.072 ;10.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : K L M N O P Q R S T
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 K 3 K 38 2
REMARK 3 1 L 3 L 38 2
REMARK 3 1 M 3 M 38 2
REMARK 3 1 N 3 N 38 2
REMARK 3 1 O 3 O 38 2
REMARK 3 1 P 3 P 38 2
REMARK 3 1 Q 3 Q 38 2
REMARK 3 1 R 3 R 38 2
REMARK 3 1 S 3 S 38 2
REMARK 3 1 T 3 T 38 2
REMARK 3 2 K 53 K 72 2
REMARK 3 2 L 53 L 72 2
REMARK 3 2 M 53 M 72 2
REMARK 3 2 N 53 N 72 2
REMARK 3 2 O 53 O 72 2
REMARK 3 2 P 53 P 72 2
REMARK 3 2 Q 53 Q 72 2
REMARK 3 2 R 53 R 72 2
REMARK 3 2 S 53 S 72 2
REMARK 3 2 T 53 T 72 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 K (A): 224 ; 0.05 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 L (A): 224 ; 0.05 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 M (A): 224 ; 0.05 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 N (A): 224 ; 0.05 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 O (A): 224 ; 0.04 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 P (A): 224 ; 0.04 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 Q (A): 224 ; 0.04 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 R (A): 224 ; 0.03 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 S (A): 224 ; 0.05 ; 0.10
REMARK 3 TIGHT POSITIONAL 1 T (A): 224 ; 0.04 ; 0.10
REMARK 3 MEDIUM POSITIONAL 1 K (A): 163 ; 0.21 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 L (A): 163 ; 0.19 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 M (A): 163 ; 0.21 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 N (A): 163 ; 0.22 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 O (A): 163 ; 0.12 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 P (A): 163 ; 0.12 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 Q (A): 163 ; 0.11 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 R (A): 163 ; 0.12 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 S (A): 163 ; 0.19 ; 0.30
REMARK 3 MEDIUM POSITIONAL 1 T (A): 163 ; 0.19 ; 0.30
REMARK 3 TIGHT THERMAL 1 K (A**2): 224 ; 4.78 ; 20.00
REMARK 3 TIGHT THERMAL 1 L (A**2): 224 ; 5.47 ; 20.00
REMARK 3 TIGHT THERMAL 1 M (A**2): 224 ; 3.82 ; 20.00
REMARK 3 TIGHT THERMAL 1 N (A**2): 224 ; 2.57 ; 20.00
REMARK 3 TIGHT THERMAL 1 O (A**2): 224 ; 4.07 ; 20.00
REMARK 3 TIGHT THERMAL 1 P (A**2): 224 ; 5.09 ; 20.00
REMARK 3 TIGHT THERMAL 1 Q (A**2): 224 ; 6.20 ; 20.00
REMARK 3 TIGHT THERMAL 1 R (A**2): 224 ; 3.59 ; 20.00
REMARK 3 TIGHT THERMAL 1 S (A**2): 224 ; 3.27 ; 20.00
REMARK 3 TIGHT THERMAL 1 T (A**2): 224 ; 3.31 ; 20.00
REMARK 3 MEDIUM THERMAL 1 K (A**2): 163 ; 4.14 ; 20.00
REMARK 3 MEDIUM THERMAL 1 L (A**2): 163 ; 5.44 ; 20.00
REMARK 3 MEDIUM THERMAL 1 M (A**2): 163 ; 3.73 ; 20.00
REMARK 3 MEDIUM THERMAL 1 N (A**2): 163 ; 3.58 ; 20.00
REMARK 3 MEDIUM THERMAL 1 O (A**2): 163 ; 3.60 ; 20.00
REMARK 3 MEDIUM THERMAL 1 P (A**2): 163 ; 4.53 ; 20.00
REMARK 3 MEDIUM THERMAL 1 Q (A**2): 163 ; 5.16 ; 20.00
REMARK 3 MEDIUM THERMAL 1 R (A**2): 163 ; 3.30 ; 20.00
REMARK 3 MEDIUM THERMAL 1 S (A**2): 163 ; 3.29 ; 20.00
REMARK 3 MEDIUM THERMAL 1 T (A**2): 163 ; 3.37 ; 20.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : O P Q R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 O 3 O 38 6
REMARK 3 1 P 3 P 38 6
REMARK 3 1 Q 3 Q 38 6
REMARK 3 1 R 3 R 38 6
REMARK 3 2 O 53 O 72 6
REMARK 3 2 P 53 P 72 6
REMARK 3 2 Q 53 Q 72 6
REMARK 3 2 R 53 R 72 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 2 O (A): 387 ; 0.04 ; 0.10
REMARK 3 LOOSE POSITIONAL 2 P (A): 387 ; 0.04 ; 0.10
REMARK 3 LOOSE POSITIONAL 2 Q (A): 387 ; 0.04 ; 0.10
REMARK 3 LOOSE POSITIONAL 2 R (A): 387 ; 0.04 ; 0.10
REMARK 3 LOOSE THERMAL 2 O (A**2): 387 ; 2.11 ; 10.00
REMARK 3 LOOSE THERMAL 2 P (A**2): 387 ; 1.72 ; 10.00
REMARK 3 LOOSE THERMAL 2 Q (A**2): 387 ; 2.19 ; 10.00
REMARK 3 LOOSE THERMAL 2 R (A**2): 387 ; 2.08 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
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 26 A 700
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3033 -32.1375 -11.9225
REMARK 3 T TENSOR
REMARK 3 T11: -0.0984 T22: -0.4168
REMARK 3 T33: -0.0590 T12: 0.0099
REMARK 3 T13: 0.0858 T23: -0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 1.7001 L22: 1.3628
REMARK 3 L33: 1.2660 L12: 0.2209
REMARK 3 L13: -0.4880 L23: 0.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: -0.0091 S13: -0.0899
REMARK 3 S21: -0.0273 S22: -0.0159 S23: 0.2008
REMARK 3 S31: 0.1298 S32: -0.3157 S33: -0.0063
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 25 B 700
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5609 16.1027 -37.9438
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.2006
REMARK 3 T33: -0.0338 T12: 0.2868
REMARK 3 T13: -0.3029 T23: 0.2257
REMARK 3 L TENSOR
REMARK 3 L11: 1.7235 L22: 3.0975
REMARK 3 L33: 0.8949 L12: 0.2106
REMARK 3 L13: -0.0366 L23: 0.1088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0534 S12: 0.2752 S13: 0.2496
REMARK 3 S21: -0.1260 S22: -0.0654 S23: 0.8398
REMARK 3 S31: -0.1127 S32: -0.5281 S33: 0.1188
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 26 C 700
REMARK 3 ORIGIN FOR THE GROUP (A): 64.6476 19.0351 4.4256
REMARK 3 T TENSOR
REMARK 3 T11: -0.1455 T22: -0.6196
REMARK 3 T33: -0.1955 T12: -0.0039
REMARK 3 T13: 0.2353 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 1.3058 L22: 1.2868
REMARK 3 L33: 2.4953 L12: -0.0589
REMARK 3 L13: -0.2222 L23: 0.3495
REMARK 3 S TENSOR
REMARK 3 S11: 0.0519 S12: -0.0071 S13: 0.0406
REMARK 3 S21: 0.1272 S22: -0.0589 S23: -0.0143
REMARK 3 S31: -0.1275 S32: -0.1828 S33: 0.0070
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 6 D 700
REMARK 3 ORIGIN FOR THE GROUP (A): 67.2176 -11.4858 5.6502
REMARK 3 T TENSOR
REMARK 3 T11: -0.0906 T22: -0.5224
REMARK 3 T33: -0.1340 T12: 0.0740
REMARK 3 T13: 0.0692 T23: 0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 1.6304 L22: 1.3647
REMARK 3 L33: 1.7105 L12: 0.4789
REMARK 3 L13: -0.8031 L23: 0.0463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.2207 S13: -0.1738
REMARK 3 S21: 0.3239 S22: -0.0456 S23: -0.1875
REMARK 3 S31: 0.0674 S32: 0.0692 S33: 0.0441
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 : E 8 E 475
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1511 -19.0131 -35.9305
REMARK 3 T TENSOR
REMARK 3 T11: -0.0243 T22: 0.1460
REMARK 3 T33: -0.0400 T12: 0.0301
REMARK 3 T13: -0.1782 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 2.1587 L22: 1.5501
REMARK 3 L33: 0.9882 L12: 0.6686
REMARK 3 L13: -0.0116 L23: -0.1760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0478 S12: 0.4004 S13: -0.2043
REMARK 3 S21: -0.3013 S22: -0.0073 S23: 0.5569
REMARK 3 S31: 0.1120 S32: -0.6126 S33: 0.0551
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 : F 7 F 601
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0638 31.0578 -20.0049
REMARK 3 T TENSOR
REMARK 3 T11: -0.0744 T22: -0.3272
REMARK 3 T33: -0.1914 T12: 0.2539
REMARK 3 T13: -0.0377 T23: 0.1888
REMARK 3 L TENSOR
REMARK 3 L11: 1.2168 L22: 2.0854
REMARK 3 L33: 1.7389 L12: 0.1782
REMARK 3 L13: -0.4617 L23: 0.3185
REMARK 3 S TENSOR
REMARK 3 S11: 0.1226 S12: 0.1709 S13: 0.5466
REMARK 3 S21: -0.3478 S22: 0.0164 S23: 0.3617
REMARK 3 S31: -0.6494 S32: -0.2322 S33: -0.1390
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 : G 1 G 276
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7330 4.5285 16.5663
REMARK 3 T TENSOR
REMARK 3 T11: 0.0279 T22: 0.2948
REMARK 3 T33: 0.1063 T12: 0.1009
REMARK 3 T13: 0.2377 T23: -0.0743
REMARK 3 L TENSOR
REMARK 3 L11: 4.2143 L22: 0.3055
REMARK 3 L33: 3.5474 L12: -0.2761
REMARK 3 L13: -3.3314 L23: 0.1912
REMARK 3 S TENSOR
REMARK 3 S11: 0.1446 S12: -0.4947 S13: 0.2687
REMARK 3 S21: 0.1642 S22: 0.0035 S23: 0.1913
REMARK 3 S31: -0.1959 S32: 0.0095 S33: -0.1480
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 13 H 90
REMARK 3 RESIDUE RANGE : I 8 I 61
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6199 -9.1637 32.5235
REMARK 3 T TENSOR
REMARK 3 T11: -0.0729 T22: 0.0124
REMARK 3 T33: -0.0270 T12: 0.1986
REMARK 3 T13: 0.3475 T23: -0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 10.9397 L22: 1.3496
REMARK 3 L33: 6.3424 L12: 0.4769
REMARK 3 L13: -3.9837 L23: -1.2003
REMARK 3 S TENSOR
REMARK 3 S11: -0.7942 S12: -0.2058 S13: -1.0766
REMARK 3 S21: 0.1175 S22: -0.0187 S23: 0.0271
REMARK 3 S31: 0.6031 S32: -0.2116 S33: 0.8129
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 10
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 3 K 74
REMARK 3 RESIDUE RANGE : L 2 L 72
REMARK 3 RESIDUE RANGE : M 1 M 72
REMARK 3 RESIDUE RANGE : N 1 N 72
REMARK 3 RESIDUE RANGE : O 1 O 73
REMARK 3 RESIDUE RANGE : P 1 P 74
REMARK 3 RESIDUE RANGE : Q 1 Q 74
REMARK 3 RESIDUE RANGE : R 1 R 73
REMARK 3 RESIDUE RANGE : S 1 S 73
REMARK 3 RESIDUE RANGE : T 2 T 73
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5244 -0.2727 67.3580
REMARK 3 T TENSOR
REMARK 3 T11: -0.4560 T22: -0.3145
REMARK 3 T33: -0.5651 T12: -0.1285
REMARK 3 T13: 0.5196 T23: -0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 4.6944 L22: 1.4811
REMARK 3 L33: 2.6369 L12: -0.2205
REMARK 3 L13: -2.5642 L23: 0.1042
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: -0.7031 S13: -0.0933
REMARK 3 S21: 0.4164 S22: -0.1620 S23: 0.0367
REMARK 3 S31: -0.0696 S32: 0.7592 S33: 0.1494
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS.
REMARK 4
REMARK 4 2XOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1290045056.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93955
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.010
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.8
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 41.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2HLD
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150
REMARK 280 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3.
REMARK 280 MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH
REMARK 280 PLATE.
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 86.85550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: NONADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -379.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, K,
REMARK 350 AND CHAINS: L, M, N, O, P, Q, R, S, T
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 -34
REMARK 465 LEU A -33
REMARK 465 ALA A -32
REMARK 465 ARG A -31
REMARK 465 THR A -30
REMARK 465 ALA A -29
REMARK 465 ALA A -28
REMARK 465 ILE A -27
REMARK 465 ARG A -26
REMARK 465 SER A -25
REMARK 465 LEU A -24
REMARK 465 SER A -23
REMARK 465 ARG A -22
REMARK 465 THR A -21
REMARK 465 LEU A -20
REMARK 465 ILE A -19
REMARK 465 ASN A -18
REMARK 465 SER A -17
REMARK 465 THR A -16
REMARK 465 LYS A -15
REMARK 465 ALA A -14
REMARK 465 ALA A -13
REMARK 465 ARG A -12
REMARK 465 PRO A -11
REMARK 465 ALA A -10
REMARK 465 ALA A -9
REMARK 465 ALA A -8
REMARK 465 ALA A -7
REMARK 465 LEU A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 THR A -3
REMARK 465 ARG A -2
REMARK 465 ARG A -1
REMARK 465 LEU A 0
REMARK 465 ALA A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 ALA A 5
REMARK 465 GLN A 6
REMARK 465 PRO A 7
REMARK 465 THR A 8
REMARK 465 GLU A 9
REMARK 465 VAL A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 ILE A 13
REMARK 465 LEU A 14
REMARK 465 GLU A 15
REMARK 465 GLU A 16
REMARK 465 ARG A 17
REMARK 465 ILE A 18
REMARK 465 LYS A 19
REMARK 465 GLY A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 ASP A 23
REMARK 465 GLU A 24
REMARK 465 ALA A 25
REMARK 465 PHE A 408
REMARK 465 GLY A 409
REMARK 465 MET B -34
REMARK 465 LEU B -33
REMARK 465 ALA B -32
REMARK 465 ARG B -31
REMARK 465 THR B -30
REMARK 465 ALA B -29
REMARK 465 ALA B -28
REMARK 465 ILE B -27
REMARK 465 ARG B -26
REMARK 465 SER B -25
REMARK 465 LEU B -24
REMARK 465 SER B -23
REMARK 465 ARG B -22
REMARK 465 THR B -21
REMARK 465 LEU B -20
REMARK 465 ILE B -19
REMARK 465 ASN B -18
REMARK 465 SER B -17
REMARK 465 THR B -16
REMARK 465 LYS B -15
REMARK 465 ALA B -14
REMARK 465 ALA B -13
REMARK 465 ARG B -12
REMARK 465 PRO B -11
REMARK 465 ALA B -10
REMARK 465 ALA B -9
REMARK 465 ALA B -8
REMARK 465 ALA B -7
REMARK 465 LEU B -6
REMARK 465 ALA B -5
REMARK 465 SER B -4
REMARK 465 THR B -3
REMARK 465 ARG B -2
REMARK 465 ARG B -1
REMARK 465 LEU B 0
REMARK 465 ALA B 1
REMARK 465 SER B 2
REMARK 465 THR B 3
REMARK 465 LYS B 4
REMARK 465 ALA B 5
REMARK 465 GLN B 6
REMARK 465 PRO B 7
REMARK 465 THR B 8
REMARK 465 GLU B 9
REMARK 465 VAL B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 ILE B 13
REMARK 465 LEU B 14
REMARK 465 GLU B 15
REMARK 465 GLU B 16
REMARK 465 ARG B 17
REMARK 465 ILE B 18
REMARK 465 LYS B 19
REMARK 465 GLY B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 ASP B 23
REMARK 465 GLU B 24
REMARK 465 PHE B 408
REMARK 465 GLY B 409
REMARK 465 MET C -34
REMARK 465 LEU C -33
REMARK 465 ALA C -32
REMARK 465 ARG C -31
REMARK 465 THR C -30
REMARK 465 ALA C -29
REMARK 465 ALA C -28
REMARK 465 ILE C -27
REMARK 465 ARG C -26
REMARK 465 SER C -25
REMARK 465 LEU C -24
REMARK 465 SER C -23
REMARK 465 ARG C -22
REMARK 465 THR C -21
REMARK 465 LEU C -20
REMARK 465 ILE C -19
REMARK 465 ASN C -18
REMARK 465 SER C -17
REMARK 465 THR C -16
REMARK 465 LYS C -15
REMARK 465 ALA C -14
REMARK 465 ALA C -13
REMARK 465 ARG C -12
REMARK 465 PRO C -11
REMARK 465 ALA C -10
REMARK 465 ALA C -9
REMARK 465 ALA C -8
REMARK 465 ALA C -7
REMARK 465 LEU C -6
REMARK 465 ALA C -5
REMARK 465 SER C -4
REMARK 465 THR C -3
REMARK 465 ARG C -2
REMARK 465 ARG C -1
REMARK 465 LEU C 0
REMARK 465 ALA C 1
REMARK 465 SER C 2
REMARK 465 THR C 3
REMARK 465 LYS C 4
REMARK 465 ALA C 5
REMARK 465 GLN C 6
REMARK 465 PRO C 7
REMARK 465 THR C 8
REMARK 465 GLU C 9
REMARK 465 VAL C 10
REMARK 465 SER C 11
REMARK 465 SER C 12
REMARK 465 ILE C 13
REMARK 465 LEU C 14
REMARK 465 GLU C 15
REMARK 465 GLU C 16
REMARK 465 ARG C 17
REMARK 465 ILE C 18
REMARK 465 LYS C 19
REMARK 465 GLY C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 ASP C 23
REMARK 465 GLU C 24
REMARK 465 ALA C 25
REMARK 465 MET D -32
REMARK 465 VAL D -31
REMARK 465 LEU D -30
REMARK 465 PRO D -29
REMARK 465 ARG D -28
REMARK 465 LEU D -27
REMARK 465 TYR D -26
REMARK 465 THR D -25
REMARK 465 ALA D -24
REMARK 465 THR D -23
REMARK 465 SER D -22
REMARK 465 ARG D -21
REMARK 465 ALA D -20
REMARK 465 ALA D -19
REMARK 465 PHE D -18
REMARK 465 LYS D -17
REMARK 465 ALA D -16
REMARK 465 ALA D -15
REMARK 465 LYS D -14
REMARK 465 GLN D -13
REMARK 465 SER D -12
REMARK 465 ALA D -11
REMARK 465 PRO D -10
REMARK 465 LEU D -9
REMARK 465 LEU D -8
REMARK 465 SER D -7
REMARK 465 THR D -6
REMARK 465 SER D -5
REMARK 465 TRP D -4
REMARK 465 LYS D -3
REMARK 465 ARG D -2
REMARK 465 CYS D -1
REMARK 465 MET D 0
REMARK 465 ALA D 1
REMARK 465 SER D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 GLN D 5
REMARK 465 ALA D 477
REMARK 465 ASN D 478
REMARK 465 MET E -32
REMARK 465 VAL E -31
REMARK 465 LEU E -30
REMARK 465 PRO E -29
REMARK 465 ARG E -28
REMARK 465 LEU E -27
REMARK 465 TYR E -26
REMARK 465 THR E -25
REMARK 465 ALA E -24
REMARK 465 THR E -23
REMARK 465 SER E -22
REMARK 465 ARG E -21
REMARK 465 ALA E -20
REMARK 465 ALA E -19
REMARK 465 PHE E -18
REMARK 465 LYS E -17
REMARK 465 ALA E -16
REMARK 465 ALA E -15
REMARK 465 LYS E -14
REMARK 465 GLN E -13
REMARK 465 SER E -12
REMARK 465 ALA E -11
REMARK 465 PRO E -10
REMARK 465 LEU E -9
REMARK 465 LEU E -8
REMARK 465 SER E -7
REMARK 465 THR E -6
REMARK 465 SER E -5
REMARK 465 TRP E -4
REMARK 465 LYS E -3
REMARK 465 ARG E -2
REMARK 465 CYS E -1
REMARK 465 MET E 0
REMARK 465 ALA E 1
REMARK 465 SER E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 GLN E 5
REMARK 465 SER E 6
REMARK 465 THR E 7
REMARK 465 ALA E 477
REMARK 465 ASN E 478
REMARK 465 MET F -32
REMARK 465 VAL F -31
REMARK 465 LEU F -30
REMARK 465 PRO F -29
REMARK 465 ARG F -28
REMARK 465 LEU F -27
REMARK 465 TYR F -26
REMARK 465 THR F -25
REMARK 465 ALA F -24
REMARK 465 THR F -23
REMARK 465 SER F -22
REMARK 465 ARG F -21
REMARK 465 ALA F -20
REMARK 465 ALA F -19
REMARK 465 PHE F -18
REMARK 465 LYS F -17
REMARK 465 ALA F -16
REMARK 465 ALA F -15
REMARK 465 LYS F -14
REMARK 465 GLN F -13
REMARK 465 SER F -12
REMARK 465 ALA F -11
REMARK 465 PRO F -10
REMARK 465 LEU F -9
REMARK 465 LEU F -8
REMARK 465 SER F -7
REMARK 465 THR F -6
REMARK 465 SER F -5
REMARK 465 TRP F -4
REMARK 465 LYS F -3
REMARK 465 ARG F -2
REMARK 465 CYS F -1
REMARK 465 MET F 0
REMARK 465 ALA F 1
REMARK 465 SER F 2
REMARK 465 ALA F 3
REMARK 465 ALA F 4
REMARK 465 GLN F 5
REMARK 465 SER F 6
REMARK 465 ALA F 477
REMARK 465 ASN F 478
REMARK 465 MET G -32
REMARK 465 LEU G -31
REMARK 465 SER G -30
REMARK 465 ARG G -29
REMARK 465 ILE G -28
REMARK 465 VAL G -27
REMARK 465 SER G -26
REMARK 465 ASN G -25
REMARK 465 ASN G -24
REMARK 465 ALA G -23
REMARK 465 THR G -22
REMARK 465 ARG G -21
REMARK 465 SER G -20
REMARK 465 VAL G -19
REMARK 465 MET G -18
REMARK 465 CYS G -17
REMARK 465 HIS G -16
REMARK 465 GLN G -15
REMARK 465 ALA G -14
REMARK 465 GLN G -13
REMARK 465 VAL G -12
REMARK 465 GLY G -11
REMARK 465 ILE G -10
REMARK 465 LEU G -9
REMARK 465 TYR G -8
REMARK 465 LYS G -7
REMARK 465 THR G -6
REMARK 465 ASN G -5
REMARK 465 PRO G -4
REMARK 465 VAL G -3
REMARK 465 ARG G -2
REMARK 465 THR G -1
REMARK 465 TYR G 0
REMARK 465 LEU G 60
REMARK 465 ASP G 61
REMARK 465 VAL G 62
REMARK 465 GLU G 63
REMARK 465 ALA G 64
REMARK 465 THR G 65
REMARK 465 GLU G 66
REMARK 465 THR G 67
REMARK 465 GLY G 68
REMARK 465 ALA G 69
REMARK 465 PRO G 70
REMARK 465 GLY G 278
REMARK 465 MET H -21
REMARK 465 LEU H -20
REMARK 465 ARG H -19
REMARK 465 SER H -18
REMARK 465 ILE H -17
REMARK 465 ILE H -16
REMARK 465 GLY H -15
REMARK 465 LYS H -14
REMARK 465 SER H -13
REMARK 465 ALA H -12
REMARK 465 SER H -11
REMARK 465 ARG H -10
REMARK 465 SER H -9
REMARK 465 LEU H -8
REMARK 465 ASN H -7
REMARK 465 PHE H -6
REMARK 465 VAL H -5
REMARK 465 ALA H -4
REMARK 465 LYS H -3
REMARK 465 ARG H -2
REMARK 465 SER H -1
REMARK 465 TYR H 0
REMARK 465 ALA H 1
REMARK 465 GLU H 2
REMARK 465 ALA H 3
REMARK 465 ALA H 4
REMARK 465 ALA H 5
REMARK 465 ALA H 6
REMARK 465 SER H 7
REMARK 465 SER H 8
REMARK 465 GLY H 9
REMARK 465 LEU H 10
REMARK 465 LYS H 11
REMARK 465 GLY H 24
REMARK 465 SER H 25
REMARK 465 PHE H 91
REMARK 465 GLN H 98
REMARK 465 ASP H 116
REMARK 465 ALA H 117
REMARK 465 LEU H 137
REMARK 465 LYS H 138
REMARK 465 SER I 1
REMARK 465 ALA I 2
REMARK 465 TRP I 3
REMARK 465 ARG I 4
REMARK 465 LYS I 5
REMARK 465 ALA I 6
REMARK 465 GLY I 7
REMARK 465 LEU I 25
REMARK 465 LYS I 26
REMARK 465 GLY I 50
REMARK 465 THR I 51
REMARK 465 ALA I 52
REMARK 465 MET K 1
REMARK 465 GLN K 2
REMARK 465 VAL K 76
REMARK 465 MET L 1
REMARK 465 PHE L 74
REMARK 465 GLY L 75
REMARK 465 VAL L 76
REMARK 465 PHE M 74
REMARK 465 GLY M 75
REMARK 465 VAL M 76
REMARK 465 PHE N 74
REMARK 465 GLY N 75
REMARK 465 VAL N 76
REMARK 465 GLY O 75
REMARK 465 VAL O 76
REMARK 465 VAL P 76
REMARK 465 VAL Q 76
REMARK 465 GLY R 75
REMARK 465 VAL R 76
REMARK 465 GLY S 75
REMARK 465 VAL S 76
REMARK 465 MET T 1
REMARK 465 GLY T 75
REMARK 465 VAL T 76
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 410 OG
REMARK 470 PHE A 510 CA C O CB CG CD1 CD2
REMARK 470 PHE A 510 CE1 CE2 CZ
REMARK 470 SER B 410 OG
REMARK 470 PHE B 510 CA C O CB CG CD1 CD2
REMARK 470 PHE B 510 CE1 CE2 CZ
REMARK 470 PHE C 408 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER C 410 OG
REMARK 470 PHE C 510 CA C O CB CG CD1 CD2
REMARK 470 PHE C 510 CE1 CE2 CZ
REMARK 470 GLU D 476 CA C O CB CG CD OE1
REMARK 470 GLU D 476 OE2
REMARK 470 GLU E 476 CA C O CB CG CD OE1
REMARK 470 GLU E 476 OE2
REMARK 470 GLU F 476 CA C O CB CG CD OE1
REMARK 470 GLU F 476 OE2
REMARK 470 SER G 40 OG
REMARK 470 GLU G 56 CG CD OE1 OE2
REMARK 470 THR G 57 OG1 CG2
REMARK 470 LYS G 58 CG CD CE NZ
REMARK 470 ASN G 59 CG OD1 ND2
REMARK 470 GLU G 198 CG CD OE1 OE2
REMARK 470 ILE G 199 CG1 CG2 CD1
REMARK 470 ASP G 200 CG OD1 OD2
REMARK 470 ASN G 204 CG OD1 ND2
REMARK 470 LEU G 277 CA C O CB CG CD1 CD2
REMARK 470 LEU H 16 CG CD1 CD2
REMARK 470 GLU H 26 CG CD OE1 OE2
REMARK 470 LYS H 35 CG CD CE NZ
REMARK 470 SER H 36 OG
REMARK 470 GLU H 50 CG CD OE1 OE2
REMARK 470 LEU H 53 CG CD1 CD2
REMARK 470 VAL H 56 CG1 CG2
REMARK 470 VAL H 59 CG1 CG2
REMARK 470 SER H 65 OG
REMARK 470 LYS H 66 CG CD CE NZ
REMARK 470 LYS H 67 CG CD CE NZ
REMARK 470 GLN H 82 CG CD OE1 NE2
REMARK 470 LEU H 93 CG CD1 CD2
REMARK 470 GLU H 94 CG CD OE1 OE2
REMARK 470 SER H 95 OG
REMARK 470 PHE H 96 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER H 97 OG
REMARK 470 GLU H 99 CG CD OE1 OE2
REMARK 470 ASN H 100 CB CG OD1 ND2
REMARK 470 ILE H 101 CG1 CG2 CD1
REMARK 470 LYS H 102 CG CD CE NZ
REMARK 470 ASN H 103 CG OD1 ND2
REMARK 470 LEU H 104 CG CD1 CD2
REMARK 470 LEU H 105 CG CD1 CD2
REMARK 470 GLU H 107 CG CD OE1 OE2
REMARK 470 LYS H 109 CG CD CE NZ
REMARK 470 LYS H 110 CG CD CE NZ
REMARK 470 ASN H 111 CG OD1 ND2
REMARK 470 VAL H 112 CG1 CG2
REMARK 470 SER H 113 OG
REMARK 470 SER H 114 OG
REMARK 470 SER H 115 CB OG
REMARK 470 ARG H 118 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 119 CG CD OE1 OE2
REMARK 470 GLU H 122 CG CD OE1 OE2
REMARK 470 ILE H 125 CG1 CG2 CD1
REMARK 470 GLN H 126 CG CD OE1 NE2
REMARK 470 VAL H 127 CG1 CG2
REMARK 470 GLU H 128 CG CD OE1 OE2
REMARK 470 VAL H 129 CG1 CG2
REMARK 470 LEU H 130 CG CD1 CD2
REMARK 470 GLU H 131 CG CD OE1 OE2
REMARK 470 ASN H 132 CG OD1 ND2
REMARK 470 LEU H 133 CG CD1 CD2
REMARK 470 GLN H 134 CG CD OE1 NE2
REMARK 470 SER H 135 OG
REMARK 470 VAL H 136 CG1 CG2
REMARK 470 MET I 8 CG SD CE
REMARK 470 ILE I 21 CG1 CG2 CD1
REMARK 470 ARG I 22 CG CD NE CZ NH1 NH2
REMARK 470 SER I 23 OG
REMARK 470 SER I 24 CA C O CB OG
REMARK 470 THR I 35 OG1 CG2
REMARK 470 GLN I 39 CG CD OE1 NE2
REMARK 470 THR I 40 OG1 CG2
REMARK 470 LYS I 48 CG CD CE NZ
REMARK 470 ASN I 49 CG OD1 ND2
REMARK 470 SER I 54 OG
REMARK 470 GLU I 55 CG CD OE1 OE2
REMARK 470 PRO I 56 CG CD
REMARK 470 THR I 57 OG1 CG2
REMARK 470 PRO I 58 CG CD
REMARK 470 MET I 59 CG SD CE
REMARK 470 THR I 60 OG1 CG2
REMARK 470 LYS I 61 CG CD CE NZ
REMARK 470 GLY K 75 CA C O
REMARK 470 LEU L 73 CA C O CB CG CD1 CD2
REMARK 470 LEU M 73 CA C O CB CG CD1 CD2
REMARK 470 LEU N 73 CA C O CB CG CD1 CD2
REMARK 470 PHE O 74 CA C O CB CG CD1 CD2
REMARK 470 PHE O 74 CE1 CE2 CZ
REMARK 470 GLY P 75 CA C O
REMARK 470 GLY Q 75 CA C O
REMARK 470 PHE R 74 CA C O CB CG CD1 CD2
REMARK 470 PHE R 74 CE1 CE2 CZ
REMARK 470 PHE S 74 CA C O CB CG CD1 CD2
REMARK 470 PHE S 74 CE1 CE2 CZ
REMARK 470 PHE T 74 CA C O CB CG CD1 CD2
REMARK 470 PHE T 74 CE1 CE2 CZ
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 PRO I 56 N - CA - CB ANGL. DEV. = 7.6 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 52 20.84 82.19
REMARK 500 PRO A 140 40.27 -86.00
REMARK 500 HIS A 145 -6.28 -148.93
REMARK 500 GLN A 220 -8.14 -59.65
REMARK 500 LYS A 229 -13.96 -47.39
REMARK 500 ALA A 238 -41.88 -29.76
REMARK 500 GLU A 294 17.36 59.52
REMARK 500 SER A 320 18.56 54.88
REMARK 500 LEU A 326 71.55 -112.84
REMARK 500 ALA A 389 -3.23 -143.05
REMARK 500 ALA A 406 5.04 -69.87
REMARK 500 GLN A 432 110.72 -164.07
REMARK 500 TYR A 435 -2.35 65.76
REMARK 500 SER A 436 72.16 -112.42
REMARK 500 GLU A 441 -9.55 -56.84
REMARK 500 HIS A 478 22.98 -150.31
REMARK 500 ASN A 479 -17.66 -48.32
REMARK 500 LEU B 66 -88.53 -81.65
REMARK 500 VAL B 97 121.24 -36.50
REMARK 500 HIS B 145 -28.85 -146.13
REMARK 500 LEU B 158 -60.61 -92.23
REMARK 500 VAL B 159 79.57 -113.99
REMARK 500 GLN B 174 41.34 74.03
REMARK 500 ASP B 226 -14.05 74.63
REMARK 500 ALA B 227 -4.67 -58.09
REMARK 500 LYS B 229 -35.66 -39.17
REMARK 500 ASN B 262 39.03 -91.79
REMARK 500 GLN B 282 -75.49 -65.43
REMARK 500 GLU B 294 42.96 36.05
REMARK 500 GLU B 309 -9.69 -55.99
REMARK 500 LEU B 326 75.94 -118.43
REMARK 500 ILE B 352 77.41 -111.16
REMARK 500 SER B 378 7.63 -68.95
REMARK 500 ALA B 389 64.68 -119.39
REMARK 500 LEU B 392 -28.93 -37.90
REMARK 500 LYS B 393 -74.35 -58.91
REMARK 500 ALA B 404 42.11 -95.73
REMARK 500 PHE B 405 20.48 -153.68
REMARK 500 ALA B 414 8.41 -65.99
REMARK 500 ARG B 422 -70.20 -75.19
REMARK 500 TYR B 448 -74.55 -42.50
REMARK 500 ASN B 477 -85.06 -121.70
REMARK 500 LYS B 500 2.28 -69.77
REMARK 500 THR B 509 42.06 -94.80
REMARK 500 LEU C 46 65.22 39.65
REMARK 500 PRO C 140 52.05 -91.63
REMARK 500 ARG C 163 97.35 -62.52
REMARK 500 ASP C 172 -174.39 -64.25
REMARK 500 GLN C 224 -19.97 -49.80
REMARK 500 ALA C 238 -39.19 -25.78
REMARK 500
REMARK 500 THIS ENTRY HAS 203 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER I 9 TYR I 10 147.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 178 OG1
REMARK 620 2 ANP A 600 O2G 135.8
REMARK 620 3 ANP A 600 O2B 75.3 74.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 178 OG1
REMARK 620 2 ANP B 600 O2B 88.4
REMARK 620 3 ANP B 600 O2G 154.9 67.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 178 OG1
REMARK 620 2 ANP C 600 O2B 79.1
REMARK 620 3 ANP C 600 O2G 147.5 80.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 164 OG1
REMARK 620 2 ANP D 600 O2B 94.4
REMARK 620 3 ANP D 600 O2G 116.9 86.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 164 OG1
REMARK 620 2 GLU F 189 OE1 101.5
REMARK 620 3 ANP F 600 O2G 169.7 79.5
REMARK 620 4 ANP F 600 O2B 83.8 163.7 92.7
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP F 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WPD RELATED DB: PDB
REMARK 900 THE MG.ADP INHIBITED STATE OF THE YEAST F1C10 ATP SYNTHASE
DBREF 2XOK A -34 510 UNP P07251 ATPA_YEAST 1 545
DBREF 2XOK B -34 510 UNP P07251 ATPA_YEAST 1 545
DBREF 2XOK C -34 510 UNP P07251 ATPA_YEAST 1 545
DBREF 2XOK D -32 474 UNP P00830 ATPB_YEAST 1 507
DBREF 2XOK E -32 474 UNP P00830 ATPB_YEAST 1 507
DBREF 2XOK F -32 474 UNP P00830 ATPB_YEAST 1 507
DBREF 2XOK G -32 278 UNP P38077 ATPG_YEAST 1 311
DBREF 2XOK H -21 138 UNP Q12165 ATPD_YEAST 1 160
DBREF 2XOK I 1 61 UNP Q2XN67 Q2XN67_YEAST 2 62
DBREF 2XOK K 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK L 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK M 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK N 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK O 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK P 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK Q 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK R 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK S 1 76 UNP P61829 ATP9_YEAST 1 76
DBREF 2XOK T 1 76 UNP P61829 ATP9_YEAST 1 76
SEQRES 1 A 545 MET LEU ALA ARG THR ALA ALA ILE ARG SER LEU SER ARG
SEQRES 2 A 545 THR LEU ILE ASN SER THR LYS ALA ALA ARG PRO ALA ALA
SEQRES 3 A 545 ALA ALA LEU ALA SER THR ARG ARG LEU ALA SER THR LYS
SEQRES 4 A 545 ALA GLN PRO THR GLU VAL SER SER ILE LEU GLU GLU ARG
SEQRES 5 A 545 ILE LYS GLY VAL SER ASP GLU ALA ASN LEU ASN GLU THR
SEQRES 6 A 545 GLY ARG VAL LEU ALA VAL GLY ASP GLY ILE ALA ARG VAL
SEQRES 7 A 545 PHE GLY LEU ASN ASN ILE GLN ALA GLU GLU LEU VAL GLU
SEQRES 8 A 545 PHE SER SER GLY VAL LYS GLY MET ALA LEU ASN LEU GLU
SEQRES 9 A 545 PRO GLY GLN VAL GLY ILE VAL LEU PHE GLY SER ASP ARG
SEQRES 10 A 545 LEU VAL LYS GLU GLY GLU LEU VAL LYS ARG THR GLY ASN
SEQRES 11 A 545 ILE VAL ASP VAL PRO VAL GLY PRO GLY LEU LEU GLY ARG
SEQRES 12 A 545 VAL VAL ASP ALA LEU GLY ASN PRO ILE ASP GLY LYS GLY
SEQRES 13 A 545 PRO ILE ASP ALA ALA GLY ARG SER ARG ALA GLN VAL LYS
SEQRES 14 A 545 ALA PRO GLY ILE LEU PRO ARG ARG SER VAL HIS GLU PRO
SEQRES 15 A 545 VAL GLN THR GLY LEU LYS ALA VAL ASP ALA LEU VAL PRO
SEQRES 16 A 545 ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY ASP ARG
SEQRES 17 A 545 GLN THR GLY LYS THR ALA VAL ALA LEU ASP THR ILE LEU
SEQRES 18 A 545 ASN GLN LYS ARG TRP ASN ASN GLY SER ASP GLU SER LYS
SEQRES 19 A 545 LYS LEU TYR CYS VAL TYR VAL ALA VAL GLY GLN LYS ARG
SEQRES 20 A 545 SER THR VAL ALA GLN LEU VAL GLN THR LEU GLU GLN HIS
SEQRES 21 A 545 ASP ALA MET LYS TYR SER ILE ILE VAL ALA ALA THR ALA
SEQRES 22 A 545 SER GLU ALA ALA PRO LEU GLN TYR LEU ALA PRO PHE THR
SEQRES 23 A 545 ALA ALA SER ILE GLY GLU TRP PHE ARG ASP ASN GLY LYS
SEQRES 24 A 545 HIS ALA LEU ILE VAL TYR ASP ASP LEU SER LYS GLN ALA
SEQRES 25 A 545 VAL ALA TYR ARG GLN LEU SER LEU LEU LEU ARG ARG PRO
SEQRES 26 A 545 PRO GLY ARG GLU ALA TYR PRO GLY ASP VAL PHE TYR LEU
SEQRES 27 A 545 HIS SER ARG LEU LEU GLU ARG ALA ALA LYS LEU SER GLU
SEQRES 28 A 545 LYS GLU GLY SER GLY SER LEU THR ALA LEU PRO VAL ILE
SEQRES 29 A 545 GLU THR GLN GLY GLY ASP VAL SER ALA TYR ILE PRO THR
SEQRES 30 A 545 ASN VAL ILE SER ILE THR ASP GLY GLN ILE PHE LEU GLU
SEQRES 31 A 545 ALA GLU LEU PHE TYR LYS GLY ILE ARG PRO ALA ILE ASN
SEQRES 32 A 545 VAL GLY LEU SER VAL SER ARG VAL GLY SER ALA ALA GLN
SEQRES 33 A 545 VAL LYS ALA LEU LYS GLN VAL ALA GLY SER LEU LYS LEU
SEQRES 34 A 545 PHE LEU ALA GLN TYR ARG GLU VAL ALA ALA PHE ALA GLN
SEQRES 35 A 545 PHE GLY SER ASP LEU ASP ALA SER THR LYS GLN THR LEU
SEQRES 36 A 545 VAL ARG GLY GLU ARG LEU THR GLN LEU LEU LYS GLN ASN
SEQRES 37 A 545 GLN TYR SER PRO LEU ALA THR GLU GLU GLN VAL PRO LEU
SEQRES 38 A 545 ILE TYR ALA GLY VAL ASN GLY HIS LEU ASP GLY ILE GLU
SEQRES 39 A 545 LEU SER ARG ILE GLY GLU PHE GLU SER SER PHE LEU SER
SEQRES 40 A 545 TYR LEU LYS SER ASN HIS ASN GLU LEU LEU THR GLU ILE
SEQRES 41 A 545 ARG GLU LYS GLY GLU LEU SER LYS GLU LEU LEU ALA SER
SEQRES 42 A 545 LEU LYS SER ALA THR GLU SER PHE VAL ALA THR PHE
SEQRES 1 B 545 MET LEU ALA ARG THR ALA ALA ILE ARG SER LEU SER ARG
SEQRES 2 B 545 THR LEU ILE ASN SER THR LYS ALA ALA ARG PRO ALA ALA
SEQRES 3 B 545 ALA ALA LEU ALA SER THR ARG ARG LEU ALA SER THR LYS
SEQRES 4 B 545 ALA GLN PRO THR GLU VAL SER SER ILE LEU GLU GLU ARG
SEQRES 5 B 545 ILE LYS GLY VAL SER ASP GLU ALA ASN LEU ASN GLU THR
SEQRES 6 B 545 GLY ARG VAL LEU ALA VAL GLY ASP GLY ILE ALA ARG VAL
SEQRES 7 B 545 PHE GLY LEU ASN ASN ILE GLN ALA GLU GLU LEU VAL GLU
SEQRES 8 B 545 PHE SER SER GLY VAL LYS GLY MET ALA LEU ASN LEU GLU
SEQRES 9 B 545 PRO GLY GLN VAL GLY ILE VAL LEU PHE GLY SER ASP ARG
SEQRES 10 B 545 LEU VAL LYS GLU GLY GLU LEU VAL LYS ARG THR GLY ASN
SEQRES 11 B 545 ILE VAL ASP VAL PRO VAL GLY PRO GLY LEU LEU GLY ARG
SEQRES 12 B 545 VAL VAL ASP ALA LEU GLY ASN PRO ILE ASP GLY LYS GLY
SEQRES 13 B 545 PRO ILE ASP ALA ALA GLY ARG SER ARG ALA GLN VAL LYS
SEQRES 14 B 545 ALA PRO GLY ILE LEU PRO ARG ARG SER VAL HIS GLU PRO
SEQRES 15 B 545 VAL GLN THR GLY LEU LYS ALA VAL ASP ALA LEU VAL PRO
SEQRES 16 B 545 ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY ASP ARG
SEQRES 17 B 545 GLN THR GLY LYS THR ALA VAL ALA LEU ASP THR ILE LEU
SEQRES 18 B 545 ASN GLN LYS ARG TRP ASN ASN GLY SER ASP GLU SER LYS
SEQRES 19 B 545 LYS LEU TYR CYS VAL TYR VAL ALA VAL GLY GLN LYS ARG
SEQRES 20 B 545 SER THR VAL ALA GLN LEU VAL GLN THR LEU GLU GLN HIS
SEQRES 21 B 545 ASP ALA MET LYS TYR SER ILE ILE VAL ALA ALA THR ALA
SEQRES 22 B 545 SER GLU ALA ALA PRO LEU GLN TYR LEU ALA PRO PHE THR
SEQRES 23 B 545 ALA ALA SER ILE GLY GLU TRP PHE ARG ASP ASN GLY LYS
SEQRES 24 B 545 HIS ALA LEU ILE VAL TYR ASP ASP LEU SER LYS GLN ALA
SEQRES 25 B 545 VAL ALA TYR ARG GLN LEU SER LEU LEU LEU ARG ARG PRO
SEQRES 26 B 545 PRO GLY ARG GLU ALA TYR PRO GLY ASP VAL PHE TYR LEU
SEQRES 27 B 545 HIS SER ARG LEU LEU GLU ARG ALA ALA LYS LEU SER GLU
SEQRES 28 B 545 LYS GLU GLY SER GLY SER LEU THR ALA LEU PRO VAL ILE
SEQRES 29 B 545 GLU THR GLN GLY GLY ASP VAL SER ALA TYR ILE PRO THR
SEQRES 30 B 545 ASN VAL ILE SER ILE THR ASP GLY GLN ILE PHE LEU GLU
SEQRES 31 B 545 ALA GLU LEU PHE TYR LYS GLY ILE ARG PRO ALA ILE ASN
SEQRES 32 B 545 VAL GLY LEU SER VAL SER ARG VAL GLY SER ALA ALA GLN
SEQRES 33 B 545 VAL LYS ALA LEU LYS GLN VAL ALA GLY SER LEU LYS LEU
SEQRES 34 B 545 PHE LEU ALA GLN TYR ARG GLU VAL ALA ALA PHE ALA GLN
SEQRES 35 B 545 PHE GLY SER ASP LEU ASP ALA SER THR LYS GLN THR LEU
SEQRES 36 B 545 VAL ARG GLY GLU ARG LEU THR GLN LEU LEU LYS GLN ASN
SEQRES 37 B 545 GLN TYR SER PRO LEU ALA THR GLU GLU GLN VAL PRO LEU
SEQRES 38 B 545 ILE TYR ALA GLY VAL ASN GLY HIS LEU ASP GLY ILE GLU
SEQRES 39 B 545 LEU SER ARG ILE GLY GLU PHE GLU SER SER PHE LEU SER
SEQRES 40 B 545 TYR LEU LYS SER ASN HIS ASN GLU LEU LEU THR GLU ILE
SEQRES 41 B 545 ARG GLU LYS GLY GLU LEU SER LYS GLU LEU LEU ALA SER
SEQRES 42 B 545 LEU LYS SER ALA THR GLU SER PHE VAL ALA THR PHE
SEQRES 1 C 545 MET LEU ALA ARG THR ALA ALA ILE ARG SER LEU SER ARG
SEQRES 2 C 545 THR LEU ILE ASN SER THR LYS ALA ALA ARG PRO ALA ALA
SEQRES 3 C 545 ALA ALA LEU ALA SER THR ARG ARG LEU ALA SER THR LYS
SEQRES 4 C 545 ALA GLN PRO THR GLU VAL SER SER ILE LEU GLU GLU ARG
SEQRES 5 C 545 ILE LYS GLY VAL SER ASP GLU ALA ASN LEU ASN GLU THR
SEQRES 6 C 545 GLY ARG VAL LEU ALA VAL GLY ASP GLY ILE ALA ARG VAL
SEQRES 7 C 545 PHE GLY LEU ASN ASN ILE GLN ALA GLU GLU LEU VAL GLU
SEQRES 8 C 545 PHE SER SER GLY VAL LYS GLY MET ALA LEU ASN LEU GLU
SEQRES 9 C 545 PRO GLY GLN VAL GLY ILE VAL LEU PHE GLY SER ASP ARG
SEQRES 10 C 545 LEU VAL LYS GLU GLY GLU LEU VAL LYS ARG THR GLY ASN
SEQRES 11 C 545 ILE VAL ASP VAL PRO VAL GLY PRO GLY LEU LEU GLY ARG
SEQRES 12 C 545 VAL VAL ASP ALA LEU GLY ASN PRO ILE ASP GLY LYS GLY
SEQRES 13 C 545 PRO ILE ASP ALA ALA GLY ARG SER ARG ALA GLN VAL LYS
SEQRES 14 C 545 ALA PRO GLY ILE LEU PRO ARG ARG SER VAL HIS GLU PRO
SEQRES 15 C 545 VAL GLN THR GLY LEU LYS ALA VAL ASP ALA LEU VAL PRO
SEQRES 16 C 545 ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY ASP ARG
SEQRES 17 C 545 GLN THR GLY LYS THR ALA VAL ALA LEU ASP THR ILE LEU
SEQRES 18 C 545 ASN GLN LYS ARG TRP ASN ASN GLY SER ASP GLU SER LYS
SEQRES 19 C 545 LYS LEU TYR CYS VAL TYR VAL ALA VAL GLY GLN LYS ARG
SEQRES 20 C 545 SER THR VAL ALA GLN LEU VAL GLN THR LEU GLU GLN HIS
SEQRES 21 C 545 ASP ALA MET LYS TYR SER ILE ILE VAL ALA ALA THR ALA
SEQRES 22 C 545 SER GLU ALA ALA PRO LEU GLN TYR LEU ALA PRO PHE THR
SEQRES 23 C 545 ALA ALA SER ILE GLY GLU TRP PHE ARG ASP ASN GLY LYS
SEQRES 24 C 545 HIS ALA LEU ILE VAL TYR ASP ASP LEU SER LYS GLN ALA
SEQRES 25 C 545 VAL ALA TYR ARG GLN LEU SER LEU LEU LEU ARG ARG PRO
SEQRES 26 C 545 PRO GLY ARG GLU ALA TYR PRO GLY ASP VAL PHE TYR LEU
SEQRES 27 C 545 HIS SER ARG LEU LEU GLU ARG ALA ALA LYS LEU SER GLU
SEQRES 28 C 545 LYS GLU GLY SER GLY SER LEU THR ALA LEU PRO VAL ILE
SEQRES 29 C 545 GLU THR GLN GLY GLY ASP VAL SER ALA TYR ILE PRO THR
SEQRES 30 C 545 ASN VAL ILE SER ILE THR ASP GLY GLN ILE PHE LEU GLU
SEQRES 31 C 545 ALA GLU LEU PHE TYR LYS GLY ILE ARG PRO ALA ILE ASN
SEQRES 32 C 545 VAL GLY LEU SER VAL SER ARG VAL GLY SER ALA ALA GLN
SEQRES 33 C 545 VAL LYS ALA LEU LYS GLN VAL ALA GLY SER LEU LYS LEU
SEQRES 34 C 545 PHE LEU ALA GLN TYR ARG GLU VAL ALA ALA PHE ALA GLN
SEQRES 35 C 545 PHE GLY SER ASP LEU ASP ALA SER THR LYS GLN THR LEU
SEQRES 36 C 545 VAL ARG GLY GLU ARG LEU THR GLN LEU LEU LYS GLN ASN
SEQRES 37 C 545 GLN TYR SER PRO LEU ALA THR GLU GLU GLN VAL PRO LEU
SEQRES 38 C 545 ILE TYR ALA GLY VAL ASN GLY HIS LEU ASP GLY ILE GLU
SEQRES 39 C 545 LEU SER ARG ILE GLY GLU PHE GLU SER SER PHE LEU SER
SEQRES 40 C 545 TYR LEU LYS SER ASN HIS ASN GLU LEU LEU THR GLU ILE
SEQRES 41 C 545 ARG GLU LYS GLY GLU LEU SER LYS GLU LEU LEU ALA SER
SEQRES 42 C 545 LEU LYS SER ALA THR GLU SER PHE VAL ALA THR PHE
SEQRES 1 D 511 MET VAL LEU PRO ARG LEU TYR THR ALA THR SER ARG ALA
SEQRES 2 D 511 ALA PHE LYS ALA ALA LYS GLN SER ALA PRO LEU LEU SER
SEQRES 3 D 511 THR SER TRP LYS ARG CYS MET ALA SER ALA ALA GLN SER
SEQRES 4 D 511 THR PRO ILE THR GLY LYS VAL THR ALA VAL ILE GLY ALA
SEQRES 5 D 511 ILE VAL ASP VAL HIS PHE GLU GLN SER GLU LEU PRO ALA
SEQRES 6 D 511 ILE LEU ASN ALA LEU GLU ILE LYS THR PRO GLN GLY LYS
SEQRES 7 D 511 LEU VAL LEU GLU VAL ALA GLN HIS LEU GLY GLU ASN THR
SEQRES 8 D 511 VAL ARG THR ILE ALA MET ASP GLY THR GLU GLY LEU VAL
SEQRES 9 D 511 ARG GLY GLU LYS VAL LEU ASP THR GLY GLY PRO ILE SER
SEQRES 10 D 511 VAL PRO VAL GLY ARG GLU THR LEU GLY ARG ILE ILE ASN
SEQRES 11 D 511 VAL ILE GLY GLU PRO ILE ASP GLU ARG GLY PRO ILE LYS
SEQRES 12 D 511 SER LYS LEU ARG LYS PRO ILE HIS ALA ASP PRO PRO SER
SEQRES 13 D 511 PHE ALA GLU GLN SER THR SER ALA GLU ILE LEU GLU THR
SEQRES 14 D 511 GLY ILE LYS VAL VAL ASP LEU LEU ALA PRO TYR ALA ARG
SEQRES 15 D 511 GLY GLY LYS ILE GLY LEU PHE GLY GLY ALA GLY VAL GLY
SEQRES 16 D 511 LYS THR VAL PHE ILE GLN GLU LEU ILE ASN ASN ILE ALA
SEQRES 17 D 511 LYS ALA HIS GLY GLY PHE SER VAL PHE THR GLY VAL GLY
SEQRES 18 D 511 GLU ARG THR ARG GLU GLY ASN ASP LEU TYR ARG GLU MET
SEQRES 19 D 511 LYS GLU THR GLY VAL ILE ASN LEU GLU GLY GLU SER LYS
SEQRES 20 D 511 VAL ALA LEU VAL PHE GLY GLN MET ASN GLU PRO PRO GLY
SEQRES 21 D 511 ALA ARG ALA ARG VAL ALA LEU THR GLY LEU THR ILE ALA
SEQRES 22 D 511 GLU TYR PHE ARG ASP GLU GLU GLY GLN ASP VAL LEU LEU
SEQRES 23 D 511 PHE ILE ASP ASN ILE PHE ARG PHE THR GLN ALA GLY SER
SEQRES 24 D 511 GLU VAL SER ALA LEU LEU GLY ARG ILE PRO SER ALA VAL
SEQRES 25 D 511 GLY TYR GLN PRO THR LEU ALA THR ASP MET GLY LEU LEU
SEQRES 26 D 511 GLN GLU ARG ILE THR THR THR LYS LYS GLY SER VAL THR
SEQRES 27 D 511 SER VAL GLN ALA VAL TYR VAL PRO ALA ASP ASP LEU THR
SEQRES 28 D 511 ASP PRO ALA PRO ALA THR THR PHE ALA HIS LEU ASP ALA
SEQRES 29 D 511 THR THR VAL LEU SER ARG GLY ILE SER GLU LEU GLY ILE
SEQRES 30 D 511 TYR PRO ALA VAL ASP PRO LEU ASP SER LYS SER ARG LEU
SEQRES 31 D 511 LEU ASP ALA ALA VAL VAL GLY GLN GLU HIS TYR ASP VAL
SEQRES 32 D 511 ALA SER LYS VAL GLN GLU THR LEU GLN THR TYR LYS SER
SEQRES 33 D 511 LEU GLN ASP ILE ILE ALA ILE LEU GLY MET ASP GLU LEU
SEQRES 34 D 511 SER GLU GLN ASP LYS LEU THR VAL GLU ARG ALA ARG LYS
SEQRES 35 D 511 ILE GLN ARG PHE LEU SER GLN PRO PHE ALA VAL ALA GLU
SEQRES 36 D 511 VAL PHE THR GLY ILE PRO GLY LYS LEU VAL ARG LEU LYS
SEQRES 37 D 511 ASP THR VAL ALA SER PHE LYS ALA VAL LEU GLU GLY LYS
SEQRES 38 D 511 TYR ASP ASN ILE PRO GLU HIS ALA PHE TYR MET VAL GLY
SEQRES 39 D 511 GLY ILE GLU ASP VAL VAL ALA LYS ALA GLU LYS LEU ALA
SEQRES 40 D 511 ALA GLU ALA ASN
SEQRES 1 E 511 MET VAL LEU PRO ARG LEU TYR THR ALA THR SER ARG ALA
SEQRES 2 E 511 ALA PHE LYS ALA ALA LYS GLN SER ALA PRO LEU LEU SER
SEQRES 3 E 511 THR SER TRP LYS ARG CYS MET ALA SER ALA ALA GLN SER
SEQRES 4 E 511 THR PRO ILE THR GLY LYS VAL THR ALA VAL ILE GLY ALA
SEQRES 5 E 511 ILE VAL ASP VAL HIS PHE GLU GLN SER GLU LEU PRO ALA
SEQRES 6 E 511 ILE LEU ASN ALA LEU GLU ILE LYS THR PRO GLN GLY LYS
SEQRES 7 E 511 LEU VAL LEU GLU VAL ALA GLN HIS LEU GLY GLU ASN THR
SEQRES 8 E 511 VAL ARG THR ILE ALA MET ASP GLY THR GLU GLY LEU VAL
SEQRES 9 E 511 ARG GLY GLU LYS VAL LEU ASP THR GLY GLY PRO ILE SER
SEQRES 10 E 511 VAL PRO VAL GLY ARG GLU THR LEU GLY ARG ILE ILE ASN
SEQRES 11 E 511 VAL ILE GLY GLU PRO ILE ASP GLU ARG GLY PRO ILE LYS
SEQRES 12 E 511 SER LYS LEU ARG LYS PRO ILE HIS ALA ASP PRO PRO SER
SEQRES 13 E 511 PHE ALA GLU GLN SER THR SER ALA GLU ILE LEU GLU THR
SEQRES 14 E 511 GLY ILE LYS VAL VAL ASP LEU LEU ALA PRO TYR ALA ARG
SEQRES 15 E 511 GLY GLY LYS ILE GLY LEU PHE GLY GLY ALA GLY VAL GLY
SEQRES 16 E 511 LYS THR VAL PHE ILE GLN GLU LEU ILE ASN ASN ILE ALA
SEQRES 17 E 511 LYS ALA HIS GLY GLY PHE SER VAL PHE THR GLY VAL GLY
SEQRES 18 E 511 GLU ARG THR ARG GLU GLY ASN ASP LEU TYR ARG GLU MET
SEQRES 19 E 511 LYS GLU THR GLY VAL ILE ASN LEU GLU GLY GLU SER LYS
SEQRES 20 E 511 VAL ALA LEU VAL PHE GLY GLN MET ASN GLU PRO PRO GLY
SEQRES 21 E 511 ALA ARG ALA ARG VAL ALA LEU THR GLY LEU THR ILE ALA
SEQRES 22 E 511 GLU TYR PHE ARG ASP GLU GLU GLY GLN ASP VAL LEU LEU
SEQRES 23 E 511 PHE ILE ASP ASN ILE PHE ARG PHE THR GLN ALA GLY SER
SEQRES 24 E 511 GLU VAL SER ALA LEU LEU GLY ARG ILE PRO SER ALA VAL
SEQRES 25 E 511 GLY TYR GLN PRO THR LEU ALA THR ASP MET GLY LEU LEU
SEQRES 26 E 511 GLN GLU ARG ILE THR THR THR LYS LYS GLY SER VAL THR
SEQRES 27 E 511 SER VAL GLN ALA VAL TYR VAL PRO ALA ASP ASP LEU THR
SEQRES 28 E 511 ASP PRO ALA PRO ALA THR THR PHE ALA HIS LEU ASP ALA
SEQRES 29 E 511 THR THR VAL LEU SER ARG GLY ILE SER GLU LEU GLY ILE
SEQRES 30 E 511 TYR PRO ALA VAL ASP PRO LEU ASP SER LYS SER ARG LEU
SEQRES 31 E 511 LEU ASP ALA ALA VAL VAL GLY GLN GLU HIS TYR ASP VAL
SEQRES 32 E 511 ALA SER LYS VAL GLN GLU THR LEU GLN THR TYR LYS SER
SEQRES 33 E 511 LEU GLN ASP ILE ILE ALA ILE LEU GLY MET ASP GLU LEU
SEQRES 34 E 511 SER GLU GLN ASP LYS LEU THR VAL GLU ARG ALA ARG LYS
SEQRES 35 E 511 ILE GLN ARG PHE LEU SER GLN PRO PHE ALA VAL ALA GLU
SEQRES 36 E 511 VAL PHE THR GLY ILE PRO GLY LYS LEU VAL ARG LEU LYS
SEQRES 37 E 511 ASP THR VAL ALA SER PHE LYS ALA VAL LEU GLU GLY LYS
SEQRES 38 E 511 TYR ASP ASN ILE PRO GLU HIS ALA PHE TYR MET VAL GLY
SEQRES 39 E 511 GLY ILE GLU ASP VAL VAL ALA LYS ALA GLU LYS LEU ALA
SEQRES 40 E 511 ALA GLU ALA ASN
SEQRES 1 F 511 MET VAL LEU PRO ARG LEU TYR THR ALA THR SER ARG ALA
SEQRES 2 F 511 ALA PHE LYS ALA ALA LYS GLN SER ALA PRO LEU LEU SER
SEQRES 3 F 511 THR SER TRP LYS ARG CYS MET ALA SER ALA ALA GLN SER
SEQRES 4 F 511 THR PRO ILE THR GLY LYS VAL THR ALA VAL ILE GLY ALA
SEQRES 5 F 511 ILE VAL ASP VAL HIS PHE GLU GLN SER GLU LEU PRO ALA
SEQRES 6 F 511 ILE LEU ASN ALA LEU GLU ILE LYS THR PRO GLN GLY LYS
SEQRES 7 F 511 LEU VAL LEU GLU VAL ALA GLN HIS LEU GLY GLU ASN THR
SEQRES 8 F 511 VAL ARG THR ILE ALA MET ASP GLY THR GLU GLY LEU VAL
SEQRES 9 F 511 ARG GLY GLU LYS VAL LEU ASP THR GLY GLY PRO ILE SER
SEQRES 10 F 511 VAL PRO VAL GLY ARG GLU THR LEU GLY ARG ILE ILE ASN
SEQRES 11 F 511 VAL ILE GLY GLU PRO ILE ASP GLU ARG GLY PRO ILE LYS
SEQRES 12 F 511 SER LYS LEU ARG LYS PRO ILE HIS ALA ASP PRO PRO SER
SEQRES 13 F 511 PHE ALA GLU GLN SER THR SER ALA GLU ILE LEU GLU THR
SEQRES 14 F 511 GLY ILE LYS VAL VAL ASP LEU LEU ALA PRO TYR ALA ARG
SEQRES 15 F 511 GLY GLY LYS ILE GLY LEU PHE GLY GLY ALA GLY VAL GLY
SEQRES 16 F 511 LYS THR VAL PHE ILE GLN GLU LEU ILE ASN ASN ILE ALA
SEQRES 17 F 511 LYS ALA HIS GLY GLY PHE SER VAL PHE THR GLY VAL GLY
SEQRES 18 F 511 GLU ARG THR ARG GLU GLY ASN ASP LEU TYR ARG GLU MET
SEQRES 19 F 511 LYS GLU THR GLY VAL ILE ASN LEU GLU GLY GLU SER LYS
SEQRES 20 F 511 VAL ALA LEU VAL PHE GLY GLN MET ASN GLU PRO PRO GLY
SEQRES 21 F 511 ALA ARG ALA ARG VAL ALA LEU THR GLY LEU THR ILE ALA
SEQRES 22 F 511 GLU TYR PHE ARG ASP GLU GLU GLY GLN ASP VAL LEU LEU
SEQRES 23 F 511 PHE ILE ASP ASN ILE PHE ARG PHE THR GLN ALA GLY SER
SEQRES 24 F 511 GLU VAL SER ALA LEU LEU GLY ARG ILE PRO SER ALA VAL
SEQRES 25 F 511 GLY TYR GLN PRO THR LEU ALA THR ASP MET GLY LEU LEU
SEQRES 26 F 511 GLN GLU ARG ILE THR THR THR LYS LYS GLY SER VAL THR
SEQRES 27 F 511 SER VAL GLN ALA VAL TYR VAL PRO ALA ASP ASP LEU THR
SEQRES 28 F 511 ASP PRO ALA PRO ALA THR THR PHE ALA HIS LEU ASP ALA
SEQRES 29 F 511 THR THR VAL LEU SER ARG GLY ILE SER GLU LEU GLY ILE
SEQRES 30 F 511 TYR PRO ALA VAL ASP PRO LEU ASP SER LYS SER ARG LEU
SEQRES 31 F 511 LEU ASP ALA ALA VAL VAL GLY GLN GLU HIS TYR ASP VAL
SEQRES 32 F 511 ALA SER LYS VAL GLN GLU THR LEU GLN THR TYR LYS SER
SEQRES 33 F 511 LEU GLN ASP ILE ILE ALA ILE LEU GLY MET ASP GLU LEU
SEQRES 34 F 511 SER GLU GLN ASP LYS LEU THR VAL GLU ARG ALA ARG LYS
SEQRES 35 F 511 ILE GLN ARG PHE LEU SER GLN PRO PHE ALA VAL ALA GLU
SEQRES 36 F 511 VAL PHE THR GLY ILE PRO GLY LYS LEU VAL ARG LEU LYS
SEQRES 37 F 511 ASP THR VAL ALA SER PHE LYS ALA VAL LEU GLU GLY LYS
SEQRES 38 F 511 TYR ASP ASN ILE PRO GLU HIS ALA PHE TYR MET VAL GLY
SEQRES 39 F 511 GLY ILE GLU ASP VAL VAL ALA LYS ALA GLU LYS LEU ALA
SEQRES 40 F 511 ALA GLU ALA ASN
SEQRES 1 G 311 MET LEU SER ARG ILE VAL SER ASN ASN ALA THR ARG SER
SEQRES 2 G 311 VAL MET CYS HIS GLN ALA GLN VAL GLY ILE LEU TYR LYS
SEQRES 3 G 311 THR ASN PRO VAL ARG THR TYR ALA THR LEU LYS GLU VAL
SEQRES 4 G 311 GLU MET ARG LEU LYS SER ILE LYS ASN ILE GLU LYS ILE
SEQRES 5 G 311 THR LYS THR MET LYS ILE VAL ALA SER THR ARG LEU SER
SEQRES 6 G 311 LYS ALA GLU LYS ALA LYS ILE SER ALA LYS LYS MET ASP
SEQRES 7 G 311 GLU ALA GLU GLN LEU PHE TYR LYS ASN ALA GLU THR LYS
SEQRES 8 G 311 ASN LEU ASP VAL GLU ALA THR GLU THR GLY ALA PRO LYS
SEQRES 9 G 311 GLU LEU ILE VAL ALA ILE THR SER ASP LYS GLY LEU CYS
SEQRES 10 G 311 GLY SER ILE HIS SER GLN LEU ALA LYS ALA VAL ARG ARG
SEQRES 11 G 311 HIS LEU ASN ASP GLN PRO ASN ALA ASP ILE VAL THR ILE
SEQRES 12 G 311 GLY ASP LYS ILE LYS MET GLN LEU LEU ARG THR HIS PRO
SEQRES 13 G 311 ASN ASN ILE LYS LEU SER ILE ASN GLY ILE GLY LYS ASP
SEQRES 14 G 311 ALA PRO THR PHE GLN GLU SER ALA LEU ILE ALA ASP LYS
SEQRES 15 G 311 LEU LEU SER VAL MET LYS ALA GLY THR TYR PRO LYS ILE
SEQRES 16 G 311 SER ILE PHE TYR ASN ASP PRO VAL SER SER LEU SER PHE
SEQRES 17 G 311 GLU PRO SER GLU LYS PRO ILE PHE ASN ALA LYS THR ILE
SEQRES 18 G 311 GLU GLN SER PRO SER PHE GLY LYS PHE GLU ILE ASP THR
SEQRES 19 G 311 ASP ALA ASN VAL PRO ARG ASP LEU PHE GLU TYR THR LEU
SEQRES 20 G 311 ALA ASN GLN MET LEU THR ALA MET ALA GLN GLY TYR ALA
SEQRES 21 G 311 ALA GLU ILE SER ALA ARG ARG ASN ALA MET ASP ASN ALA
SEQRES 22 G 311 SER LYS ASN ALA GLY ASP MET ILE ASN ARG TYR SER ILE
SEQRES 23 G 311 LEU TYR ASN ARG THR ARG GLN ALA VAL ILE THR ASN GLU
SEQRES 24 G 311 LEU VAL ASP ILE ILE THR GLY ALA SER SER LEU GLY
SEQRES 1 H 160 MET LEU ARG SER ILE ILE GLY LYS SER ALA SER ARG SER
SEQRES 2 H 160 LEU ASN PHE VAL ALA LYS ARG SER TYR ALA GLU ALA ALA
SEQRES 3 H 160 ALA ALA SER SER GLY LEU LYS LEU GLN PHE ALA LEU PRO
SEQRES 4 H 160 HIS GLU THR LEU TYR SER GLY SER GLU VAL THR GLN VAL
SEQRES 5 H 160 ASN LEU PRO ALA LYS SER GLY ARG ILE GLY VAL LEU ALA
SEQRES 6 H 160 ASN HIS VAL PRO THR VAL GLU GLN LEU LEU PRO GLY VAL
SEQRES 7 H 160 VAL GLU VAL MET GLU GLY SER ASN SER LYS LYS PHE PHE
SEQRES 8 H 160 ILE SER GLY GLY PHE ALA THR VAL GLN PRO ASP SER GLN
SEQRES 9 H 160 LEU CYS VAL THR ALA ILE GLU ALA PHE PRO LEU GLU SER
SEQRES 10 H 160 PHE SER GLN GLU ASN ILE LYS ASN LEU LEU ALA GLU ALA
SEQRES 11 H 160 LYS LYS ASN VAL SER SER SER ASP ALA ARG GLU ALA ALA
SEQRES 12 H 160 GLU ALA ALA ILE GLN VAL GLU VAL LEU GLU ASN LEU GLN
SEQRES 13 H 160 SER VAL LEU LYS
SEQRES 1 I 61 SER ALA TRP ARG LYS ALA GLY MET SER TYR ALA ALA TYR
SEQRES 2 I 61 LEU ASN VAL ALA ALA GLN ALA ILE ARG SER SER LEU LYS
SEQRES 3 I 61 THR GLU LEU GLN THR ALA SER VAL THR ASN ARG SER GLN
SEQRES 4 I 61 THR ASP ALA PHE TYR THR GLN TYR LYS ASN GLY THR ALA
SEQRES 5 I 61 ALA SER GLU PRO THR PRO MET THR LYS
SEQRES 1 K 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 K 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 K 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 K 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 K 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 K 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 L 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 L 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 L 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 L 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 L 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 L 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 M 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 M 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 M 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 M 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 M 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 M 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 N 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 N 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 N 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 N 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 N 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 N 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 O 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 O 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 O 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 O 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 O 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 O 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 P 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 P 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 P 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 P 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 P 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 P 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 Q 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 Q 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 Q 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 Q 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 Q 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 Q 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 R 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 R 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 R 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 R 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 R 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 R 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 S 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 S 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 S 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 S 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 S 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 S 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
SEQRES 1 T 76 MET GLN LEU VAL LEU ALA ALA LYS TYR ILE GLY ALA GLY
SEQRES 2 T 76 ILE SER THR ILE GLY LEU LEU GLY ALA GLY ILE GLY ILE
SEQRES 3 T 76 ALA ILE VAL PHE ALA ALA LEU ILE ASN GLY VAL SER ARG
SEQRES 4 T 76 ASN PRO SER ILE LYS ASP THR VAL PHE PRO MET ALA ILE
SEQRES 5 T 76 LEU GLY PHE ALA LEU SER GLU ALA THR GLY LEU PHE CYS
SEQRES 6 T 76 LEU MET VAL SER PHE LEU LEU LEU PHE GLY VAL
HET ANP A 600 31
HET MG A 700 1
HET ANP B 600 31
HET MG B 700 1
HET ANP C 600 31
HET MG C 700 1
HET ANP D 600 31
HET MG D 700 1
HET ANP F 600 31
HET MG F 700 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 20 ANP 5(C10 H17 N6 O12 P3)
FORMUL 21 MG 5(MG 2+)
HELIX 1 1 SER A 80 VAL A 84 5 5
HELIX 2 2 LEU A 152 VAL A 159 1 8
HELIX 3 3 GLY A 176 ASN A 187 1 12
HELIX 4 4 GLN A 188 ASN A 193 1 6
HELIX 5 5 ASP A 196 LYS A 200 5 5
HELIX 6 6 LYS A 211 GLU A 223 1 13
HELIX 7 7 GLN A 224 ASP A 226 5 3
HELIX 8 8 ALA A 227 LYS A 229 5 3
HELIX 9 9 ALA A 241 ASN A 262 1 22
HELIX 10 10 ASP A 272 LEU A 287 1 16
HELIX 11 11 GLY A 292 TYR A 296 5 5
HELIX 12 12 ASP A 299 ARG A 310 1 12
HELIX 13 13 SER A 315 GLY A 319 5 5
HELIX 14 14 ALA A 338 SER A 346 1 9
HELIX 15 15 GLU A 355 GLY A 362 1 8
HELIX 16 16 VAL A 376 GLN A 381 5 6
HELIX 17 17 VAL A 382 VAL A 388 1 7
HELIX 18 18 SER A 391 VAL A 402 1 12
HELIX 19 19 ALA A 403 GLN A 407 5 5
HELIX 20 20 ASP A 413 LEU A 430 1 18
HELIX 21 21 ALA A 439 ASN A 452 1 14
HELIX 22 22 ARG A 462 GLY A 489 1 28
HELIX 23 23 SER A 492 THR A 509 1 18
HELIX 24 24 SER B 80 VAL B 84 5 5
HELIX 25 25 GLY B 102 LEU B 106 5 5
HELIX 26 26 LEU B 152 VAL B 159 1 8
HELIX 27 27 GLY B 176 GLN B 188 1 13
HELIX 28 28 GLN B 188 ASN B 193 1 6
HELIX 29 29 LYS B 211 GLN B 224 1 14
HELIX 30 30 ALA B 241 ASN B 262 1 22
HELIX 31 31 ASP B 272 LEU B 287 1 16
HELIX 32 32 GLY B 292 TYR B 296 5 5
HELIX 33 33 ASP B 299 GLU B 309 1 11
HELIX 34 34 SER B 315 GLY B 319 5 5
HELIX 35 35 ALA B 338 SER B 346 1 9
HELIX 36 36 GLU B 355 LYS B 361 1 7
HELIX 37 37 ASN B 368 SER B 372 5 5
HELIX 38 38 VAL B 382 ALA B 389 1 8
HELIX 39 39 SER B 391 GLN B 398 1 8
HELIX 40 40 TYR B 399 ALA B 404 1 6
HELIX 41 41 LYS B 417 LYS B 431 1 15
HELIX 42 42 ALA B 439 ASN B 452 1 14
HELIX 43 43 GLU B 459 SER B 461 5 3
HELIX 44 44 ARG B 462 LYS B 475 1 14
HELIX 45 45 HIS B 478 LYS B 488 1 11
HELIX 46 46 SER B 492 LYS B 500 1 9
HELIX 47 47 THR B 503 THR B 509 1 7
HELIX 48 48 GLY C 102 LEU C 106 5 5
HELIX 49 49 LEU C 152 VAL C 159 1 8
HELIX 50 50 GLY C 176 GLN C 188 1 13
HELIX 51 51 GLN C 188 ASN C 193 1 6
HELIX 52 52 ASP C 196 LYS C 200 5 5
HELIX 53 53 LYS C 211 HIS C 225 1 15
HELIX 54 54 ALA C 227 LYS C 229 5 3
HELIX 55 55 ALA C 241 ASN C 262 1 22
HELIX 56 56 ASP C 272 ARG C 288 1 17
HELIX 57 57 GLY C 292 TYR C 296 5 5
HELIX 58 58 ASP C 299 GLU C 309 1 11
HELIX 59 59 SER C 315 GLY C 319 5 5
HELIX 60 60 ALA C 338 THR C 348 1 11
HELIX 61 61 GLU C 355 LYS C 361 1 7
HELIX 62 62 VAL C 376 GLN C 381 5 6
HELIX 63 63 VAL C 382 ALA C 389 1 8
HELIX 64 64 SER C 391 ALA C 406 1 16
HELIX 65 65 GLN C 407 GLY C 409 5 3
HELIX 66 66 SER C 415 LEU C 430 1 16
HELIX 67 67 ALA C 439 ASN C 452 1 14
HELIX 68 68 ARG C 462 ASN C 477 1 16
HELIX 69 69 HIS C 478 GLY C 489 1 12
HELIX 70 70 SER C 492 ALA C 508 1 17
HELIX 71 71 GLY D 88 LEU D 92 5 5
HELIX 72 72 SER D 123 GLU D 126 5 4
HELIX 73 73 ILE D 138 ALA D 145 1 8
HELIX 74 74 GLY D 162 HIS D 178 1 17
HELIX 75 75 ARG D 190 GLY D 205 1 16
HELIX 76 76 PRO D 225 ALA D 230 1 6
HELIX 77 77 ARG D 231 GLU D 246 1 16
HELIX 78 78 ILE D 258 ALA D 270 1 13
HELIX 79 79 SER D 277 TYR D 281 5 5
HELIX 80 80 THR D 284 GLU D 294 1 11
HELIX 81 81 PRO D 313 ASP D 316 5 4
HELIX 82 82 ASP D 319 PHE D 326 1 8
HELIX 83 83 ALA D 327 LEU D 329 5 3
HELIX 84 84 SER D 336 LEU D 342 1 7
HELIX 85 85 ASP D 359 GLY D 364 1 6
HELIX 86 86 GLY D 364 GLY D 392 1 29
HELIX 87 87 SER D 397 LEU D 414 1 18
HELIX 88 88 ALA D 421 GLY D 426 1 6
HELIX 89 89 ARG D 433 GLU D 446 1 14
HELIX 90 90 PRO D 453 TYR D 458 5 6
HELIX 91 91 GLY D 462 ALA D 475 1 14
HELIX 92 92 GLY E 88 LEU E 92 5 5
HELIX 93 93 ILE E 138 ALA E 145 1 8
HELIX 94 94 GLY E 162 ALA E 177 1 16
HELIX 95 95 ARG E 190 THR E 204 1 15
HELIX 96 96 PRO E 225 GLU E 246 1 22
HELIX 97 97 ASN E 257 LEU E 272 1 16
HELIX 98 98 SER E 277 TYR E 281 5 5
HELIX 99 99 THR E 284 GLU E 294 1 11
HELIX 100 100 VAL E 312 ASP E 316 5 5
HELIX 101 101 ASP E 319 ALA E 327 1 9
HELIX 102 102 SER E 336 LEU E 342 1 7
HELIX 103 103 ASP E 359 GLY E 364 1 6
HELIX 104 104 GLY E 364 GLN E 385 1 22
HELIX 105 105 ILE E 387 GLY E 392 1 6
HELIX 106 106 SER E 397 LEU E 414 1 18
HELIX 107 107 ALA E 421 GLY E 426 1 6
HELIX 108 108 ARG E 433 GLU E 446 1 14
HELIX 109 109 ILE E 463 ALA E 474 1 12
HELIX 110 110 GLY F 88 LEU F 92 5 5
HELIX 111 111 ILE F 138 ALA F 145 1 8
HELIX 112 112 GLY F 162 ALA F 177 1 16
HELIX 113 113 ARG F 190 GLY F 205 1 16
HELIX 114 114 PRO F 225 ALA F 230 1 6
HELIX 115 115 ARG F 231 GLU F 246 1 16
HELIX 116 116 ILE F 258 ALA F 270 1 13
HELIX 117 117 SER F 277 TYR F 281 5 5
HELIX 118 118 THR F 284 GLU F 294 1 11
HELIX 119 119 PRO F 313 ASP F 316 5 4
HELIX 120 120 ASP F 319 PHE F 326 1 8
HELIX 121 121 ALA F 327 LEU F 329 5 3
HELIX 122 122 SER F 336 LEU F 342 1 7
HELIX 123 123 ASP F 359 GLY F 364 1 6
HELIX 124 124 GLY F 364 LEU F 391 1 28
HELIX 125 125 GLY F 392 LEU F 396 5 5
HELIX 126 126 SER F 397 SER F 415 1 19
HELIX 127 127 ALA F 421 GLY F 426 1 6
HELIX 128 128 ARG F 433 GLU F 446 1 14
HELIX 129 129 PRO F 453 TYR F 458 5 6
HELIX 130 130 GLY F 462 ALA F 474 1 13
HELIX 131 131 THR G 2 ALA G 37 1 36
HELIX 132 132 LYS G 43 ALA G 55 1 13
HELIX 133 133 SER G 86 HIS G 98 1 13
HELIX 134 134 GLY G 111 ARG G 120 1 10
HELIX 135 135 THR G 139 VAL G 153 1 15
HELIX 136 136 ASN G 184 SER G 191 1 8
HELIX 137 137 PRO G 192 PHE G 197 5 6
HELIX 138 138 ASN G 204 SER G 276 1 73
HELIX 139 139 GLU H 99 SER H 114 1 16
HELIX 140 140 ALA H 120 SER H 135 1 16
HELIX 141 141 ALA I 12 VAL I 16 5 5
HELIX 142 142 ALA I 32 SER I 38 1 7
HELIX 143 143 LEU K 5 SER K 15 1 11
HELIX 144 144 GLY K 18 SER K 38 1 21
HELIX 145 145 THR K 46 ALA K 51 1 6
HELIX 146 146 ILE K 52 LEU K 72 1 21
HELIX 147 147 GLN L 2 SER L 15 1 14
HELIX 148 148 GLY L 18 SER L 38 1 21
HELIX 149 149 THR L 46 LEU L 72 1 27
HELIX 150 150 GLN M 2 SER M 15 1 14
HELIX 151 151 GLY M 18 SER M 38 1 21
HELIX 152 152 VAL M 47 ILE M 52 1 6
HELIX 153 153 ILE M 52 LEU M 72 1 21
HELIX 154 154 GLN N 2 SER N 15 1 14
HELIX 155 155 GLY N 18 SER N 38 1 21
HELIX 156 156 SER N 42 THR N 46 1 5
HELIX 157 157 VAL N 47 LEU N 72 1 26
HELIX 158 158 MET O 1 SER O 15 1 15
HELIX 159 159 GLY O 18 SER O 38 1 21
HELIX 160 160 SER O 42 THR O 46 1 5
HELIX 161 161 VAL O 47 ILE O 52 1 6
HELIX 162 162 ILE O 52 LEU O 72 1 21
HELIX 163 163 MET P 1 SER P 15 1 15
HELIX 164 164 GLY P 18 SER P 38 1 21
HELIX 165 165 THR P 46 LEU P 72 1 27
HELIX 166 166 GLN Q 2 SER Q 15 1 14
HELIX 167 167 GLY Q 18 SER Q 38 1 21
HELIX 168 168 THR Q 46 LEU Q 72 1 27
HELIX 169 169 MET R 1 SER R 15 1 15
HELIX 170 170 GLY R 18 VAL R 37 1 20
HELIX 171 171 SER R 42 THR R 46 1 5
HELIX 172 172 VAL R 47 LEU R 72 1 26
HELIX 173 173 GLN S 2 SER S 15 1 14
HELIX 174 174 GLY S 18 SER S 38 1 21
HELIX 175 175 SER S 42 THR S 46 1 5
HELIX 176 176 VAL S 47 LEU S 72 1 26
HELIX 177 177 GLN T 2 SER T 15 1 14
HELIX 178 178 GLY T 18 SER T 38 1 21
HELIX 179 179 THR T 46 LEU T 72 1 27
SHEET 1 1 1 THR A 30 GLY A 37 0
SHEET 1 2 1 ILE A 40 GLY A 45 0
SHEET 1 3 1 GLU A 53 PHE A 57 0
SHEET 1 4 1 LYS A 62 LEU A 68 0
SHEET 1 5 1 GLN A 72 LEU A 77 0
SHEET 1 6 1 LEU A 89 ILE A 96 0
SHEET 1 7 1 ASP A 98 VAL A 101 0
SHEET 1 8 1 VAL A 109 ASP A 111 0
SHEET 1 9 1 GLY A 127 ARG A 130 0
SHEET 1 10 1 PRO A 147 VAL A 148 0
SHEET 1 11 1 ILE A 161 GLY A 162 0
SHEET 1 12 1 LEU A 168 GLY A 171 0
SHEET 1 13 1 TYR A 202 VAL A 208 0
SHEET 1 14 1 SER A 231 ALA A 236 0
SHEET 1 15 1 HIS A 265 ASP A 271 0
SHEET 1 16 1 ALA A 312 LYS A 313 0
SHEET 1 17 1 SER A 322 GLU A 330 0
SHEET 1 18 1 GLY A 350 LEU A 354 0
SHEET 1 19 1 ILE A 367 SER A 374 0
SHEET 1 20 1 THR B 30 GLY B 37 0
SHEET 1 21 1 ILE B 40 GLY B 45 0
SHEET 1 22 1 GLU B 53 PHE B 57 0
SHEET 1 23 1 LYS B 62 LEU B 68 0
SHEET 1 24 1 GLN B 72 LEU B 77 0
SHEET 1 25 1 LEU B 89 ILE B 96 0
SHEET 1 26 1 ASP B 98 VAL B 101 0
SHEET 1 27 1 VAL B 109 VAL B 110 0
SHEET 1 28 1 GLY B 127 ARG B 130 0
SHEET 1 29 1 LEU B 168 ASP B 172 0
SHEET 1 30 1 TYR B 202 VAL B 208 0
SHEET 1 31 1 SER B 231 ALA B 236 0
SHEET 1 32 1 HIS B 265 ASP B 271 0
SHEET 1 33 1 SER B 322 LEU B 323 0
SHEET 1 34 1 LEU B 326 THR B 331 0
SHEET 1 35 1 GLY B 350 LEU B 354 0
SHEET 1 36 1 VAL B 373 SER B 374 0
SHEET 1 37 1 THR C 30 GLY C 37 0
SHEET 1 38 1 ILE C 40 GLY C 45 0
SHEET 1 39 1 GLU C 53 PHE C 57 0
SHEET 1 40 1 LYS C 62 LEU C 68 0
SHEET 1 41 1 VAL C 73 LEU C 77 0
SHEET 1 42 1 LEU C 89 ILE C 96 0
SHEET 1 43 1 ASP C 98 VAL C 101 0
SHEET 1 44 1 VAL C 109 ASP C 111 0
SHEET 1 45 1 GLY C 127 ARG C 130 0
SHEET 1 46 1 LEU C 168 GLY C 171 0
SHEET 1 47 1 TYR C 202 VAL C 208 0
SHEET 1 48 1 SER C 231 ALA C 236 0
SHEET 1 49 1 HIS C 265 ASP C 271 0
SHEET 1 50 1 ALA C 312 LYS C 313 0
SHEET 1 51 1 SER C 322 GLU C 330 0
SHEET 1 52 1 GLN C 351 LEU C 354 0
SHEET 1 53 1 THR D 10 ILE D 17 0
SHEET 1 54 1 ILE D 20 PHE D 25 0
SHEET 1 55 1 ALA D 36 LYS D 40 0
SHEET 1 56 1 LYS D 45 GLY D 55 0
SHEET 1 57 1 THR D 58 ALA D 63 0
SHEET 1 58 1 LYS D 75 ASP D 78 0
SHEET 1 59 1 SER D 84 PRO D 86 0
SHEET 1 60 1 ILE D 95 ASN D 97 0
SHEET 1 61 1 ARG D 114 PRO D 116 0
SHEET 1 62 1 LYS D 152 GLY D 157 0
SHEET 1 63 1 PHE D 181 VAL D 187 0
SHEET 1 64 1 VAL D 215 GLY D 220 0
SHEET 1 65 1 VAL D 251 ASP D 256 0
SHEET 1 66 1 VAL D 304 TYR D 311 0
SHEET 1 67 1 ALA D 331 VAL D 334 0
SHEET 1 68 1 LYS D 354 SER D 355 0
SHEET 1 69 1 THR E 10 ILE E 17 0
SHEET 1 70 1 ILE E 20 HIS E 24 0
SHEET 1 71 1 ALA E 36 LYS E 40 0
SHEET 1 72 1 LYS E 45 GLY E 55 0
SHEET 1 73 1 THR E 58 ALA E 63 0
SHEET 1 74 1 LYS E 75 ASP E 78 0
SHEET 1 75 1 SER E 84 PRO E 86 0
SHEET 1 76 1 ILE E 95 ILE E 96 0
SHEET 1 77 1 ARG E 114 PRO E 116 0
SHEET 1 78 1 ILE E 133 LEU E 134 0
SHEET 1 79 1 TYR E 147 ALA E 148 0
SHEET 1 80 1 LYS E 152 PHE E 156 0
SHEET 1 81 1 SER E 182 GLU E 189 0
SHEET 1 82 1 VAL E 215 GLN E 221 0
SHEET 1 83 1 ASP E 250 ASP E 256 0
SHEET 1 84 1 SER E 303 ALA E 309 0
SHEET 1 85 1 ALA E 331 VAL E 334 0
SHEET 1 86 1 ILE F 9 ILE F 17 0
SHEET 1 87 1 ILE F 20 PHE F 25 0
SHEET 1 88 1 ALA F 36 LYS F 40 0
SHEET 1 89 1 LYS F 45 GLY F 55 0
SHEET 1 90 1 THR F 58 ALA F 63 0
SHEET 1 91 1 LYS F 75 ASP F 78 0
SHEET 1 92 1 SER F 84 PRO F 86 0
SHEET 1 93 1 ILE F 95 ILE F 96 0
SHEET 1 94 1 ARG F 114 PRO F 116 0
SHEET 1 95 1 LYS F 152 GLY F 157 0
SHEET 1 96 1 PHE F 181 VAL F 187 0
SHEET 1 97 1 LEU F 217 GLY F 220 0
SHEET 1 98 1 VAL F 251 ASP F 256 0
SHEET 1 99 1 VAL F 304 TYR F 311 0
SHEET 1 100 1 ALA F 331 LEU F 335 0
SHEET 1 101 1 LYS F 354 SER F 355 0
SHEET 1 102 1 GLU G 72 ILE G 77 0
SHEET 1 103 1 ASP G 106 ILE G 110 0
SHEET 1 104 1 ILE G 126 ASN G 131 0
SHEET 1 105 1 LYS G 161 ASP G 168 0
SHEET 1 106 1 GLU G 176 ILE G 182 0
SHEET 1 107 1 GLN H 29 PRO H 33 0
SHEET 1 108 1 ARG H 38 LEU H 42 0
SHEET 1 109 1 VAL H 49 LEU H 52 0
SHEET 1 110 1 VAL H 57 VAL H 59 0
SHEET 1 111 1 LYS H 66 PHE H 68 0
SHEET 1 112 1 GLY H 73 VAL H 77 0
SHEET 1 113 1 LEU H 83 ALA H 87 0
SHEET 1 114 1 PHE I 43 GLN I 46 0
SHEET 1 115 1 PRO I 58 THR I 60 0
LINK OG1 THR A 178 MG MG A 700 1555 1555 2.14
LINK O2G ANP A 600 MG MG A 700 1555 1555 2.03
LINK O2B ANP A 600 MG MG A 700 1555 1555 1.97
LINK OG1 THR B 178 MG MG B 700 1555 1555 1.92
LINK O2B ANP B 600 MG MG B 700 1555 1555 2.57
LINK O2G ANP B 600 MG MG B 700 1555 1555 1.78
LINK OG1 THR C 178 MG MG C 700 1555 1555 2.00
LINK O2B ANP C 600 MG MG C 700 1555 1555 2.10
LINK O2G ANP C 600 MG MG C 700 1555 1555 1.81
LINK OG1 THR D 164 MG MG D 700 1555 1555 2.14
LINK O2B ANP D 600 MG MG D 700 1555 1555 2.27
LINK O2G ANP D 600 MG MG D 700 1555 1555 1.85
LINK OG1 THR F 164 MG MG F 700 1555 1555 1.77
LINK OE1 GLU F 189 MG MG F 700 1555 1555 2.80
LINK O2G ANP F 600 MG MG F 700 1555 1555 1.64
LINK O2B ANP F 600 MG MG F 700 1555 1555 2.30
CISPEP 1 ASP A 271 ASP A 272 0 0.57
CISPEP 2 ARG A 364 PRO A 365 0 9.52
CISPEP 3 ASP B 271 ASP B 272 0 -5.64
CISPEP 4 ARG B 364 PRO B 365 0 4.26
CISPEP 5 ASP C 271 ASP C 272 0 12.82
CISPEP 6 ARG C 364 PRO C 365 0 0.49
CISPEP 7 ASP D 256 ASN D 257 0 -1.86
CISPEP 8 TYR D 345 PRO D 346 0 -0.53
CISPEP 9 ASP E 256 ASN E 257 0 5.60
CISPEP 10 TYR E 345 PRO E 346 0 3.86
CISPEP 11 ASP F 256 ASN F 257 0 -0.64
CISPEP 12 TYR F 345 PRO F 346 0 3.54
CISPEP 13 ASN K 40 PRO K 41 0 -10.35
CISPEP 14 ASN L 40 PRO L 41 0 -14.07
CISPEP 15 ASN M 40 PRO M 41 0 11.29
CISPEP 16 ASN N 40 PRO N 41 0 -5.90
CISPEP 17 ASN O 40 PRO O 41 0 -6.73
CISPEP 18 ASN P 40 PRO P 41 0 -5.12
CISPEP 19 ASN Q 40 PRO Q 41 0 -18.44
CISPEP 20 ASN R 40 PRO R 41 0 -8.78
CISPEP 21 ASN S 40 PRO S 41 0 -4.36
CISPEP 22 ASN T 40 PRO T 41 0 -7.24
SITE 1 AC1 10 GLN A 174 GLY A 176 LYS A 177 THR A 178
SITE 2 AC1 10 ALA A 179 PHE A 359 ARG A 364 GLN A 432
SITE 3 AC1 10 GLN A 434 MG A 700
SITE 1 AC2 2 THR A 178 ANP A 600
SITE 1 AC3 13 ARG B 173 GLN B 174 THR B 175 GLY B 176
SITE 2 AC3 13 LYS B 177 THR B 178 ALA B 179 GLU B 330
SITE 3 AC3 13 PHE B 359 ARG B 364 GLN B 432 GLN B 434
SITE 4 AC3 13 MG B 700
SITE 1 AC4 2 THR B 178 ANP B 600
SITE 1 AC5 12 ARG C 173 GLN C 174 THR C 175 GLY C 176
SITE 2 AC5 12 LYS C 177 THR C 178 ALA C 179 GLU C 330
SITE 3 AC5 12 GLN C 432 GLN C 434 MG C 700 TYR F 368
SITE 1 AC6 2 THR C 178 ANP C 600
SITE 1 AC7 17 SER C 346 ARG C 375 GLY D 158 ALA D 159
SITE 2 AC7 17 GLY D 160 VAL D 161 GLY D 162 LYS D 163
SITE 3 AC7 17 THR D 164 VAL D 165 GLU D 189 ARG D 190
SITE 4 AC7 17 TYR D 345 PHE D 418 ALA D 421 PHE D 424
SITE 5 AC7 17 MG D 700
SITE 1 AC8 5 THR D 164 GLU D 189 ARG D 190 GLU D 193
SITE 2 AC8 5 ANP D 600
SITE 1 AC9 19 ILE B 345 SER B 346 VAL B 373 ARG B 375
SITE 2 AC9 19 GLY F 158 ALA F 159 GLY F 160 VAL F 161
SITE 3 AC9 19 GLY F 162 LYS F 163 THR F 164 VAL F 165
SITE 4 AC9 19 GLU F 189 ARG F 190 TYR F 345 PHE F 418
SITE 5 AC9 19 ALA F 421 PHE F 424 MG F 700
SITE 1 BC1 4 THR F 164 GLU F 189 GLU F 193 ANP F 600
CRYST1 135.352 173.711 137.889 90.00 91.77 90.00 P 1 21 1 20
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 0.007388 0.000000 0.000228 0.00000
SCALE2 0.000000 0.005757 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007256 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
