HEADER LYASE 09-OCT-07 2VDI
TITLE CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH
TITLE 2 A LARGE-SUBUNIT C192S MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE LARGE
COMPND 5 CHAIN, RUBISCO LARGE SUBUNIT;
COMPND 6 EC: 4.1.1.39;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;
COMPND 11 CHAIN: I, J, K, L, M, N, O, P;
COMPND 12 SYNONYM: RUBISCO SMALL SUBUNIT 1,RIBULOSE-1,5-BISPHOSPHATE
COMPND 13 CARBOXYLASE SMALL CHAIN;
COMPND 14 EC: 4.1.1.39;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 3 ORGANISM_TAXID: 3055;
SOURCE 4 STRAIN: 18-7G;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLS-C192S;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 10 ORGANISM_TAXID: 3055;
SOURCE 11 STRAIN: 18-7G;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PLS-C192S
KEYWDS VICINAL CYSTEINES, CO2/O2 SPECIFICITY, PHOTOSYNTHESIS,
KEYWDS 2 TRANSIT PEPTIDE, PHOTORESPIRATION, METAL-BINDING,
KEYWDS 3 HYDROXYLATION, OXIDOREDUCTASE, METHYLATION, CHLOROPLAST,
KEYWDS 4 CALVIN CYCLE, MONOOXYGENASE, LYASE, RUBISCO, PLASTID,
KEYWDS 5 MAGNESIUM, ACETYLATION, CARBON DIOXIDE FIXATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.-J.GARCIA-MURRIA,S.KARKEHABADI,J.MARIN-NAVARRO,
AUTHOR 2 S.SATAGOPAN,I.ANDERSSON,R.J.SPREITZER,J.MORENO
REVDAT 3 24-FEB-09 2VDI 1 VERSN
REVDAT 2 11-NOV-08 2VDI 1 JRNL REMARK
REVDAT 1 04-NOV-08 2VDI 0
JRNL AUTH M.-J.GARCIA-MURRIA,S.KARKEHABADI,J.MARIN-NAVARRO,
JRNL AUTH 2 S.SATAGOPAN,I.ANDERSSON,R.J.SPREITZER,J.MORENO
JRNL TITL STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF THE
JRNL TITL 2 REPLACEMENT OF PROXIMAL RESIDUES CYS-172 AND CYS-
JRNL TITL 3 192 IN THE LARGE SUBUNIT OF RIBULOSE 1,5-
JRNL TITL 4 BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM
JRNL TITL 5 CHLAMYDOMONAS REINHARDTII
JRNL REF BIOCHEM.J. V. 411 241 2008
JRNL REFN ISSN 0264-6021
JRNL PMID 18072944
JRNL DOI 10.1042/BJ20071422
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 112065
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5907
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8248
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 451
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 37780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 756
REMARK 3 SOLVENT ATOMS : 1538
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.93000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : -0.62000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.30000
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): 0.392
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.774
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.840
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.828
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 39431 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 53411 ; 1.114 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4828 ; 5.665 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1840 ;32.243 ;23.174
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6308 ;15.645 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 312 ;16.517 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5674 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30331 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 19371 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 26824 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2243 ; 0.139 ; 0.200
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): 103 ; 0.314 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.417 ; 0.200
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): 24603 ; 0.493 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38631 ; 0.807 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 16916 ; 1.239 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14780 ; 1.973 ; 4.500
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 : 16
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 13 A 438 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3630 ; .00 ; .05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3630 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 13 B 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 B 440 B 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 3630 ; .03 ; .05
REMARK 3 TIGHT THERMAL 2 B (A**2): 3630 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 13 C 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 C 440 C 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 3630 ; .03 ; .05
REMARK 3 TIGHT THERMAL 3 C (A**2): 3630 ; .07 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 13 D 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 D 440 D 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 D (A): 3630 ; .03 ; .05
REMARK 3 TIGHT THERMAL 4 D (A**2): 3630 ; .07 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : E A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 13 E 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 E 440 E 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 E (A): 3629 ; .03 ; .05
REMARK 3 TIGHT THERMAL 5 E (A**2): 3629 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : F A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 F 13 F 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 F 440 F 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 F (A): 3630 ; .03 ; .05
REMARK 3 TIGHT THERMAL 6 F (A**2): 3630 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : G A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 13 G 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 G 440 G 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 G (A): 3630 ; .03 ; .05
REMARK 3 TIGHT THERMAL 7 G (A**2): 3630 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : H A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 13 H 438 1
REMARK 3 1 A 13 A 438 1
REMARK 3 2 H 440 H 477 1
REMARK 3 2 A 440 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 H (A): 3630 ; .03 ; .05
REMARK 3 TIGHT THERMAL 8 H (A**2): 3630 ; .07 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 I 1 I 83 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 I (A): 1121 ; .00 ; .05
REMARK 3 TIGHT THERMAL 9 I (A**2): 1121 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : J I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 J 1 J 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 J 85 J 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 J 131 J 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 J (A): 1121 ; .03 ; .05
REMARK 3 TIGHT THERMAL 10 J (A**2): 1121 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : K I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 K 1 K 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 K 85 K 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 K 131 K 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 K (A): 1121 ; .03 ; .05
REMARK 3 TIGHT THERMAL 11 K (A**2): 1121 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : L I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 1 L 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 L 85 L 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 L 131 L 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 L (A): 1121 ; .03 ; .05
REMARK 3 TIGHT THERMAL 12 L (A**2): 1121 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : M I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 M 1 M 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 M 85 M 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 M 131 M 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 13 M (A): 1121 ; .03 ; .05
REMARK 3 TIGHT THERMAL 13 M (A**2): 1121 ; .09 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : N I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 N 1 N 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 N 85 N 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 N 131 N 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 14 N (A): 1120 ; .03 ; .05
REMARK 3 TIGHT THERMAL 14 N (A**2): 1120 ; .07 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : O I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 O 1 O 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 O 85 O 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 O 131 O 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 15 O (A): 1121 ; .03 ; .05
REMARK 3 TIGHT THERMAL 15 O (A**2): 1121 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : P I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 P 1 P 83 1
REMARK 3 1 I 1 I 83 1
REMARK 3 2 P 85 P 129 1
REMARK 3 2 I 85 I 129 1
REMARK 3 3 P 131 P 140 1
REMARK 3 3 I 131 I 140 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 16 P (A): 1121 ; .03 ; .05
REMARK 3 TIGHT THERMAL 16 P (A**2): 1121 ; .08 ; .50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2VDI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-07.
REMARK 100 THE PDBE ID CODE IS EBI-34101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.098
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118474
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.65
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : 12.0
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.20
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 1GK8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 89.10300
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 GENERATING THE BIOMOLECULE
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 128190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 117940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -472 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS:J, K, L, M, N, O, P
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, CYS 192 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, CYS 192 TO SER
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 1
REMARK 465 VAL A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 LYS A 8
REMARK 465 ALA A 9
REMARK 465 GLY A 10
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 PRO B 3
REMARK 465 GLN B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 THR B 7
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 PRO C 3
REMARK 465 GLN C 4
REMARK 465 THR C 5
REMARK 465 GLU C 6
REMARK 465 THR C 7
REMARK 465 LYS C 8
REMARK 465 ALA C 9
REMARK 465 GLY C 10
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 PRO D 3
REMARK 465 GLN D 4
REMARK 465 THR D 5
REMARK 465 GLU D 6
REMARK 465 THR D 7
REMARK 465 LYS D 8
REMARK 465 ALA D 9
REMARK 465 GLY D 10
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 PRO E 3
REMARK 465 GLN E 4
REMARK 465 THR E 5
REMARK 465 GLU E 6
REMARK 465 THR E 7
REMARK 465 LYS E 8
REMARK 465 ALA E 9
REMARK 465 GLY E 10
REMARK 465 MET F 1
REMARK 465 VAL F 2
REMARK 465 PRO F 3
REMARK 465 GLN F 4
REMARK 465 THR F 5
REMARK 465 GLU F 6
REMARK 465 THR F 7
REMARK 465 LYS F 8
REMARK 465 ALA F 9
REMARK 465 GLY F 10
REMARK 465 MET G 1
REMARK 465 VAL G 2
REMARK 465 PRO G 3
REMARK 465 GLN G 4
REMARK 465 THR G 5
REMARK 465 GLU G 6
REMARK 465 THR G 7
REMARK 465 LYS G 8
REMARK 465 ALA G 9
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 PRO H 3
REMARK 465 GLN H 4
REMARK 465 THR H 5
REMARK 465 GLU H 6
REMARK 465 THR H 7
REMARK 465 LYS H 8
REMARK 465 ALA H 9
REMARK 465 GLY H 10
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 PHE N 132 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 OE1 GLU D 460 NZ LYS F 14 1557 1.89
REMARK 500 NZ LYS F 14 OE1 GLU D 460 1547 1.89
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 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 SER A 62 -77.65 -144.07
REMARK 500 THR A 75 -164.14 -117.32
REMARK 500 CYS A 172 127.61 -172.44
REMARK 500 ASN A 207 -90.86 -122.60
REMARK 500 MET A 212 110.41 -162.53
REMARK 500 TYR A 239 99.48 -65.57
REMARK 500 MET A 297 -11.55 87.52
REMARK 500 VAL A 331 -50.59 67.42
REMARK 500 ASP A 357 89.91 -157.75
REMARK 500 SER B 62 -76.09 -145.19
REMARK 500 THR B 75 -165.10 -114.14
REMARK 500 ASN B 207 -89.09 -122.26
REMARK 500 TYR B 239 98.22 -64.66
REMARK 500 MET B 297 -13.34 87.67
REMARK 500 VAL B 331 -49.57 70.70
REMARK 500 ASP B 357 91.70 -160.05
REMARK 500 SER C 62 -81.74 -141.48
REMARK 500 THR C 75 -164.73 -117.48
REMARK 500 CYS C 172 124.25 -174.57
REMARK 500 ASN C 207 -92.68 -126.24
REMARK 500 MET C 212 109.13 -162.32
REMARK 500 MET C 297 -15.02 96.05
REMARK 500 VAL C 331 -52.07 67.12
REMARK 500 LYS C 356 128.49 -37.11
REMARK 500 ASP C 357 87.23 -156.69
REMARK 500 SER D 62 -77.64 -146.77
REMARK 500 THR D 75 -166.72 -120.16
REMARK 500 CYS D 172 127.86 -174.78
REMARK 500 ASN D 207 -93.99 -120.72
REMARK 500 MET D 212 113.41 -165.68
REMARK 500 TYR D 239 97.58 -62.63
REMARK 500 MET D 297 -12.28 86.50
REMARK 500 VAL D 331 -49.61 67.60
REMARK 500 LYS D 356 129.24 -39.63
REMARK 500 SER E 62 -78.78 -143.45
REMARK 500 THR E 75 -163.52 -116.06
REMARK 500 CYS E 172 125.92 -170.78
REMARK 500 ASN E 207 -91.59 -121.41
REMARK 500 TYR E 239 99.87 -65.64
REMARK 500 MET E 297 -11.83 89.36
REMARK 500 VAL E 331 -49.97 67.67
REMARK 500 ASP E 357 91.25 -160.10
REMARK 500 SER F 62 -74.71 -136.56
REMARK 500 THR F 65 -165.72 -129.18
REMARK 500 THR F 75 -165.27 -116.07
REMARK 500 CYS F 172 131.28 -171.99
REMARK 500 ASN F 207 -90.72 -123.23
REMARK 500 MET F 212 110.21 -163.22
REMARK 500 TYR F 239 98.50 -64.07
REMARK 500 ARG F 295 31.71 -98.74
REMARK 500 MET F 297 -12.95 90.43
REMARK 500 VAL F 331 -52.29 68.73
REMARK 500 LYS F 356 129.39 -36.92
REMARK 500 ASP F 357 89.33 -158.84
REMARK 500 SER G 62 -79.40 -145.28
REMARK 500 THR G 65 -169.33 -129.44
REMARK 500 THR G 75 -166.78 -117.32
REMARK 500 ASN G 207 -89.80 -119.52
REMARK 500 MET G 212 115.76 -162.35
REMARK 500 TYR G 239 98.54 -67.71
REMARK 500 MET G 297 -9.33 85.22
REMARK 500 VAL G 331 -55.17 70.45
REMARK 500 ASP G 357 87.05 -156.60
REMARK 500 SER H 62 -78.81 -147.35
REMARK 500 THR H 65 -163.80 -129.42
REMARK 500 THR H 75 -160.97 -119.20
REMARK 500 ASN H 207 -91.32 -122.51
REMARK 500 MET H 212 109.87 -161.97
REMARK 500 MET H 297 -10.53 86.94
REMARK 500 VAL H 331 -48.45 66.68
REMARK 500 PHE I 12 47.93 -142.23
REMARK 500 GLU I 13 -141.60 57.00
REMARK 500 PHE I 15 -3.57 82.68
REMARK 500 LYS I 77 -123.80 55.21
REMARK 500 PHE J 12 48.64 -143.40
REMARK 500 GLU J 13 -146.53 54.85
REMARK 500 PHE J 15 -2.10 81.54
REMARK 500 LYS J 77 -121.39 52.69
REMARK 500 PHE K 12 46.67 -143.80
REMARK 500 GLU K 13 -138.56 57.62
REMARK 500 PHE K 15 -6.62 85.39
REMARK 500 SER K 62 49.26 -87.02
REMARK 500 LYS K 77 -123.01 53.80
REMARK 500 GLN K 115 70.48 47.37
REMARK 500 PHE L 12 48.15 -142.48
REMARK 500 GLU L 13 -137.87 58.47
REMARK 500 PHE L 15 -4.32 81.23
REMARK 500 LYS L 77 -124.42 58.50
REMARK 500 PHE M 12 45.98 -140.89
REMARK 500 GLU M 13 -141.72 58.67
REMARK 500 PHE M 15 -7.66 81.29
REMARK 500 LYS M 77 -124.08 54.79
REMARK 500 GLN M 115 72.28 47.61
REMARK 500 PHE N 12 48.42 -143.69
REMARK 500 GLU N 13 -143.13 57.06
REMARK 500 PHE N 15 -4.49 87.07
REMARK 500 LYS N 77 -120.21 56.62
REMARK 500 GLN N 115 73.88 46.45
REMARK 500 PHE O 12 46.66 -143.64
REMARK 500 GLU O 13 -143.34 57.90
REMARK 500 PHE O 15 0.29 83.00
REMARK 500 SER O 62 54.02 -90.95
REMARK 500 LYS O 77 -126.83 52.20
REMARK 500 PHE P 12 49.13 -144.23
REMARK 500 GLU P 13 -144.28 55.88
REMARK 500 PHE P 15 -0.87 81.24
REMARK 500 SER P 62 47.90 -90.48
REMARK 500 LYS P 77 -126.88 56.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
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 A1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201 OQ1
REMARK 620 2 ASP A 203 OD1 97.5
REMARK 620 3 GLU A 204 OE1 91.3 90.4
REMARK 620 4 CAP A1477 O3 84.8 173.6 83.5
REMARK 620 5 CAP A1477 O2 96.1 110.9 156.2 74.6
REMARK 620 6 CAP A1477 O7 165.7 95.4 94.7 83.0 73.5
REMARK 620 7 CAP A1477 C2 112.5 129.0 127.1 54.6 29.8 53.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 204 OE1
REMARK 620 2 KCX B 201 OQ1 89.1
REMARK 620 3 ASP B 203 OD1 86.4 96.5
REMARK 620 4 CAP B1477 O3 86.3 86.1 172.2
REMARK 620 5 CAP B1477 C2 130.8 113.9 129.4 55.0
REMARK 620 6 CAP B1477 O2 158.9 95.0 113.5 73.4 29.9
REMARK 620 7 CAP B1477 C 112.7 144.8 111.5 69.0 31.1 54.9
REMARK 620 8 CAP B1477 O7 95.8 168.3 94.4 83.6 55.2 76.6 24.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 201 OQ1
REMARK 620 2 ASP C 203 OD1 96.9
REMARK 620 3 CAP C1477 O3 82.1 178.9
REMARK 620 4 CAP C1477 O2 91.3 107.9 72.1
REMARK 620 5 CAP C1477 O7 162.1 95.5 85.5 72.6
REMARK 620 6 GLU C 204 OE1 92.7 95.0 85.2 156.1 99.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 203 OD1
REMARK 620 2 CAP D1477 O2 112.2
REMARK 620 3 CAP D1477 O7 98.8 73.8
REMARK 620 4 KCX D 201 OQ1 93.6 95.7 166.1
REMARK 620 5 GLU D 204 OE1 91.7 154.9 95.7 90.1
REMARK 620 6 CAP D1477 O3 174.1 73.4 80.6 87.7 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E1477 C2
REMARK 620 2 CAP E1477 O7 54.1
REMARK 620 3 GLU E 204 OE1 123.6 90.4
REMARK 620 4 KCX E 201 OQ1 113.8 165.6 91.5
REMARK 620 5 CAP E1477 O3 54.5 83.1 82.1 83.0
REMARK 620 6 CAP E1477 O2 29.8 73.8 153.0 98.7 74.4
REMARK 620 7 ASP E 203 OD1 131.7 94.9 87.7 99.4 169.6 114.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP F1477 O3
REMARK 620 2 CAP F1477 O2 72.9
REMARK 620 3 CAP F1477 O7 79.9 70.7
REMARK 620 4 KCX F 201 OQ1 81.4 96.6 159.8
REMARK 620 5 ASP F 203 OD1 177.6 109.3 99.7 99.3
REMARK 620 6 GLU F 204 OE1 80.4 149.5 90.7 93.6 97.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 203 OD1
REMARK 620 2 CAP G1477 O2 107.4
REMARK 620 3 CAP G1477 O7 94.1 70.0
REMARK 620 4 GLU G 204 OE1 91.0 158.8 99.0
REMARK 620 5 CAP G1477 O3 177.2 74.1 84.2 87.1
REMARK 620 6 KCX G 201 OQ1 100.4 94.4 161.4 92.3 81.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H1477 O3
REMARK 620 2 CAP H1477 O2 71.8
REMARK 620 3 CAP H1477 O7 84.3 72.6
REMARK 620 4 KCX H 201 OQ1 82.4 93.5 163.3
REMARK 620 5 ASP H 203 OD1 178.3 109.9 96.0 97.6
REMARK 620 6 GLU H 204 OE1 85.0 155.8 98.9 90.1 93.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V67 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900 RUBISCO WITH A LARGE-SUBUNIT SUPRESSOR
REMARK 900 MUTATION T342I
REMARK 900 RELATED ID: 2V63 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RUBISCO FROM
REMARK 900 CHLAMYDOMONAS REINHARDTII WITH A LARGE-SUBUNIT
REMARK 900 V331A MUTATION
REMARK 900 RELATED ID: 2V68 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900 RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,
REMARK 900 T342I
REMARK 900 RELATED ID: 1IR2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5
REMARK 900 -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM
REMARK 900 GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED
REMARK 900 WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (
REMARK 900 2-CABP)
REMARK 900 RELATED ID: 1UZH RELATED DB: PDB
REMARK 900 A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO
REMARK 900 ENZYME
REMARK 900 RELATED ID: 2V69 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900 RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E
REMARK 900 RELATED ID: 1UW9 RELATED DB: PDB
REMARK 900 L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
REMARK 900 RELATED ID: 1UZD RELATED DB: PDB
REMARK 900 CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
REMARK 900 RELATED ID: 2VDH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900 RUBISCO WITH A LARGE-SUBUNIT C172S MUTATION
REMARK 900 RELATED ID: 1UWA RELATED DB: PDB
REMARK 900 L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
REMARK 900 RELATED ID: 2V6A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900 RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,
REMARK 900 G344S
REMARK 900 RELATED ID: 1GK8 RELATED DB: PDB
REMARK 900 RUBISCO FROM CHLAMYDOMONAS REINHARDTII
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE UNP P00877 HAS A VARIANT (PRO46LEU)
REMARK 999 WHICH OCCURS IN STRAIN 137C
REMARK 999 LARGE CHAIN RESIDUE 46 DIFFERS FROM UNP P00877
REMARK 999 AND IS IDENTIFIED AS PRO FROM THE ELECTRON
REMARK 999 DENSITY.
DBREF 2VDI A 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI B 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI C 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI D 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI E 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI F 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI G 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI H 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2VDI I 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI J 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI K 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI L 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI M 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI N 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI O 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2VDI P 1 140 UNP P00873 RBS1_CHLRE 46 185
SEQADV 2VDI PRO A 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER A 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO B 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER B 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO C 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER C 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO D 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER D 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO E 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER E 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO F 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER F 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO G 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER G 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQADV 2VDI PRO H 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2VDI SER H 192 UNP P00877 CYS 192 ENGINEERED MUTATION
SEQRES 1 A 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 A 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 A 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 A 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 A 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 A 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 A 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 A 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 A 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 A 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 A 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 A 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 A 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 A 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 A 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 A 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 A 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 A 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 A 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 A 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 A 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 A 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 A 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 A 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 A 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 A 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 A 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 A 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 A 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 A 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 A 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 A 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 A 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 A 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 A 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 A 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 A 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 B 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 B 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 B 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 B 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 B 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 B 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 B 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 B 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 B 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 B 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 B 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 B 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 B 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 B 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 B 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 B 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 B 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 B 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 B 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 B 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 B 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 B 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 B 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 B 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 B 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 B 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 B 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 B 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 B 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 B 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 B 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 B 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 B 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 B 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 B 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 B 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 B 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 C 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 C 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 C 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 C 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 C 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 C 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 C 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 C 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 C 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 C 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 C 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 C 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 C 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 C 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 C 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 C 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 C 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 C 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 C 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 C 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 C 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 C 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 C 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 C 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 C 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 C 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 C 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 C 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 C 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 C 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 C 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 C 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 C 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 C 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 C 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 C 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 C 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 D 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 D 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 D 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 D 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 D 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 D 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 D 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 D 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 D 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 D 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 D 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 D 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 D 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 D 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 D 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 D 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 D 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 D 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 D 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 D 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 D 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 D 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 D 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 D 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 D 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 D 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 D 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 D 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 D 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 D 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 D 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 D 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 D 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 D 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 D 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 D 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 D 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 E 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 E 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 E 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 E 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 E 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 E 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 E 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 E 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 E 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 E 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 E 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 E 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 E 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 E 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 E 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 E 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 E 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 E 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 E 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 E 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 E 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 E 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 E 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 E 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 E 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 E 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 E 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 E 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 E 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 E 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 E 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 E 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 E 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 E 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 E 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 E 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 E 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 F 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 F 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 F 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 F 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 F 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 F 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 F 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 F 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 F 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 F 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 F 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 F 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 F 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 F 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 F 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 F 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 F 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 F 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 F 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 F 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 F 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 F 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 F 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 F 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 F 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 F 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 F 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 F 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 F 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 F 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 F 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 F 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 F 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 F 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 F 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 F 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 F 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 G 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 G 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 G 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 G 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 G 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 G 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 G 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 G 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 G 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 G 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 G 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 G 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 G 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 G 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 G 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 G 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 G 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 G 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 G 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 G 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 G 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 G 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 G 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 G 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 G 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 G 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 G 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 G 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 G 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 G 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 G 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 G 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 G 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 G 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 G 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 G 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 G 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 H 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 H 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 H 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 H 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 H 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 H 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 H 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 H 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 H 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 H 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 H 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 H 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 H 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 H 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 H 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU SER LEU ARG GLY
SEQRES 16 H 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 H 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 H 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 H 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 H 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 H 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 H 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 H 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 H 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 H 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 H 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 H 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 H 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 H 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 H 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 H 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 H 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 H 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 H 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 H 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 H 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 H 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 I 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 I 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 I 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 I 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 I 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 I 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 I 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 I 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 I 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 I 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 I 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 J 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 J 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 J 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 J 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 J 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 J 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 J 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 J 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 J 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 J 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 J 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 K 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 K 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 K 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 K 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 K 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 K 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 K 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 K 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 K 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 K 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 K 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 L 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 L 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 L 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 L 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 L 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 L 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 L 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 L 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 L 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 L 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 L 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 M 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 M 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 M 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 M 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 M 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 M 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 M 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 M 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 M 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 M 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 M 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 N 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 N 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 N 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 N 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 N 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 N 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 N 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 N 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 N 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 N 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 N 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 O 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 O 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 O 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 O 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 O 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 O 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 O 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 O 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 O 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 O 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 O 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 P 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 P 140 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 P 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 P 140 PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES 5 P 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 P 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 P 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 P 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 P 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 P 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES 11 P 140 ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
MODRES 2VDI HYP G 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC C 256 CYS S-METHYLCYSTEINE
MODRES 2VDI SMC D 256 CYS S-METHYLCYSTEINE
MODRES 2VDI MME P 1 MET N-METHYL METHIONINE
MODRES 2VDI HYP B 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI HYP H 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC G 256 CYS S-METHYLCYSTEINE
MODRES 2VDI HYP E 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC A 256 CYS S-METHYLCYSTEINE
MODRES 2VDI SMC E 256 CYS S-METHYLCYSTEINE
MODRES 2VDI MME M 1 MET N-METHYL METHIONINE
MODRES 2VDI HYP H 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI MME N 1 MET N-METHYL METHIONINE
MODRES 2VDI SMC E 369 CYS S-METHYLCYSTEINE
MODRES 2VDI HYP A 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC B 256 CYS S-METHYLCYSTEINE
MODRES 2VDI KCX D 201 LYS LYSYL-CARBAMATE
MODRES 2VDI MME L 1 MET N-METHYL METHIONINE
MODRES 2VDI KCX E 201 LYS LYSYL-CARBAMATE
MODRES 2VDI HYP C 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI HYP D 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC C 369 CYS S-METHYLCYSTEINE
MODRES 2VDI KCX F 201 LYS LYSYL-CARBAMATE
MODRES 2VDI SMC A 369 CYS S-METHYLCYSTEINE
MODRES 2VDI MME J 1 MET N-METHYL METHIONINE
MODRES 2VDI SMC H 369 CYS S-METHYLCYSTEINE
MODRES 2VDI KCX A 201 LYS LYSYL-CARBAMATE
MODRES 2VDI MME I 1 MET N-METHYL METHIONINE
MODRES 2VDI KCX H 201 LYS LYSYL-CARBAMATE
MODRES 2VDI KCX B 201 LYS LYSYL-CARBAMATE
MODRES 2VDI HYP E 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC B 369 CYS S-METHYLCYSTEINE
MODRES 2VDI HYP G 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI HYP A 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC H 256 CYS S-METHYLCYSTEINE
MODRES 2VDI HYP B 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI HYP C 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC D 369 CYS S-METHYLCYSTEINE
MODRES 2VDI HYP D 151 PRO 4-HYDROXYPROLINE
MODRES 2VDI KCX C 201 LYS LYSYL-CARBAMATE
MODRES 2VDI HYP F 104 PRO 4-HYDROXYPROLINE
MODRES 2VDI SMC F 369 CYS S-METHYLCYSTEINE
MODRES 2VDI SMC G 369 CYS S-METHYLCYSTEINE
MODRES 2VDI MME K 1 MET N-METHYL METHIONINE
MODRES 2VDI SMC F 256 CYS S-METHYLCYSTEINE
MODRES 2VDI MME O 1 MET N-METHYL METHIONINE
MODRES 2VDI KCX G 201 LYS LYSYL-CARBAMATE
MODRES 2VDI HYP F 151 PRO 4-HYDROXYPROLINE
HET HYP A 104 8
HET HYP A 151 8
HET KCX A 201 12
HET SMC A 256 7
HET SMC A 369 7
HET MG A1476 1
HET CAP A1477 21
HET HYP B 104 8
HET HYP B 151 8
HET KCX B 201 12
HET SMC B 256 7
HET SMC B 369 7
HET MG B1476 1
HET CAP B1477 21
HET HYP C 104 8
HET HYP C 151 8
HET KCX C 201 12
HET SMC C 256 7
HET SMC C 369 7
HET MG C1476 1
HET CAP C1477 21
HET HYP D 104 8
HET HYP D 151 8
HET KCX D 201 12
HET SMC D 256 7
HET SMC D 369 7
HET MG D1476 1
HET CAP D1477 21
HET HYP E 104 8
HET HYP E 151 8
HET KCX E 201 12
HET SMC E 256 7
HET SMC E 369 7
HET MG E1476 1
HET CAP E1477 21
HET HYP F 104 8
HET HYP F 151 8
HET KCX F 201 12
HET SMC F 256 7
HET SMC F 369 7
HET MG F1476 1
HET CAP F1477 21
HET HYP G 104 8
HET HYP G 151 8
HET KCX G 201 12
HET SMC G 256 7
HET SMC G 369 7
HET MG G1476 1
HET CAP G1477 21
HET HYP H 104 8
HET HYP H 151 8
HET KCX H 201 12
HET SMC H 256 7
HET SMC H 369 7
HET MG H1476 1
HET CAP H1477 21
HET MME I 1 9
HET MME J 1 9
HET MME K 1 9
HET MME L 1 9
HET MME M 1 9
HET MME N 1 9
HET MME O 1 9
HET MME P 1 9
HET EDO A1478 4
HET EDO A1479 4
HET EDO A1480 4
HET EDO A1481 4
HET EDO H1478 4
HET EDO H1479 4
HET EDO H1480 4
HET EDO H1481 4
HET EDO H1482 4
HET EDO G1478 4
HET EDO G1479 4
HET EDO G1480 4
HET EDO G1481 4
HET EDO O1141 4
HET EDO O1142 4
HET EDO F1478 4
HET EDO F1479 4
HET EDO F1480 4
HET EDO F1481 4
HET EDO F1482 4
HET EDO F1483 4
HET EDO C1478 4
HET EDO C1479 4
HET EDO K1141 4
HET EDO B1478 4
HET EDO B1479 4
HET EDO B1480 4
HET EDO B1481 4
HET EDO J1141 4
HET EDO C1480 4
HET EDO G1482 4
HET EDO A1482 4
HET EDO D1478 4
HET EDO D1479 4
HET EDO D1480 4
HET EDO E1478 4
HET EDO E1479 4
HET EDO E1480 4
HET EDO E1481 4
HET EDO E1482 4
HET EDO N1141 4
HET EDO L1141 4
HET EDO J1142 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM MME N-METHYL METHIONINE
HETNAM SMC S-METHYLCYSTEINE
HETNAM HYP 4-HYDROXYPROLINE
HETNAM MG MAGNESIUM ION
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
FORMUL 17 EDO 43(C2 H6 O2)
FORMUL 18 CAP 8(C6 H14 O13 P2)
FORMUL 19 MME 8(C6 H13 N O2 S)
FORMUL 20 SMC 16(C4 H9 N O2 S)
FORMUL 21 HYP 16(C5 H9 N O3)
FORMUL 22 MG 8(MG 2+)
FORMUL 23 KCX 8(C7 H14 N2 O4)
FORMUL 24 HOH *1538(H2 O1)
HELIX 1 1 TYR A 20 TYR A 25 1 6
HELIX 2 2 PRO A 49 SER A 61 1 13
HELIX 3 3 VAL A 69 THR A 75 5 7
HELIX 4 4 SER A 76 LYS A 81 1 6
HELIX 5 5 HYP A 104 PHE A 108 5 5
HELIX 6 6 SER A 112 VAL A 121 1 10
HELIX 7 7 ASN A 123 GLY A 126 5 4
HELIX 8 8 PRO A 141 LYS A 146 1 6
HELIX 9 9 HIS A 153 ASN A 163 1 11
HELIX 10 10 SER A 181 ARG A 194 1 14
HELIX 11 11 ARG A 213 GLY A 233 1 21
HELIX 12 12 THR A 246 GLY A 261 1 16
HELIX 13 13 TYR A 269 GLY A 288 1 20
HELIX 14 14 MET A 297 ARG A 303 1 7
HELIX 15 15 HIS A 310 GLY A 322 1 13
HELIX 16 16 GLU A 338 ASP A 351 1 14
HELIX 17 17 ARG A 358 GLY A 361 5 4
HELIX 18 18 HIS A 383 TRP A 385 5 3
HELIX 19 19 HIS A 386 GLY A 395 1 10
HELIX 20 20 GLY A 403 GLY A 408 1 6
HELIX 21 21 GLY A 412 GLU A 433 1 22
HELIX 22 22 ASP A 436 LYS A 450 1 15
HELIX 23 23 SER A 452 LYS A 463 1 12
HELIX 24 24 TYR B 20 TYR B 25 1 6
HELIX 25 25 PRO B 49 SER B 61 1 13
HELIX 26 26 VAL B 69 THR B 75 5 7
HELIX 27 27 SER B 76 LYS B 81 1 6
HELIX 28 28 HYP B 104 PHE B 108 5 5
HELIX 29 29 SER B 112 VAL B 121 1 10
HELIX 30 30 ASN B 123 GLY B 126 5 4
HELIX 31 31 PRO B 141 LYS B 146 1 6
HELIX 32 32 HIS B 153 ASN B 163 1 11
HELIX 33 33 SER B 181 GLY B 195 1 15
HELIX 34 34 ARG B 213 GLY B 233 1 21
HELIX 35 35 THR B 246 LEU B 260 1 15
HELIX 36 36 TYR B 269 GLY B 288 1 20
HELIX 37 37 MET B 297 ARG B 303 1 7
HELIX 38 38 HIS B 310 GLY B 322 1 13
HELIX 39 39 GLU B 338 ASP B 351 1 14
HELIX 40 40 ARG B 358 GLY B 361 5 4
HELIX 41 41 HIS B 383 TRP B 385 5 3
HELIX 42 42 HIS B 386 GLY B 395 1 10
HELIX 43 43 GLY B 403 GLY B 408 1 6
HELIX 44 44 GLY B 412 GLU B 433 1 22
HELIX 45 45 ASP B 436 LYS B 450 1 15
HELIX 46 46 SER B 452 LYS B 463 1 12
HELIX 47 47 TYR C 20 TYR C 25 1 6
HELIX 48 48 PRO C 49 GLU C 60 1 12
HELIX 49 49 VAL C 69 THR C 75 5 7
HELIX 50 50 SER C 76 LYS C 81 1 6
HELIX 51 51 HYP C 104 PHE C 108 5 5
HELIX 52 52 SER C 112 VAL C 121 1 10
HELIX 53 53 ASN C 123 GLY C 126 5 4
HELIX 54 54 PRO C 141 LYS C 146 1 6
HELIX 55 55 HIS C 153 ASN C 163 1 11
HELIX 56 56 SER C 181 ARG C 194 1 14
HELIX 57 57 ARG C 213 GLY C 233 1 21
HELIX 58 58 THR C 246 LEU C 260 1 15
HELIX 59 59 TYR C 269 GLY C 288 1 20
HELIX 60 60 MET C 297 ARG C 303 1 7
HELIX 61 61 HIS C 310 GLY C 322 1 13
HELIX 62 62 GLU C 338 ASP C 351 1 14
HELIX 63 63 ARG C 358 GLY C 361 5 4
HELIX 64 64 HIS C 383 TRP C 385 5 3
HELIX 65 65 HIS C 386 GLY C 395 1 10
HELIX 66 66 GLY C 403 GLY C 408 1 6
HELIX 67 67 GLY C 412 GLY C 434 1 23
HELIX 68 68 GLU C 440 SER C 452 1 13
HELIX 69 69 SER C 452 LYS C 463 1 12
HELIX 70 70 TYR D 20 TYR D 25 1 6
HELIX 71 71 PRO D 49 SER D 61 1 13
HELIX 72 72 VAL D 69 THR D 75 5 7
HELIX 73 73 SER D 76 LYS D 81 1 6
HELIX 74 74 HYP D 104 PHE D 108 5 5
HELIX 75 75 SER D 112 GLY D 122 1 11
HELIX 76 76 ASN D 123 GLY D 126 5 4
HELIX 77 77 PRO D 141 LYS D 146 1 6
HELIX 78 78 GLY D 154 ASN D 163 1 10
HELIX 79 79 SER D 181 ARG D 194 1 14
HELIX 80 80 ARG D 213 GLY D 233 1 21
HELIX 81 81 THR D 246 GLY D 261 1 16
HELIX 82 82 TYR D 269 GLY D 288 1 20
HELIX 83 83 MET D 297 ARG D 303 1 7
HELIX 84 84 HIS D 310 GLY D 322 1 13
HELIX 85 85 GLU D 338 ASP D 351 1 14
HELIX 86 86 ARG D 358 GLY D 361 5 4
HELIX 87 87 HIS D 383 TRP D 385 5 3
HELIX 88 88 HIS D 386 GLY D 395 1 10
HELIX 89 89 GLY D 403 GLY D 408 1 6
HELIX 90 90 GLY D 412 GLU D 433 1 22
HELIX 91 91 ASP D 436 LYS D 450 1 15
HELIX 92 92 SER D 452 LYS D 463 1 12
HELIX 93 93 TYR E 20 TYR E 25 1 6
HELIX 94 94 PRO E 49 SER E 61 1 13
HELIX 95 95 VAL E 69 THR E 75 5 7
HELIX 96 96 SER E 76 LYS E 81 1 6
HELIX 97 97 HYP E 104 PHE E 108 5 5
HELIX 98 98 SER E 112 GLY E 122 1 11
HELIX 99 99 ASN E 123 GLY E 126 5 4
HELIX 100 100 PRO E 141 LYS E 146 1 6
HELIX 101 101 HIS E 153 ASN E 163 1 11
HELIX 102 102 SER E 181 ARG E 194 1 14
HELIX 103 103 ARG E 213 GLY E 233 1 21
HELIX 104 104 THR E 246 GLY E 261 1 16
HELIX 105 105 TYR E 269 GLY E 288 1 20
HELIX 106 106 MET E 297 ARG E 303 1 7
HELIX 107 107 HIS E 310 GLY E 322 1 13
HELIX 108 108 GLU E 338 ASP E 351 1 14
HELIX 109 109 ARG E 358 GLY E 361 5 4
HELIX 110 110 HIS E 383 TRP E 385 5 3
HELIX 111 111 HIS E 386 GLY E 395 1 10
HELIX 112 112 GLY E 403 GLY E 408 1 6
HELIX 113 113 GLY E 412 GLU E 433 1 22
HELIX 114 114 ASP E 436 LYS E 450 1 15
HELIX 115 115 SER E 452 LYS E 463 1 12
HELIX 116 116 TYR F 20 TYR F 25 1 6
HELIX 117 117 PRO F 49 SER F 61 1 13
HELIX 118 118 VAL F 69 THR F 75 5 7
HELIX 119 119 SER F 76 LYS F 81 1 6
HELIX 120 120 HYP F 104 PHE F 108 5 5
HELIX 121 121 SER F 112 VAL F 121 1 10
HELIX 122 122 ASN F 123 GLY F 126 5 4
HELIX 123 123 PRO F 141 LYS F 146 1 6
HELIX 124 124 HIS F 153 ASN F 163 1 11
HELIX 125 125 SER F 181 ARG F 194 1 14
HELIX 126 126 ARG F 213 GLY F 233 1 21
HELIX 127 127 THR F 246 LEU F 260 1 15
HELIX 128 128 TYR F 269 GLY F 288 1 20
HELIX 129 129 MET F 297 ARG F 303 1 7
HELIX 130 130 HIS F 310 GLY F 322 1 13
HELIX 131 131 GLU F 338 ASP F 351 1 14
HELIX 132 132 ARG F 358 GLY F 361 5 4
HELIX 133 133 HIS F 383 TRP F 385 5 3
HELIX 134 134 HIS F 386 GLY F 395 1 10
HELIX 135 135 GLY F 403 GLY F 408 1 6
HELIX 136 136 GLY F 412 GLU F 433 1 22
HELIX 137 137 ASP F 436 LYS F 450 1 15
HELIX 138 138 SER F 452 TRP F 462 1 11
HELIX 139 139 TYR G 20 TYR G 25 1 6
HELIX 140 140 PRO G 49 SER G 61 1 13
HELIX 141 141 VAL G 69 THR G 75 5 7
HELIX 142 142 SER G 76 LYS G 81 1 6
HELIX 143 143 HYP G 104 PHE G 108 5 5
HELIX 144 144 SER G 112 VAL G 121 1 10
HELIX 145 145 ASN G 123 GLY G 126 5 4
HELIX 146 146 PRO G 141 LYS G 146 1 6
HELIX 147 147 HIS G 153 ASN G 163 1 11
HELIX 148 148 SER G 181 ARG G 194 1 14
HELIX 149 149 ARG G 213 GLY G 233 1 21
HELIX 150 150 THR G 246 LEU G 260 1 15
HELIX 151 151 TYR G 269 GLY G 288 1 20
HELIX 152 152 MET G 297 ARG G 303 1 7
HELIX 153 153 HIS G 310 GLY G 322 1 13
HELIX 154 154 GLU G 338 ASP G 351 1 14
HELIX 155 155 ARG G 358 GLY G 361 5 4
HELIX 156 156 HIS G 383 TRP G 385 5 3
HELIX 157 157 HIS G 386 GLY G 395 1 10
HELIX 158 158 GLY G 403 GLY G 408 1 6
HELIX 159 159 GLY G 412 GLU G 433 1 22
HELIX 160 160 ASP G 436 LYS G 450 1 15
HELIX 161 161 SER G 452 LYS G 463 1 12
HELIX 162 162 TYR H 20 TYR H 25 1 6
HELIX 163 163 PRO H 49 SER H 61 1 13
HELIX 164 164 VAL H 69 THR H 75 5 7
HELIX 165 165 SER H 76 LYS H 81 1 6
HELIX 166 166 HYP H 104 PHE H 108 5 5
HELIX 167 167 SER H 112 GLY H 122 1 11
HELIX 168 168 ASN H 123 GLY H 126 5 4
HELIX 169 169 PRO H 141 LYS H 146 1 6
HELIX 170 170 GLY H 154 ASN H 163 1 10
HELIX 171 171 SER H 181 ARG H 194 1 14
HELIX 172 172 ARG H 213 GLY H 233 1 21
HELIX 173 173 THR H 246 GLY H 261 1 16
HELIX 174 174 TYR H 269 GLY H 288 1 20
HELIX 175 175 MET H 297 ARG H 303 1 7
HELIX 176 176 HIS H 310 GLY H 322 1 13
HELIX 177 177 GLU H 338 ASP H 351 1 14
HELIX 178 178 ARG H 358 GLY H 361 5 4
HELIX 179 179 HIS H 383 TRP H 385 5 3
HELIX 180 180 HIS H 386 GLY H 395 1 10
HELIX 181 181 GLY H 403 GLY H 408 1 6
HELIX 182 182 GLY H 412 GLU H 433 1 22
HELIX 183 183 ASP H 436 LYS H 450 1 15
HELIX 184 184 SER H 452 LYS H 463 1 12
HELIX 185 185 THR I 22 ASN I 36 1 15
HELIX 186 186 GLU I 46 ALA I 50 5 5
HELIX 187 187 ASN I 54 PHE I 60 5 7
HELIX 188 188 ASP I 85 PHE I 100 1 16
HELIX 189 189 PRO I 134 ARG I 138 5 5
HELIX 190 190 THR J 22 ASN J 36 1 15
HELIX 191 191 GLU J 46 ALA J 50 5 5
HELIX 192 192 ASN J 54 PHE J 60 5 7
HELIX 193 193 ASP J 85 PHE J 100 1 16
HELIX 194 194 PRO J 134 ARG J 138 5 5
HELIX 195 195 THR K 22 ASN K 36 1 15
HELIX 196 196 GLU K 46 ALA K 50 5 5
HELIX 197 197 ASN K 54 PHE K 60 5 7
HELIX 198 198 ASP K 85 PHE K 100 1 16
HELIX 199 199 PRO K 134 ARG K 138 5 5
HELIX 200 200 THR L 22 ASN L 36 1 15
HELIX 201 201 GLU L 46 ALA L 50 5 5
HELIX 202 202 ASN L 54 PHE L 60 5 7
HELIX 203 203 ASP L 85 PHE L 100 1 16
HELIX 204 204 PRO L 134 ARG L 138 5 5
HELIX 205 205 THR M 22 ASN M 36 1 15
HELIX 206 206 GLU M 46 ALA M 50 5 5
HELIX 207 207 ASN M 54 PHE M 60 5 7
HELIX 208 208 ASP M 85 PHE M 100 1 16
HELIX 209 209 PRO M 134 ARG M 138 5 5
HELIX 210 210 THR N 22 ASN N 36 1 15
HELIX 211 211 GLU N 46 ALA N 50 5 5
HELIX 212 212 ASN N 54 PHE N 60 5 7
HELIX 213 213 ASP N 85 PHE N 100 1 16
HELIX 214 214 PRO N 134 ARG N 138 5 5
HELIX 215 215 THR O 22 ASN O 36 1 15
HELIX 216 216 GLU O 46 ALA O 50 5 5
HELIX 217 217 ASN O 54 PHE O 60 5 7
HELIX 218 218 ASP O 85 PHE O 100 1 16
HELIX 219 219 PRO O 134 ARG O 138 5 5
HELIX 220 220 THR P 22 ASN P 36 1 15
HELIX 221 221 GLU P 46 ALA P 50 5 5
HELIX 222 222 ASN P 54 PHE P 60 5 7
HELIX 223 223 ASP P 85 PHE P 100 1 16
HELIX 224 224 PRO P 134 ARG P 138 5 5
SHEET 1 AA 5 ARG A 83 PRO A 89 0
SHEET 2 AA 5 TYR A 97 TYR A 103 -1 O ILE A 98 N GLU A 88
SHEET 3 AA 5 ILE A 36 PRO A 44 -1 O ILE A 36 N TYR A 103
SHEET 4 AA 5 LEU A 130 ARG A 139 -1 N ARG A 131 O THR A 43
SHEET 5 AA 5 GLY A 308 ILE A 309 1 O GLY A 308 N LEU A 135
SHEET 1 AB 8 LEU A 169 GLY A 171 0
SHEET 2 AB 8 CYS A 399 GLN A 401 1 O LEU A 400 N GLY A 171
SHEET 3 AB 8 MET A 375 SER A 379 1 O PRO A 376 N CYS A 399
SHEET 4 AB 8 HIS A 325 HIS A 327 1 O LEU A 326 N VAL A 377
SHEET 5 AB 8 LEU A 290 HIS A 294 1 O ILE A 293 N HIS A 327
SHEET 6 AB 8 ILE A 264 ASP A 268 1 O ILE A 265 N HIS A 292
SHEET 7 AB 8 GLY A 237 ASN A 241 1 O LEU A 240 N MET A 266
SHEET 8 AB 8 PHE A 199 KCX A 201 1 O THR A 200 N TYR A 239
SHEET 1 AC 2 TYR A 353 VAL A 354 0
SHEET 2 AC 2 GLN A 366 ASP A 367 -1 O GLN A 366 N VAL A 354
SHEET 1 BA 5 ARG B 83 PRO B 89 0
SHEET 2 BA 5 TYR B 97 TYR B 103 -1 O ILE B 98 N GLU B 88
SHEET 3 BA 5 ILE B 36 PRO B 44 -1 O ILE B 36 N TYR B 103
SHEET 4 BA 5 LEU B 130 ARG B 139 -1 N ARG B 131 O THR B 43
SHEET 5 BA 5 GLY B 308 ILE B 309 1 O GLY B 308 N LEU B 135
SHEET 1 BB 8 LEU B 169 GLY B 171 0
SHEET 2 BB 8 CYS B 399 GLN B 401 1 O LEU B 400 N GLY B 171
SHEET 3 BB 8 MET B 375 SER B 379 1 O PRO B 376 N CYS B 399
SHEET 4 BB 8 HIS B 325 HIS B 327 1 O LEU B 326 N VAL B 377
SHEET 5 BB 8 LEU B 290 HIS B 294 1 O ILE B 293 N HIS B 327
SHEET 6 BB 8 ILE B 264 ASP B 268 1 O ILE B 265 N HIS B 292
SHEET 7 BB 8 GLY B 237 ASN B 241 1 O LEU B 240 N MET B 266
SHEET 8 BB 8 PHE B 199 KCX B 201 1 O THR B 200 N TYR B 239
SHEET 1 BC 2 TYR B 353 VAL B 354 0
SHEET 2 BC 2 GLN B 366 ASP B 367 -1 O GLN B 366 N VAL B 354
SHEET 1 CA 5 ARG C 83 PRO C 89 0
SHEET 2 CA 5 TYR C 97 TYR C 103 -1 O ILE C 98 N GLU C 88
SHEET 3 CA 5 ILE C 36 PRO C 44 -1 O ILE C 36 N TYR C 103
SHEET 4 CA 5 LEU C 130 ARG C 139 -1 N ARG C 131 O THR C 43
SHEET 5 CA 5 GLY C 308 ILE C 309 1 O GLY C 308 N LEU C 135
SHEET 1 CB 8 LEU C 169 GLY C 171 0
SHEET 2 CB 8 CYS C 399 GLN C 401 1 O LEU C 400 N GLY C 171
SHEET 3 CB 8 MET C 375 SER C 379 1 O PRO C 376 N CYS C 399
SHEET 4 CB 8 HIS C 325 HIS C 327 1 O LEU C 326 N VAL C 377
SHEET 5 CB 8 LEU C 290 HIS C 294 1 O ILE C 293 N HIS C 327
SHEET 6 CB 8 ILE C 264 ASP C 268 1 O ILE C 265 N HIS C 292
SHEET 7 CB 8 GLY C 237 ASN C 241 1 O LEU C 240 N MET C 266
SHEET 8 CB 8 PHE C 199 KCX C 201 1 O THR C 200 N TYR C 239
SHEET 1 CC 2 TYR C 353 VAL C 354 0
SHEET 2 CC 2 GLN C 366 ASP C 367 -1 O GLN C 366 N VAL C 354
SHEET 1 DA 5 ARG D 83 PRO D 89 0
SHEET 2 DA 5 TYR D 97 TYR D 103 -1 O ILE D 98 N GLU D 88
SHEET 3 DA 5 ILE D 36 PRO D 44 -1 O ILE D 36 N TYR D 103
SHEET 4 DA 5 LEU D 130 ARG D 139 -1 N ARG D 131 O THR D 43
SHEET 5 DA 5 GLY D 308 ILE D 309 1 O GLY D 308 N LEU D 135
SHEET 1 DB 8 LEU D 169 GLY D 171 0
SHEET 2 DB 8 CYS D 399 GLN D 401 1 O LEU D 400 N GLY D 171
SHEET 3 DB 8 MET D 375 SER D 379 1 O PRO D 376 N CYS D 399
SHEET 4 DB 8 HIS D 325 HIS D 327 1 O LEU D 326 N VAL D 377
SHEET 5 DB 8 LEU D 290 HIS D 294 1 O ILE D 293 N HIS D 327
SHEET 6 DB 8 ILE D 264 ASP D 268 1 O ILE D 265 N HIS D 292
SHEET 7 DB 8 GLY D 237 ASN D 241 1 O LEU D 240 N MET D 266
SHEET 8 DB 8 PHE D 199 KCX D 201 1 O THR D 200 N TYR D 239
SHEET 1 DC 2 TYR D 353 VAL D 354 0
SHEET 2 DC 2 GLN D 366 ASP D 367 -1 O GLN D 366 N VAL D 354
SHEET 1 EA 5 ARG E 83 PRO E 89 0
SHEET 2 EA 5 TYR E 97 TYR E 103 -1 O ILE E 98 N GLU E 88
SHEET 3 EA 5 ILE E 36 PRO E 44 -1 O ILE E 36 N TYR E 103
SHEET 4 EA 5 LEU E 130 ARG E 139 -1 N ARG E 131 O THR E 43
SHEET 5 EA 5 GLY E 308 ILE E 309 1 O GLY E 308 N LEU E 135
SHEET 1 EB 8 LEU E 169 GLY E 171 0
SHEET 2 EB 8 CYS E 399 GLN E 401 1 O LEU E 400 N GLY E 171
SHEET 3 EB 8 MET E 375 SER E 379 1 O PRO E 376 N CYS E 399
SHEET 4 EB 8 HIS E 325 HIS E 327 1 O LEU E 326 N VAL E 377
SHEET 5 EB 8 LEU E 290 HIS E 294 1 O ILE E 293 N HIS E 327
SHEET 6 EB 8 ILE E 264 ASP E 268 1 O ILE E 265 N HIS E 292
SHEET 7 EB 8 GLY E 237 ASN E 241 1 O LEU E 240 N MET E 266
SHEET 8 EB 8 PHE E 199 KCX E 201 1 O THR E 200 N TYR E 239
SHEET 1 EC 2 TYR E 353 VAL E 354 0
SHEET 2 EC 2 GLN E 366 ASP E 367 -1 O GLN E 366 N VAL E 354
SHEET 1 FA 5 ARG F 83 PRO F 89 0
SHEET 2 FA 5 TYR F 97 TYR F 103 -1 O ILE F 98 N GLU F 88
SHEET 3 FA 5 ILE F 36 PRO F 44 -1 O ILE F 36 N TYR F 103
SHEET 4 FA 5 LEU F 130 ARG F 139 -1 N ARG F 131 O THR F 43
SHEET 5 FA 5 GLY F 308 ILE F 309 1 O GLY F 308 N LEU F 135
SHEET 1 FB 8 LEU F 169 GLY F 171 0
SHEET 2 FB 8 CYS F 399 GLN F 401 1 O LEU F 400 N GLY F 171
SHEET 3 FB 8 MET F 375 SER F 379 1 O PRO F 376 N CYS F 399
SHEET 4 FB 8 HIS F 325 HIS F 327 1 O LEU F 326 N VAL F 377
SHEET 5 FB 8 LEU F 290 HIS F 294 1 O ILE F 293 N HIS F 327
SHEET 6 FB 8 ILE F 264 ASP F 268 1 O ILE F 265 N HIS F 292
SHEET 7 FB 8 GLY F 237 ASN F 241 1 O LEU F 240 N MET F 266
SHEET 8 FB 8 PHE F 199 KCX F 201 1 O THR F 200 N TYR F 239
SHEET 1 FC 2 TYR F 353 VAL F 354 0
SHEET 2 FC 2 GLN F 366 ASP F 367 -1 O GLN F 366 N VAL F 354
SHEET 1 GA 5 ARG G 83 PRO G 89 0
SHEET 2 GA 5 TYR G 97 TYR G 103 -1 O ILE G 98 N GLU G 88
SHEET 3 GA 5 ILE G 36 PRO G 44 -1 O ILE G 36 N TYR G 103
SHEET 4 GA 5 LEU G 130 ARG G 139 -1 N ARG G 131 O THR G 43
SHEET 5 GA 5 GLY G 308 ILE G 309 1 O GLY G 308 N LEU G 135
SHEET 1 GB 8 LEU G 169 GLY G 171 0
SHEET 2 GB 8 CYS G 399 GLN G 401 1 O LEU G 400 N GLY G 171
SHEET 3 GB 8 MET G 375 SER G 379 1 O PRO G 376 N CYS G 399
SHEET 4 GB 8 HIS G 325 HIS G 327 1 O LEU G 326 N VAL G 377
SHEET 5 GB 8 LEU G 290 HIS G 294 1 O ILE G 293 N HIS G 327
SHEET 6 GB 8 ILE G 264 ASP G 268 1 O ILE G 265 N HIS G 292
SHEET 7 GB 8 GLY G 237 ASN G 241 1 O LEU G 240 N MET G 266
SHEET 8 GB 8 PHE G 199 KCX G 201 1 O THR G 200 N TYR G 239
SHEET 1 GC 2 TYR G 353 VAL G 354 0
SHEET 2 GC 2 GLN G 366 ASP G 367 -1 O GLN G 366 N VAL G 354
SHEET 1 HA 5 ARG H 83 PRO H 89 0
SHEET 2 HA 5 TYR H 97 TYR H 103 -1 O ILE H 98 N GLU H 88
SHEET 3 HA 5 ILE H 36 PRO H 44 -1 O ILE H 36 N TYR H 103
SHEET 4 HA 5 LEU H 130 ARG H 139 -1 N ARG H 131 O THR H 43
SHEET 5 HA 5 GLY H 308 ILE H 309 1 O GLY H 308 N LEU H 135
SHEET 1 HB 8 LEU H 169 GLY H 171 0
SHEET 2 HB 8 CYS H 399 GLN H 401 1 O LEU H 400 N GLY H 171
SHEET 3 HB 8 MET H 375 SER H 379 1 O PRO H 376 N CYS H 399
SHEET 4 HB 8 HIS H 325 HIS H 327 1 O LEU H 326 N VAL H 377
SHEET 5 HB 8 LEU H 290 HIS H 294 1 O ILE H 293 N HIS H 327
SHEET 6 HB 8 ILE H 264 ASP H 268 1 O ILE H 265 N HIS H 292
SHEET 7 HB 8 GLY H 237 ASN H 241 1 O LEU H 240 N MET H 266
SHEET 8 HB 8 PHE H 199 KCX H 201 1 O THR H 200 N TYR H 239
SHEET 1 HC 2 TYR H 353 VAL H 354 0
SHEET 2 HC 2 GLN H 366 ASP H 367 -1 O GLN H 366 N VAL H 354
SHEET 1 IA 4 THR I 74 TRP I 76 0
SHEET 2 IA 4 ILE I 39 ALA I 45 -1 O LEU I 42 N TRP I 76
SHEET 3 IA 4 TYR I 104 ASP I 111 -1 O TYR I 104 N ALA I 45
SHEET 4 IA 4 VAL I 116 GLN I 124 -1 O VAL I 116 N ASP I 111
SHEET 1 JA 4 THR J 74 TRP J 76 0
SHEET 2 JA 4 ILE J 39 ALA J 45 -1 O LEU J 42 N TRP J 76
SHEET 3 JA 4 TYR J 104 ASP J 111 -1 O TYR J 104 N ALA J 45
SHEET 4 JA 4 VAL J 116 GLN J 124 -1 O VAL J 116 N ASP J 111
SHEET 1 KA 4 THR K 74 TRP K 76 0
SHEET 2 KA 4 ILE K 39 ALA K 45 -1 O LEU K 42 N TRP K 76
SHEET 3 KA 4 TYR K 104 ASP K 111 -1 O TYR K 104 N ALA K 45
SHEET 4 KA 4 VAL K 116 GLN K 124 -1 O VAL K 116 N ASP K 111
SHEET 1 LA 4 THR L 74 TRP L 76 0
SHEET 2 LA 4 ILE L 39 ALA L 45 -1 O LEU L 42 N TRP L 76
SHEET 3 LA 4 TYR L 104 ASP L 111 -1 O TYR L 104 N ALA L 45
SHEET 4 LA 4 VAL L 116 GLN L 124 -1 O VAL L 116 N ASP L 111
SHEET 1 MA 4 THR M 74 TRP M 76 0
SHEET 2 MA 4 ILE M 39 ALA M 45 -1 O LEU M 42 N TRP M 76
SHEET 3 MA 4 TYR M 104 ASP M 111 -1 O TYR M 104 N ALA M 45
SHEET 4 MA 4 VAL M 116 GLN M 124 -1 O VAL M 116 N ASP M 111
SHEET 1 NA 4 THR N 74 TRP N 76 0
SHEET 2 NA 4 ILE N 39 ALA N 45 -1 O LEU N 42 N TRP N 76
SHEET 3 NA 4 TYR N 104 ASP N 111 -1 O TYR N 104 N ALA N 45
SHEET 4 NA 4 VAL N 116 GLN N 124 -1 O VAL N 116 N ASP N 111
SHEET 1 OA 4 THR O 74 TRP O 76 0
SHEET 2 OA 4 ILE O 39 ALA O 45 -1 O LEU O 42 N TRP O 76
SHEET 3 OA 4 TYR O 104 ASP O 111 -1 O TYR O 104 N ALA O 45
SHEET 4 OA 4 VAL O 116 GLN O 124 -1 O VAL O 116 N ASP O 111
SHEET 1 PA 4 THR P 74 TRP P 76 0
SHEET 2 PA 4 ILE P 39 ALA P 45 -1 O LEU P 42 N TRP P 76
SHEET 3 PA 4 TYR P 104 ASP P 111 -1 O TYR P 104 N ALA P 45
SHEET 4 PA 4 VAL P 116 GLN P 124 -1 O VAL P 116 N ASP P 111
SSBOND 1 CYS C 247 CYS D 247 1555 1555 2.08
SSBOND 2 CYS E 247 CYS F 247 1555 1555 2.08
SSBOND 3 CYS G 247 CYS H 247 1555 1555 2.09
LINK C TYR A 103 N HYP A 104 1555 1555 1.34
LINK C HYP A 104 N ILE A 105 1555 1555 1.33
LINK C GLY A 150 N HYP A 151 1555 1555 1.34
LINK C HYP A 151 N PRO A 152 1555 1555 1.35
LINK C THR A 200 N KCX A 201 1555 1555 1.33
LINK C KCX A 201 N ASP A 202 1555 1555 1.33
LINK C VAL A 255 N SMC A 256 1555 1555 1.33
LINK C SMC A 256 N ALA A 257 1555 1555 1.34
LINK C TRP A 368 N SMC A 369 1555 1555 1.33
LINK C SMC A 369 N SER A 370 1555 1555 1.33
LINK MG MG A1476 OQ1 KCX A 201 1555 1555 2.09
LINK MG MG A1476 OD1 ASP A 203 1555 1555 1.90
LINK MG MG A1476 OE1 GLU A 204 1555 1555 2.03
LINK MG MG A1476 O3 CAP A1477 1555 1555 2.25
LINK MG MG A1476 O2 CAP A1477 1555 1555 2.23
LINK MG MG A1476 O7 CAP A1477 1555 1555 2.23
LINK MG MG A1476 C2 CAP A1477 1555 1555 2.88
LINK C TYR B 103 N HYP B 104 1555 1555 1.34
LINK C HYP B 104 N ILE B 105 1555 1555 1.33
LINK C GLY B 150 N HYP B 151 1555 1555 1.34
LINK C HYP B 151 N PRO B 152 1555 1555 1.35
LINK C THR B 200 N KCX B 201 1555 1555 1.33
LINK C KCX B 201 N ASP B 202 1555 1555 1.34
LINK C VAL B 255 N SMC B 256 1555 1555 1.34
LINK C SMC B 256 N ALA B 257 1555 1555 1.33
LINK C TRP B 368 N SMC B 369 1555 1555 1.34
LINK C SMC B 369 N SER B 370 1555 1555 1.33
LINK MG MG B1476 OE1 GLU B 204 1555 1555 2.05
LINK MG MG B1476 OQ1 KCX B 201 1555 1555 2.15
LINK MG MG B1476 OD1 ASP B 203 1555 1555 1.99
LINK MG MG B1476 O3 CAP B1477 1555 1555 2.24
LINK MG MG B1476 C2 CAP B1477 1555 1555 2.87
LINK MG MG B1476 O2 CAP B1477 1555 1555 2.27
LINK MG MG B1476 C CAP B1477 1555 1555 2.90
LINK MG MG B1476 O7 CAP B1477 1555 1555 2.21
LINK C TYR C 103 N HYP C 104 1555 1555 1.34
LINK C HYP C 104 N ILE C 105 1555 1555 1.33
LINK C GLY C 150 N HYP C 151 1555 1555 1.35
LINK C HYP C 151 N PRO C 152 1555 1555 1.35
LINK C THR C 200 N KCX C 201 1555 1555 1.33
LINK C KCX C 201 N ASP C 202 1555 1555 1.33
LINK C VAL C 255 N SMC C 256 1555 1555 1.33
LINK C SMC C 256 N ALA C 257 1555 1555 1.34
LINK C TRP C 368 N SMC C 369 1555 1555 1.33
LINK C SMC C 369 N SER C 370 1555 1555 1.34
LINK MG MG C1476 OQ1 KCX C 201 1555 1555 2.11
LINK MG MG C1476 OD1 ASP C 203 1555 1555 1.85
LINK MG MG C1476 O3 CAP C1477 1555 1555 2.25
LINK MG MG C1476 OE1 GLU C 204 1555 1555 1.99
LINK MG MG C1476 O7 CAP C1477 1555 1555 2.21
LINK MG MG C1476 O2 CAP C1477 1555 1555 2.31
LINK C TYR D 103 N HYP D 104 1555 1555 1.34
LINK C HYP D 104 N ILE D 105 1555 1555 1.33
LINK C GLY D 150 N HYP D 151 1555 1555 1.35
LINK C HYP D 151 N PRO D 152 1555 1555 1.35
LINK C THR D 200 N KCX D 201 1555 1555 1.33
LINK C KCX D 201 N ASP D 202 1555 1555 1.33
LINK C VAL D 255 N SMC D 256 1555 1555 1.33
LINK C SMC D 256 N ALA D 257 1555 1555 1.33
LINK C TRP D 368 N SMC D 369 1555 1555 1.33
LINK C SMC D 369 N SER D 370 1555 1555 1.34
LINK MG MG D1476 O7 CAP D1477 1555 1555 2.17
LINK MG MG D1476 O2 CAP D1477 1555 1555 2.29
LINK MG MG D1476 OD1 ASP D 203 1555 1555 1.85
LINK MG MG D1476 O3 CAP D1477 1555 1555 2.24
LINK MG MG D1476 OE1 GLU D 204 1555 1555 2.07
LINK MG MG D1476 OQ1 KCX D 201 1555 1555 2.07
LINK C TYR E 103 N HYP E 104 1555 1555 1.35
LINK C HYP E 104 N ILE E 105 1555 1555 1.34
LINK C GLY E 150 N HYP E 151 1555 1555 1.34
LINK C HYP E 151 N PRO E 152 1555 1555 1.35
LINK C THR E 200 N KCX E 201 1555 1555 1.33
LINK C KCX E 201 N ASP E 202 1555 1555 1.33
LINK C VAL E 255 N SMC E 256 1555 1555 1.33
LINK C SMC E 256 N ALA E 257 1555 1555 1.33
LINK C TRP E 368 N SMC E 369 1555 1555 1.34
LINK C SMC E 369 N SER E 370 1555 1555 1.33
LINK MG MG E1476 OD1 ASP E 203 1555 1555 1.88
LINK MG MG E1476 O2 CAP E1477 1555 1555 2.23
LINK MG MG E1476 O3 CAP E1477 1555 1555 2.31
LINK MG MG E1476 OQ1 KCX E 201 1555 1555 2.09
LINK MG MG E1476 C2 CAP E1477 1555 1555 2.88
LINK MG MG E1476 OE1 GLU E 204 1555 1555 2.12
LINK MG MG E1476 O7 CAP E1477 1555 1555 2.31
LINK C TYR F 103 N HYP F 104 1555 1555 1.34
LINK C HYP F 104 N ILE F 105 1555 1555 1.33
LINK C GLY F 150 N HYP F 151 1555 1555 1.34
LINK C HYP F 151 N PRO F 152 1555 1555 1.36
LINK C THR F 200 N KCX F 201 1555 1555 1.33
LINK C KCX F 201 N ASP F 202 1555 1555 1.33
LINK C VAL F 255 N SMC F 256 1555 1555 1.33
LINK C SMC F 256 N ALA F 257 1555 1555 1.33
LINK C TRP F 368 N SMC F 369 1555 1555 1.34
LINK C SMC F 369 N SER F 370 1555 1555 1.34
LINK MG MG F1476 O7 CAP F1477 1555 1555 2.28
LINK MG MG F1476 O2 CAP F1477 1555 1555 2.30
LINK MG MG F1476 O3 CAP F1477 1555 1555 2.29
LINK MG MG F1476 OD1 ASP F 203 1555 1555 1.82
LINK MG MG F1476 OE1 GLU F 204 1555 1555 2.04
LINK MG MG F1476 OQ1 KCX F 201 1555 1555 2.06
LINK C TYR G 103 N HYP G 104 1555 1555 1.34
LINK C HYP G 104 N ILE G 105 1555 1555 1.33
LINK C GLY G 150 N HYP G 151 1555 1555 1.34
LINK C HYP G 151 N PRO G 152 1555 1555 1.34
LINK C THR G 200 N KCX G 201 1555 1555 1.33
LINK C KCX G 201 N ASP G 202 1555 1555 1.33
LINK C VAL G 255 N SMC G 256 1555 1555 1.33
LINK C SMC G 256 N ALA G 257 1555 1555 1.34
LINK C TRP G 368 N SMC G 369 1555 1555 1.34
LINK C SMC G 369 N SER G 370 1555 1555 1.34
LINK MG MG G1476 OQ1 KCX G 201 1555 1555 2.09
LINK MG MG G1476 OD1 ASP G 203 1555 1555 1.89
LINK MG MG G1476 O2 CAP G1477 1555 1555 2.27
LINK MG MG G1476 O7 CAP G1477 1555 1555 2.29
LINK MG MG G1476 OE1 GLU G 204 1555 1555 1.93
LINK MG MG G1476 O3 CAP G1477 1555 1555 2.19
LINK C TYR H 103 N HYP H 104 1555 1555 1.34
LINK C HYP H 104 N ILE H 105 1555 1555 1.33
LINK C GLY H 150 N HYP H 151 1555 1555 1.35
LINK C HYP H 151 N PRO H 152 1555 1555 1.35
LINK C THR H 200 N KCX H 201 1555 1555 1.32
LINK C KCX H 201 N ASP H 202 1555 1555 1.33
LINK C VAL H 255 N SMC H 256 1555 1555 1.32
LINK C SMC H 256 N ALA H 257 1555 1555 1.33
LINK C TRP H 368 N SMC H 369 1555 1555 1.34
LINK C SMC H 369 N SER H 370 1555 1555 1.33
LINK MG MG H1476 OE1 GLU H 204 1555 1555 1.96
LINK MG MG H1476 OD1 ASP H 203 1555 1555 1.86
LINK MG MG H1476 OQ1 KCX H 201 1555 1555 2.20
LINK MG MG H1476 O7 CAP H1477 1555 1555 2.29
LINK MG MG H1476 O2 CAP H1477 1555 1555 2.27
LINK MG MG H1476 O3 CAP H1477 1555 1555 2.28
LINK C MME I 1 N MET I 2 1555 1555 1.33
LINK C MME J 1 N MET J 2 1555 1555 1.32
LINK C MME K 1 N MET K 2 1555 1555 1.33
LINK C MME L 1 N MET L 2 1555 1555 1.33
LINK C MME M 1 N MET M 2 1555 1555 1.33
LINK C MME N 1 N MET N 2 1555 1555 1.33
LINK C MME O 1 N MET O 2 1555 1555 1.32
LINK C MME P 1 N MET P 2 1555 1555 1.33
CISPEP 1 LYS A 175 PRO A 176 0 1.72
CISPEP 2 LYS B 175 PRO B 176 0 -2.68
CISPEP 3 LYS C 175 PRO C 176 0 2.81
CISPEP 4 LYS D 175 PRO D 176 0 -0.60
CISPEP 5 LYS E 175 PRO E 176 0 -0.81
CISPEP 6 LYS F 175 PRO F 176 0 1.42
CISPEP 7 LYS G 175 PRO G 176 0 0.34
CISPEP 8 LYS H 175 PRO H 176 0 3.07
SITE 1 AC1 5 LYS A 177 KCX A 201 ASP A 203 GLU A 204
SITE 2 AC1 5 CAP A1477
SITE 1 AC2 27 THR A 173 LYS A 175 LYS A 177 KCX A 201
SITE 2 AC2 27 ASP A 203 GLU A 204 HIS A 294 ARG A 295
SITE 3 AC2 27 HIS A 327 LYS A 334 LEU A 335 SER A 379
SITE 4 AC2 27 GLY A 380 GLY A 381 GLY A 403 GLY A 404
SITE 5 AC2 27 MG A1476 HOH A2124 HOH A2133 HOH A2150
SITE 6 AC2 27 HOH A2151 GLU B 60 THR B 65 TRP B 66
SITE 7 AC2 27 ASN B 123 HOH B2017 HOH B2037
SITE 1 AC3 5 LYS B 177 KCX B 201 ASP B 203 GLU B 204
SITE 2 AC3 5 CAP B1477
SITE 1 AC4 28 GLU A 60 THR A 65 TRP A 66 ASN A 123
SITE 2 AC4 28 HOH A2038 THR B 173 LYS B 175 LYS B 177
SITE 3 AC4 28 KCX B 201 ASP B 203 GLU B 204 HIS B 294
SITE 4 AC4 28 ARG B 295 HIS B 327 LYS B 334 LEU B 335
SITE 5 AC4 28 SER B 379 GLY B 380 GLY B 381 GLY B 403
SITE 6 AC4 28 GLY B 404 MG B1476 HOH B2053 HOH B2091
SITE 7 AC4 28 HOH B2124 HOH B2150 HOH B2151 HOH B2152
SITE 1 AC5 5 LYS C 177 KCX C 201 ASP C 203 GLU C 204
SITE 2 AC5 5 CAP C1477
SITE 1 AC6 28 THR C 173 LYS C 175 LYS C 177 KCX C 201
SITE 2 AC6 28 ASP C 203 GLU C 204 HIS C 294 ARG C 295
SITE 3 AC6 28 HIS C 327 LYS C 334 LEU C 335 SER C 379
SITE 4 AC6 28 GLY C 380 GLY C 381 GLY C 403 GLY C 404
SITE 5 AC6 28 MG C1476 HOH C2055 HOH C2118 HOH C2126
SITE 6 AC6 28 HOH C2141 HOH C2142 HOH C2143 HOH C2144
SITE 7 AC6 28 GLU D 60 THR D 65 TRP D 66 ASN D 123
SITE 1 AC7 5 LYS D 177 KCX D 201 ASP D 203 GLU D 204
SITE 2 AC7 5 CAP D1477
SITE 1 AC8 27 GLU C 60 THR C 65 TRP C 66 ASN C 123
SITE 2 AC8 27 THR D 173 LYS D 175 LYS D 177 KCX D 201
SITE 3 AC8 27 ASP D 203 GLU D 204 HIS D 294 ARG D 295
SITE 4 AC8 27 HIS D 327 LYS D 334 LEU D 335 SER D 379
SITE 5 AC8 27 GLY D 380 GLY D 381 GLY D 403 GLY D 404
SITE 6 AC8 27 MG D1476 HOH D2129 HOH D2154 HOH D2155
SITE 7 AC8 27 HOH D2156 HOH D2157 HOH D2158
SITE 1 AC9 5 LYS E 177 KCX E 201 ASP E 203 GLU E 204
SITE 2 AC9 5 CAP E1477
SITE 1 BC1 28 THR E 173 LYS E 175 LYS E 177 KCX E 201
SITE 2 BC1 28 ASP E 203 GLU E 204 HIS E 294 ARG E 295
SITE 3 BC1 28 HIS E 327 LYS E 334 LEU E 335 SER E 379
SITE 4 BC1 28 GLY E 380 GLY E 381 GLY E 403 GLY E 404
SITE 5 BC1 28 MG E1476 HOH E2110 HOH E2138 HOH E2155
SITE 6 BC1 28 HOH E2156 HOH E2157 HOH E2158 GLU F 60
SITE 7 BC1 28 THR F 65 TRP F 66 ASN F 123 HOH F2015
SITE 1 BC2 5 LYS F 177 KCX F 201 ASP F 203 GLU F 204
SITE 2 BC2 5 CAP F1477
SITE 1 BC3 27 GLU E 60 THR E 65 TRP E 66 ASN E 123
SITE 2 BC3 27 HOH E2018 THR F 173 LYS F 175 LYS F 177
SITE 3 BC3 27 KCX F 201 ASP F 203 GLU F 204 HIS F 294
SITE 4 BC3 27 ARG F 295 HIS F 327 LYS F 334 LEU F 335
SITE 5 BC3 27 SER F 379 GLY F 380 GLY F 381 GLY F 403
SITE 6 BC3 27 GLY F 404 MG F1476 HOH F2088 HOH F2090
SITE 7 BC3 27 HOH F2112 HOH F2113 HOH F2115
SITE 1 BC4 5 LYS G 177 KCX G 201 ASP G 203 GLU G 204
SITE 2 BC4 5 CAP G1477
SITE 1 BC5 28 THR G 173 LYS G 175 LYS G 177 KCX G 201
SITE 2 BC5 28 ASP G 203 GLU G 204 HIS G 294 ARG G 295
SITE 3 BC5 28 HIS G 327 LYS G 334 LEU G 335 SER G 379
SITE 4 BC5 28 GLY G 380 GLY G 381 GLY G 403 GLY G 404
SITE 5 BC5 28 MG G1476 HOH G2066 HOH G2107 HOH G2137
SITE 6 BC5 28 HOH G2157 HOH G2158 HOH G2159 HOH G2160
SITE 7 BC5 28 GLU H 60 THR H 65 TRP H 66 ASN H 123
SITE 1 BC6 5 LYS H 177 KCX H 201 ASP H 203 GLU H 204
SITE 2 BC6 5 CAP H1477
SITE 1 BC7 25 GLU G 60 THR G 65 TRP G 66 ASN G 123
SITE 2 BC7 25 HOH G2047 THR H 173 LYS H 175 LYS H 177
SITE 3 BC7 25 KCX H 201 ASP H 203 GLU H 204 HIS H 294
SITE 4 BC7 25 ARG H 295 HIS H 327 LYS H 334 LEU H 335
SITE 5 BC7 25 SER H 379 GLY H 380 GLY H 381 GLY H 403
SITE 6 BC7 25 GLY H 404 MG H1476 HOH H2098 HOH H2145
SITE 7 BC7 25 HOH H2146
SITE 1 BC8 5 TYR A 24 THR A 68 VAL A 69 ASP A 72
SITE 2 BC8 5 EDO A1479
SITE 1 BC9 6 LYS A 18 THR A 65 TRP A 66 THR A 67
SITE 2 BC9 6 THR A 68 EDO A1478
SITE 1 CC1 3 GLU A 52 HOH A2152 PHE B 469
SITE 1 CC2 4 ARG A 295 HIS A 298 ASP A 473 HOH A2153
SITE 1 CC3 8 TYR H 24 THR H 68 VAL H 69 ASP H 72
SITE 2 CC3 8 EDO H1479 HOH H2016 HOH H2147 HOH H2148
SITE 1 CC4 9 LYS H 18 TYR H 20 THR H 65 TRP H 66
SITE 2 CC4 9 THR H 67 THR H 68 EDO H1478 HOH H2005
SITE 3 CC4 9 HOH H2148
SITE 1 CC5 3 PHE G 469 HOH G2162 GLU H 52
SITE 1 CC6 5 LYS H 466 PHE H 467 GLU H 468 PHE H 469
SITE 2 CC6 5 HOH H2149
SITE 1 CC7 4 ARG H 295 PHE H 345 ASP H 473 HOH H2150
SITE 1 CC8 6 TYR G 24 GLY G 64 THR G 68 VAL G 69
SITE 2 CC8 6 ASP G 72 HOH G2161
SITE 1 CC9 8 VAL G 17 LYS G 18 THR G 65 TRP G 66
SITE 2 CC9 8 THR G 67 THR G 68 HOH G2016 HOH G2161
SITE 1 DC1 5 LYS G 466 PHE G 467 GLU G 468 PHE G 469
SITE 2 DC1 5 HOH G2162
SITE 1 DC2 7 ARG G 295 SER G 328 GLY G 329 GLU G 336
SITE 2 DC2 7 GLY G 337 THR G 342 PHE G 345
SITE 1 DC3 6 TYR A 226 LYS A 227 HOH A2071 LYS O 49
SITE 2 DC3 6 GLU O 55 HOH O2022
SITE 1 DC4 5 GLY O 37 ILE O 39 PHE O 81 GLY O 82
SITE 2 DC4 5 CYS O 83
SITE 1 DC5 4 LEU E 270 HOH E2099 LEU F 270 HOH F2132
SITE 1 DC6 10 PRO E 176 THR F 63 GLY F 64 THR F 65
SITE 2 DC6 10 THR F 67 VAL F 69 ASP F 72 HOH F2007
SITE 3 DC6 10 HOH F2018 HOH F2022
SITE 1 DC7 6 VAL F 17 LYS F 18 THR F 65 TRP F 66
SITE 2 DC7 6 THR F 67 THR F 68
SITE 1 DC8 2 PHE E 469 GLU F 52
SITE 1 DC9 4 LYS F 466 PHE F 467 GLU F 468 PHE F 469
SITE 1 EC1 5 ARG F 295 SER F 328 GLU F 336 PHE F 345
SITE 2 EC1 5 HOH F2097
SITE 1 EC2 4 TYR C 24 THR C 68 VAL C 69 ASP C 72
SITE 1 EC3 5 LYS C 18 THR C 65 TRP C 66 THR C 67
SITE 2 EC3 5 THR C 68
SITE 1 EC4 4 GLY K 37 TRP K 38 ILE K 39 GLY K 82
SITE 1 EC5 6 TYR B 24 THR B 68 VAL B 69 ASP B 72
SITE 2 EC5 6 EDO B1479 HOH B2153
SITE 1 EC6 7 LYS B 18 THR B 65 TRP B 66 THR B 67
SITE 2 EC6 7 THR B 68 EDO B1478 HOH B2008
SITE 1 EC7 2 GLU B 52 ALA B 129
SITE 1 EC8 4 HOH A2152 LYS B 466 GLU B 468 PHE B 469
SITE 1 EC9 8 TYR H 226 LYS H 227 ALA H 230 LYS J 49
SITE 2 EC9 8 GLU J 55 ASP J 69 HOH J2019 HOH J2023
SITE 1 FC1 4 LEU C 270 HOH C2145 HOH C2146 LEU D 270
SITE 1 FC2 5 LEU G 270 GLY G 273 PHE G 274 LEU H 270
SITE 2 FC2 5 THR H 271
SITE 1 FC3 6 LEU A 270 GLY A 273 PHE A 274 HOH A2154
SITE 2 FC3 6 LEU B 270 THR B 271
SITE 1 FC4 5 LYS D 18 THR D 65 TRP D 66 THR D 67
SITE 2 FC4 5 THR D 68
SITE 1 FC5 3 PHE C 469 GLU D 52 HOH D2005
SITE 1 FC6 3 LYS D 466 GLU D 468 PHE D 469
SITE 1 FC7 5 TYR E 24 GLY E 64 VAL E 69 ASP E 72
SITE 2 FC7 5 EDO E1479
SITE 1 FC8 6 LYS E 18 THR E 65 TRP E 66 THR E 67
SITE 2 FC8 6 THR E 68 EDO E1478
SITE 1 FC9 1 GLU E 52
SITE 1 GC1 4 LYS E 466 GLU E 468 PHE E 469 HOH E2159
SITE 1 GC2 4 GLU E 336 GLY E 337 GLU E 338 ASP E 473
SITE 1 GC3 3 ILE N 39 GLY N 82 CYS N 83
SITE 1 GC4 4 GLY L 37 TRP L 38 ILE L 39 GLY L 82
SITE 1 GC5 4 GLY J 37 GLY J 82 CYS J 83 HOH J2036
CRYST1 120.831 178.206 122.917 90.00 117.76 90.00 P 1 21 1 16
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 0.008276 0.000000 0.004356 0.00000
SCALE2 0.000000 0.005611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009194 0.00000
MTRIX1 1 0.594200 0.770100 0.232000 -93.38000 1
MTRIX2 1 0.770300 -0.627900 0.111400 144.00000 1
MTRIX3 1 0.231400 0.112500 -0.966300 163.90000 1
MTRIX1 2 0.095120 -0.772400 -0.628000 101.20000 1
MTRIX2 2 0.290500 0.625000 -0.724600 99.89000 1
MTRIX3 2 0.952100 -0.113500 0.283800 90.32000 1
MTRIX1 3 -0.683200 0.487600 0.543600 -121.90000 1
MTRIX2 3 0.487700 -0.249400 0.836700 43.97000 1
MTRIX3 3 0.543500 0.836700 -0.067420 31.66000 1
MTRIX1 4 -0.814300 -0.482000 0.323300 -23.35000 1
MTRIX2 4 -0.481200 0.249300 -0.840400 126.30000 1
MTRIX3 4 0.324500 -0.839900 -0.435000 201.10000 1
MTRIX1 5 -0.779700 -0.290200 -0.554800 36.44000 1
MTRIX2 5 -0.287800 -0.620700 0.729300 69.22000 1
MTRIX3 5 -0.556000 0.728300 0.400500 -21.33000 1
MTRIX1 6 0.089240 0.290600 0.952700 -124.60000 1
MTRIX2 6 -0.773000 0.623400 -0.117700 26.66000 1
MTRIX3 6 -0.628100 -0.725900 0.280300 110.80000 1
MTRIX1 7 0.497400 -0.007779 -0.867500 65.09000 1
MTRIX2 7 -0.007026 -1.000000 0.004939 169.20000 1
MTRIX3 7 -0.867500 0.003638 -0.497500 110.90000 1
MTRIX1 8 0.591700 0.771900 0.232600 -93.56000 1
MTRIX2 8 0.773200 -0.625000 0.107000 144.40000 1
MTRIX3 8 0.228000 0.116500 -0.966700 163.70000 1
MTRIX1 9 0.096170 -0.771100 -0.629400 101.30000 1
MTRIX2 9 0.283700 0.627400 -0.725200 99.82000 1
MTRIX3 9 0.954100 -0.108800 0.279100 90.54000 1
MTRIX1 10 -0.680300 0.491700 0.543500 -122.20000 1
MTRIX2 10 0.493100 -0.241700 0.835800 43.50000 1
MTRIX3 10 0.542300 0.836600 -0.078010 32.79000 1
MTRIX1 11 -0.811600 -0.482400 0.329600 -24.01000 1
MTRIX2 11 -0.486000 0.244300 -0.839100 126.50000 1
MTRIX3 11 0.324300 -0.841200 -0.432700 200.90000 1
MTRIX1 12 -0.781000 -0.291400 -0.552400 36.24000 1
MTRIX2 12 -0.281000 -0.625900 0.727500 69.77000 1
MTRIX3 12 -0.557800 0.723400 0.407000 -21.73000 1
MTRIX1 13 0.091400 0.287000 0.953600 -124.50000 1
MTRIX2 13 -0.776800 0.619700 -0.112100 26.24000 1
MTRIX3 13 -0.623100 -0.730400 0.279600 111.20000 1
MTRIX1 14 0.496000 -0.006674 -0.868300 65.11000 1
MTRIX2 14 -0.006531 -1.000000 0.003955 169.30000 1
MTRIX3 14 -0.868300 0.003710 -0.496000 110.70000 1
(ATOM LINES ARE NOT SHOWN.)
END
