HEADER OXIDOREDUCTASE 13-JUL-07 2V63
TITLE CRYSTAL STRUCTURE OF RUBISCO FROM CHLAMYDOMONAS REINHARDTII
TITLE 2 WITH A LARGE-SUBUNIT V331A 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: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE SMALL
COMPND 13 CHAIN, RUBISCO SMALL SUBUNIT 1;
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: 2137;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLS-V331A;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 10 ORGANISM_TAXID: 3055;
SOURCE 11 STRAIN: 2137;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PLS-V331A
KEYWDS LARGE SUBUNIT LOOP 6 MUTATION, CO2/O2 SPECIFICITY, CARBON
KEYWDS 2 DIOXIDE FIXATION, PHOTOSYNTHESIS, TRANSIT PEPTIDE,
KEYWDS 3 PHOTORESPIRATION, METAL-BINDING, HYDROXYLATION,
KEYWDS 4 OXIDOREDUCTASE, METHYLATION, CHLOROPLAST, CALVIN CYCLE,
KEYWDS 5 MONOOXYGENASE, LYASE, RUBISCO, PLASTID, MAGNESIUM,
KEYWDS 6 ACETYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,
AUTHOR 2 I.ANDERSSON
REVDAT 6 24-FEB-09 2V63 1 VERSN
REVDAT 5 23-OCT-07 2V63 1 REMARK
REVDAT 4 02-OCT-07 2V63 1 JRNL REMARK
REVDAT 3 28-AUG-07 2V63 1 AUTHOR
REVDAT 2 07-AUG-07 2V63 1 SOURCE REMARK
REVDAT 1 31-JUL-07 2V63 0
JRNL AUTH S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,
JRNL AUTH 2 I.ANDERSSON
JRNL TITL STRUCTURAL ANALYSIS OF ALTERED LARGE-SUBUNIT LOOP-
JRNL TITL 2 6-CARBOXY-TERMINUS INTERACTIONS THAT INFLUENCE
JRNL TITL 3 CATALYTIC EFFICIENCY AND CO2 O2 SPECIFICITY OF
JRNL TITL 4 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE
JRNL REF BIOCHEMISTRY V. 46 11080 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17824672
JRNL DOI 10.1021/BI701063F
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 369935
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 19621
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17388
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 912
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 37813
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 768
REMARK 3 SOLVENT ATOMS : 2892
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.794
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 39483 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 53456 ; 1.108 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4828 ; 5.631 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1859 ;30.604 ;23.168
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6328 ;13.328 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 319 ;15.644 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5656 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30387 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 19533 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 27022 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 3203 ; 0.120 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 14 ; 0.024 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 127 ; 0.291 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.133 ; 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): 24678 ; 0.654 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38601 ; 1.043 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 16985 ; 1.730 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14855 ; 2.795 ; 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): 3636 ; .00 ; .05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3636 ; .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): 3623 ; .02 ; .05
REMARK 3 TIGHT THERMAL 2 B (A**2): 3623 ; .09 ; .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 437 1
REMARK 3 1 A 13 A 437 1
REMARK 3 2 C 442 C 477 1
REMARK 3 2 A 442 A 477 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 3610 ; .02 ; .05
REMARK 3 TIGHT THERMAL 3 C (A**2): 3610 ; .09 ; .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): 3620 ; .02 ; .05
REMARK 3 TIGHT THERMAL 4 D (A**2): 3620 ; .09 ; .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): 3620 ; .02 ; .05
REMARK 3 TIGHT THERMAL 5 E (A**2): 3620 ; .12 ; .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): 3610 ; .02 ; .05
REMARK 3 TIGHT THERMAL 6 F (A**2): 3610 ; .15 ; .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): 3618 ; .02 ; .05
REMARK 3 TIGHT THERMAL 7 G (A**2): 3618 ; .11 ; .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): 3620 ; .02 ; .05
REMARK 3 TIGHT THERMAL 8 H (A**2): 3620 ; .09 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 I (A): 1039 ; .00 ; .05
REMARK 3 TIGHT THERMAL 9 I (A**2): 1039 ; .00 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : J I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 J (A): 1037 ; .03 ; .05
REMARK 3 TIGHT THERMAL 10 J (A**2): 1037 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : K I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 K (A): 1037 ; .02 ; .05
REMARK 3 TIGHT THERMAL 11 K (A**2): 1037 ; .09 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : L I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 L (A): 1039 ; .03 ; .05
REMARK 3 TIGHT THERMAL 12 L (A**2): 1039 ; .10 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : M I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 13 M (A): 1036 ; .03 ; .05
REMARK 3 TIGHT THERMAL 13 M (A**2): 1036 ; .13 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : N I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 14 N (A): 1038 ; .02 ; .05
REMARK 3 TIGHT THERMAL 14 N (A**2): 1038 ; .12 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : O I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 15 O (A): 1037 ; .02 ; .05
REMARK 3 TIGHT THERMAL 15 O (A**2): 1037 ; .08 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : P I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 16 P (A): 1039 ; .02 ; .05
REMARK 3 TIGHT THERMAL 16 P (A**2): 1039 ; .12 ; .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 2V63 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-07.
REMARK 100 THE PDBE ID CODE IS EBI-33172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9392
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 389935
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 14.8
REMARK 200 R MERGE (I) : 0.23
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.46
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.01
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 88.72300
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 127910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 153680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -728.8 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, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, VAL 331 TO ALA
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 LEU A 475
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 LYS B 8
REMARK 465 LEU B 475
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 LEU C 475
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 LEU D 475
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 LEU E 475
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 LEU F 475
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 LEU G 475
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 LEU H 475
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU G 93 - O HOH G 2058 2.15
REMARK 500 O PRO I 20 - O HOH I 2010 2.16
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 -80.48 -138.75
REMARK 500 ASN A 207 -91.39 -119.63
REMARK 500 MET A 212 107.84 -165.91
REMARK 500 MET A 297 -8.68 86.32
REMARK 500 ALA A 331 -44.89 73.92
REMARK 500 SER B 62 -80.29 -137.18
REMARK 500 ASN B 207 -89.56 -121.03
REMARK 500 MET B 212 107.30 -165.96
REMARK 500 MET B 297 -8.13 86.46
REMARK 500 ALA B 331 -45.72 75.38
REMARK 500 ASP B 357 89.92 -158.31
REMARK 500 SER C 62 -81.52 -138.78
REMARK 500 ASN C 207 -89.20 -119.69
REMARK 500 MET C 212 106.63 -166.10
REMARK 500 ALA C 296 130.98 -39.50
REMARK 500 MET C 297 -8.47 87.63
REMARK 500 ALA C 331 -46.61 72.82
REMARK 500 ASP C 357 89.87 -158.38
REMARK 500 SER D 62 -81.70 -137.81
REMARK 500 ASN D 207 -90.69 -119.57
REMARK 500 MET D 212 109.94 -164.83
REMARK 500 ALA D 296 131.84 -38.70
REMARK 500 MET D 297 -11.06 86.71
REMARK 500 ALA D 331 -44.59 76.12
REMARK 500 SER E 62 -81.43 -141.96
REMARK 500 ASN E 207 -92.18 -119.57
REMARK 500 MET E 212 109.88 -162.16
REMARK 500 ALA E 296 130.78 -39.93
REMARK 500 MET E 297 -9.13 87.21
REMARK 500 ALA E 331 -42.96 73.74
REMARK 500 SER F 62 -78.46 -138.37
REMARK 500 ASN F 207 -90.38 -123.61
REMARK 500 MET F 212 105.83 -164.64
REMARK 500 MET F 297 -7.31 84.61
REMARK 500 ALA F 331 -45.54 72.13
REMARK 500 ASP F 357 90.65 -160.32
REMARK 500 SER G 62 -80.59 -139.74
REMARK 500 ASN G 207 -92.41 -121.87
REMARK 500 MET G 212 107.41 -167.13
REMARK 500 ALA G 296 132.46 -36.85
REMARK 500 MET G 297 -8.51 86.96
REMARK 500 ALA G 331 -45.15 72.66
REMARK 500 SER H 62 -81.90 -135.62
REMARK 500 ASN H 207 -92.48 -117.23
REMARK 500 MET H 212 108.26 -164.19
REMARK 500 MET H 297 -6.63 87.03
REMARK 500 ALA H 331 -43.84 75.42
REMARK 500 ASP H 357 89.64 -160.46
REMARK 500 GLU I 13 -142.01 57.95
REMARK 500 PHE I 15 -1.08 82.86
REMARK 500 LYS I 77 -123.79 56.53
REMARK 500 GLU J 13 -140.57 55.34
REMARK 500 PHE J 15 -0.78 81.67
REMARK 500 LYS J 77 -123.45 54.96
REMARK 500 GLU K 13 -140.82 58.57
REMARK 500 PHE K 15 -1.78 82.37
REMARK 500 LYS K 77 -121.87 53.05
REMARK 500 GLU L 13 -140.43 56.41
REMARK 500 PHE L 15 -0.05 84.31
REMARK 500 LYS L 77 -123.54 56.81
REMARK 500 GLU M 13 -141.86 59.27
REMARK 500 PHE M 15 -0.99 82.43
REMARK 500 LYS M 77 -124.49 56.74
REMARK 500 PHE N 12 44.63 -141.13
REMARK 500 GLU N 13 -141.27 59.79
REMARK 500 PHE N 15 -0.66 82.95
REMARK 500 LYS N 77 -124.32 56.38
REMARK 500 PHE O 12 48.83 -140.19
REMARK 500 GLU O 13 -142.02 56.14
REMARK 500 PHE O 15 1.62 82.39
REMARK 500 LYS O 77 -123.34 55.54
REMARK 500 PHE P 12 47.95 -143.04
REMARK 500 GLU P 13 -142.69 57.40
REMARK 500 PHE P 15 -0.31 81.86
REMARK 500 LYS P 77 -124.07 58.34
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 A 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201 OQ1
REMARK 620 2 ASP A 203 OD1 90.2
REMARK 620 3 CAP A 476 O2 94.4 104.3
REMARK 620 4 GLU A 204 OE1 88.5 92.2 163.2
REMARK 620 5 CAP A 476 O3 86.4 176.5 75.1 88.6
REMARK 620 6 CAP A 476 O7 169.3 96.9 76.1 99.1 86.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 201 OQ1
REMARK 620 2 CAP B 477 O2 98.3
REMARK 620 3 CAP B 477 O3 91.0 75.9
REMARK 620 4 ASP B 203 OD1 90.4 101.4 177.1
REMARK 620 5 GLU B 204 OE1 90.7 163.2 89.8 92.7
REMARK 620 6 CAP B 477 O7 171.1 73.3 84.2 94.1 96.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP C 477 O3
REMARK 620 2 KCX C 201 OQ1 89.7
REMARK 620 3 ASP C 203 OD1 177.7 90.9
REMARK 620 4 CAP C 477 O2 74.9 94.7 102.8
REMARK 620 5 GLU C 204 OE1 89.3 91.5 92.9 163.0
REMARK 620 6 CAP C 477 O7 82.3 166.5 96.7 72.9 99.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 203 OD1
REMARK 620 2 GLU D 204 OE1 94.1
REMARK 620 3 CAP D 477 O2 103.3 161.1
REMARK 620 4 CAP D 477 O7 95.1 97.4 74.0
REMARK 620 5 KCX D 201 OQ1 91.5 91.1 95.8 168.8
REMARK 620 6 CAP D 477 O3 177.7 88.0 74.7 85.3 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E 477 O2
REMARK 620 2 CAP E 477 O3 74.0
REMARK 620 3 CAP E 477 O7 76.4 88.0
REMARK 620 4 ASP E 203 OD1 103.6 175.5 95.2
REMARK 620 5 GLU E 204 OE1 162.8 89.8 97.6 92.9
REMARK 620 6 KCX E 201 OQ1 93.4 84.6 168.8 91.8 90.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 203 OD1
REMARK 620 2 CAP F 477 O2 105.4
REMARK 620 3 CAP F 477 O7 94.9 72.8
REMARK 620 4 KCX F 201 OQ1 91.9 95.8 168.0
REMARK 620 5 GLU F 204 OE1 91.0 162.6 100.6 89.2
REMARK 620 6 CAP F 477 O3 179.5 75.0 85.5 87.8 88.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 203 OD1
REMARK 620 2 CAP G 477 O2 101.2
REMARK 620 3 CAP G 477 O7 95.6 73.2
REMARK 620 4 KCX G 201 OQ1 91.0 93.6 166.1
REMARK 620 5 GLU G 204 OE1 95.6 162.3 99.9 91.6
REMARK 620 6 CAP G 477 O3 174.8 73.6 83.7 88.5 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H 477 O3
REMARK 620 2 KCX H 201 OQ1 87.5
REMARK 620 3 CAP H 477 O2 74.6 95.0
REMARK 620 4 CAP H 477 O7 87.4 170.8 76.3
REMARK 620 5 ASP H 203 OD1 176.2 89.4 103.5 95.4
REMARK 620 6 GLU H 204 OE1 89.4 90.0 162.9 97.5 92.8
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 CAP A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1477
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 O1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1476
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UW9 RELATED DB: PDB
REMARK 900 L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
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: 1UZD RELATED DB: PDB
REMARK 900 CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
REMARK 900 RELATED ID: 1UZH RELATED DB: PDB
REMARK 900 A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO
REMARK 900 ENZYME
REMARK 900 RELATED ID: 1GK8 RELATED DB: PDB
REMARK 900 RUBISCO FROM CHLAMYDOMONAS REINHARDTII
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: 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: 2V69 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900 RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E
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 999
REMARK 999 SEQUENCE
REMARK 999 THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877)
REMARK 999 HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR
REMARK 999 AND 2137.
DBREF 2V63 A 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 B 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 C 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 D 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 E 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 F 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 G 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 H 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V63 I 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 J 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 K 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 L 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 M 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 N 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 O 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V63 P 1 140 UNP P00873 RBS1_CHLRE 46 185
SEQADV 2V63 PRO A 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA A 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO B 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA B 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO C 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA C 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO D 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA D 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO E 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA E 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO F 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA F 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO G 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA G 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V63 PRO H 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V63 ALA H 331 UNP P00877 VAL 331 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 CYS 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 ALA 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 CYS 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 ALA 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 CYS 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 ALA 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 CYS 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 ALA 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 CYS 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 ALA 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 CYS 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 ALA 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 CYS 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 ALA 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 CYS 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 ALA 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 2V63 HYP A 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP A 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX A 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC A 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC A 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP B 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP B 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX B 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC B 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC B 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP C 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP C 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX C 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC C 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC C 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP D 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP D 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX D 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC D 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC D 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP E 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP E 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX E 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC E 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC E 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP F 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP F 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX F 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC F 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC F 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP G 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP G 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX G 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC G 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC G 369 CYS S-METHYLCYSTEINE
MODRES 2V63 HYP H 104 PRO 4-HYDROXYPROLINE
MODRES 2V63 HYP H 151 PRO 4-HYDROXYPROLINE
MODRES 2V63 KCX H 201 LYS LYSYL-CARBAMATE
MODRES 2V63 SMC H 256 CYS S-METHYLCYSTEINE
MODRES 2V63 SMC H 369 CYS S-METHYLCYSTEINE
MODRES 2V63 MME I 1 MET N-METHYL METHIONINE
MODRES 2V63 MME J 1 MET N-METHYL METHIONINE
MODRES 2V63 MME K 1 MET N-METHYL METHIONINE
MODRES 2V63 MME L 1 MET N-METHYL METHIONINE
MODRES 2V63 MME M 1 MET N-METHYL METHIONINE
MODRES 2V63 MME N 1 MET N-METHYL METHIONINE
MODRES 2V63 MME O 1 MET N-METHYL METHIONINE
MODRES 2V63 MME P 1 MET N-METHYL METHIONINE
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 CAP A 476 21
HET MG A 477 1
HET MG B 476 1
HET CAP B 477 21
HET MG C 476 1
HET CAP C 477 21
HET MG D 476 1
HET CAP D 477 21
HET MG E 476 1
HET CAP E 477 21
HET MG F 476 1
HET CAP F 477 21
HET MG G 476 1
HET CAP G 477 21
HET MG H 476 1
HET CAP H 477 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 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 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 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 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 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 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 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 A1477 4
HET EDO A1478 4
HET EDO A1479 4
HET EDO H1477 4
HET EDO H1478 4
HET EDO O1141 4
HET EDO O1142 4
HET EDO C1475 4
HET EDO K1141 4
HET EDO B1475 4
HET EDO B1476 4
HET EDO B1477 4
HET EDO B1478 4
HET EDO J1141 4
HET EDO G1479 4
HET EDO D1475 4
HET EDO D1476 4
HET EDO E1475 4
HET EDO E1477 4
HET EDO J1142 4
HET EDO D1477 4
HET EDO D1478 4
HET EDO P1141 4
HET EDO N1141 4
HET EDO N1142 4
HET EDO L1141 4
HET EDO L1142 4
HET EDO A1480 4
HET EDO C1477 4
HET EDO C1478 4
HET EDO C1479 4
HET EDO G1480 4
HET EDO I1141 4
HET EDO K1142 4
HET EDO M1141 4
HET EDO M1142 4
HET EDO C1476 4
HET EDO H1475 4
HET EDO H1476 4
HET EDO G1475 4
HET EDO G1476 4
HET EDO G1477 4
HET EDO G1478 4
HET EDO E1476 4
HET EDO F1475 4
HET EDO F1476 4
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM HYP 4-HYDROXYPROLINE
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM SMC S-METHYLCYSTEINE
HETNAM MME N-METHYL METHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 17 HYP 16(C5 H9 N O3)
FORMUL 18 KCX 8(C7 H14 N2 O4)
FORMUL 19 SMC 16(C4 H9 N O2 S)
FORMUL 20 MME 8(C6 H13 N O2 S)
FORMUL 21 EDO 46(C2 H6 O2)
FORMUL 22 MG 8(MG 2+)
FORMUL 23 CAP 8(C6 H14 O13 P2)
FORMUL 24 HOH *2892(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 GLY A 122 1 11
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 GLY A 154 ASN A 163 1 10
HELIX 10 10 SER A 181 GLY A 195 1 15
HELIX 11 11 ARG A 213 GLY A 233 1 21
HELIX 12 12 THR A 246 VAL A 255 1 10
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 463 1 28
HELIX 23 23 TYR B 20 TYR B 25 1 6
HELIX 24 24 PRO B 49 SER B 61 1 13
HELIX 25 25 VAL B 69 THR B 75 5 7
HELIX 26 26 SER B 76 LYS B 81 1 6
HELIX 27 27 HYP B 104 PHE B 108 5 5
HELIX 28 28 SER B 112 GLY B 122 1 11
HELIX 29 29 ASN B 123 GLY B 126 5 4
HELIX 30 30 PRO B 141 LYS B 146 1 6
HELIX 31 31 GLY B 154 ASN B 163 1 10
HELIX 32 32 SER B 181 GLY B 195 1 15
HELIX 33 33 ARG B 213 GLY B 233 1 21
HELIX 34 34 THR B 246 VAL B 255 1 10
HELIX 35 35 TYR B 269 GLY B 288 1 20
HELIX 36 36 MET B 297 ARG B 303 1 7
HELIX 37 37 HIS B 310 GLY B 322 1 13
HELIX 38 38 GLU B 338 ASP B 351 1 14
HELIX 39 39 ARG B 358 GLY B 361 5 4
HELIX 40 40 HIS B 383 TRP B 385 5 3
HELIX 41 41 HIS B 386 GLY B 395 1 10
HELIX 42 42 GLY B 403 GLY B 408 1 6
HELIX 43 43 GLY B 412 GLU B 433 1 22
HELIX 44 44 ASP B 436 LYS B 463 1 28
HELIX 45 45 TYR C 20 TYR C 25 1 6
HELIX 46 46 PRO C 49 SER C 61 1 13
HELIX 47 47 VAL C 69 THR C 75 5 7
HELIX 48 48 SER C 76 LYS C 81 1 6
HELIX 49 49 HYP C 104 PHE C 108 5 5
HELIX 50 50 SER C 112 GLY C 122 1 11
HELIX 51 51 ASN C 123 GLY C 126 5 4
HELIX 52 52 PRO C 141 LYS C 146 1 6
HELIX 53 53 GLY C 154 ASN C 163 1 10
HELIX 54 54 SER C 181 GLY C 195 1 15
HELIX 55 55 ARG C 213 GLY C 233 1 21
HELIX 56 56 THR C 246 VAL C 255 1 10
HELIX 57 57 TYR C 269 GLY C 288 1 20
HELIX 58 58 MET C 297 ARG C 303 1 7
HELIX 59 59 HIS C 310 GLY C 322 1 13
HELIX 60 60 GLU C 338 ASP C 351 1 14
HELIX 61 61 ARG C 358 GLY C 361 5 4
HELIX 62 62 HIS C 383 TRP C 385 5 3
HELIX 63 63 HIS C 386 GLY C 395 1 10
HELIX 64 64 GLY C 403 GLY C 408 1 6
HELIX 65 65 GLY C 412 GLU C 433 1 22
HELIX 66 66 GLU C 440 SER C 452 1 13
HELIX 67 67 SER C 452 LYS C 463 1 12
HELIX 68 68 TYR D 20 TYR D 25 1 6
HELIX 69 69 PRO D 49 SER D 61 1 13
HELIX 70 70 VAL D 69 THR D 75 5 7
HELIX 71 71 SER D 76 LYS D 81 1 6
HELIX 72 72 HYP D 104 PHE D 108 5 5
HELIX 73 73 SER D 112 GLY D 122 1 11
HELIX 74 74 ASN D 123 GLY D 126 5 4
HELIX 75 75 PRO D 141 LYS D 146 1 6
HELIX 76 76 GLY D 154 ASN D 163 1 10
HELIX 77 77 SER D 181 GLY D 195 1 15
HELIX 78 78 ARG D 213 GLY D 233 1 21
HELIX 79 79 THR D 246 VAL D 255 1 10
HELIX 80 80 TYR D 269 GLY D 288 1 20
HELIX 81 81 MET D 297 ARG D 303 1 7
HELIX 82 82 HIS D 310 GLY D 322 1 13
HELIX 83 83 GLU D 338 ASP D 351 1 14
HELIX 84 84 ARG D 358 GLY D 361 5 4
HELIX 85 85 HIS D 383 TRP D 385 5 3
HELIX 86 86 HIS D 386 GLY D 395 1 10
HELIX 87 87 GLY D 403 GLY D 408 1 6
HELIX 88 88 GLY D 412 GLU D 433 1 22
HELIX 89 89 ASP D 436 LYS D 463 1 28
HELIX 90 90 TYR E 20 TYR E 25 1 6
HELIX 91 91 PRO E 49 SER E 61 1 13
HELIX 92 92 VAL E 69 THR E 75 5 7
HELIX 93 93 SER E 76 LYS E 81 1 6
HELIX 94 94 HYP E 104 PHE E 108 5 5
HELIX 95 95 SER E 112 GLY E 122 1 11
HELIX 96 96 ASN E 123 GLY E 126 5 4
HELIX 97 97 PRO E 141 LYS E 146 1 6
HELIX 98 98 GLY E 154 ASN E 163 1 10
HELIX 99 99 SER E 181 GLY E 195 1 15
HELIX 100 100 ARG E 213 GLY E 233 1 21
HELIX 101 101 THR E 246 VAL E 255 1 10
HELIX 102 102 TYR E 269 GLY E 288 1 20
HELIX 103 103 MET E 297 ARG E 303 1 7
HELIX 104 104 HIS E 310 GLY E 322 1 13
HELIX 105 105 GLU E 338 ASP E 351 1 14
HELIX 106 106 ARG E 358 GLY E 361 5 4
HELIX 107 107 HIS E 383 TRP E 385 5 3
HELIX 108 108 HIS E 386 GLY E 395 1 10
HELIX 109 109 GLY E 403 GLY E 408 1 6
HELIX 110 110 GLY E 412 GLU E 433 1 22
HELIX 111 111 ASP E 436 LYS E 463 1 28
HELIX 112 112 TYR F 20 TYR F 25 1 6
HELIX 113 113 PRO F 49 SER F 61 1 13
HELIX 114 114 VAL F 69 THR F 75 5 7
HELIX 115 115 SER F 76 LYS F 81 1 6
HELIX 116 116 HYP F 104 PHE F 108 5 5
HELIX 117 117 SER F 112 GLY F 122 1 11
HELIX 118 118 ASN F 123 GLY F 126 5 4
HELIX 119 119 PRO F 141 LYS F 146 1 6
HELIX 120 120 GLY F 154 ASN F 163 1 10
HELIX 121 121 SER F 181 GLY F 195 1 15
HELIX 122 122 ARG F 213 GLY F 233 1 21
HELIX 123 123 THR F 246 VAL F 255 1 10
HELIX 124 124 TYR F 269 GLY F 288 1 20
HELIX 125 125 MET F 297 ARG F 303 1 7
HELIX 126 126 HIS F 310 GLY F 322 1 13
HELIX 127 127 GLU F 338 ASP F 351 1 14
HELIX 128 128 ARG F 358 GLY F 361 5 4
HELIX 129 129 HIS F 383 TRP F 385 5 3
HELIX 130 130 HIS F 386 GLY F 395 1 10
HELIX 131 131 GLY F 403 GLY F 408 1 6
HELIX 132 132 GLY F 412 GLU F 433 1 22
HELIX 133 133 ASP F 436 LYS F 463 1 28
HELIX 134 134 TYR G 20 TYR G 25 1 6
HELIX 135 135 PRO G 49 SER G 61 1 13
HELIX 136 136 VAL G 69 THR G 75 5 7
HELIX 137 137 SER G 76 LYS G 81 1 6
HELIX 138 138 HYP G 104 PHE G 108 5 5
HELIX 139 139 SER G 112 GLY G 122 1 11
HELIX 140 140 ASN G 123 GLY G 126 5 4
HELIX 141 141 PRO G 141 LYS G 146 1 6
HELIX 142 142 GLY G 154 ASN G 163 1 10
HELIX 143 143 SER G 181 GLY G 195 1 15
HELIX 144 144 ARG G 213 GLY G 233 1 21
HELIX 145 145 THR G 246 VAL G 255 1 10
HELIX 146 146 TYR G 269 GLY G 288 1 20
HELIX 147 147 MET G 297 ARG G 303 1 7
HELIX 148 148 HIS G 310 GLY G 322 1 13
HELIX 149 149 GLU G 338 ASP G 351 1 14
HELIX 150 150 ARG G 358 GLY G 361 5 4
HELIX 151 151 HIS G 383 TRP G 385 5 3
HELIX 152 152 HIS G 386 GLY G 395 1 10
HELIX 153 153 GLY G 403 GLY G 408 1 6
HELIX 154 154 GLY G 412 GLU G 433 1 22
HELIX 155 155 ASP G 436 LYS G 463 1 28
HELIX 156 156 TYR H 20 TYR H 25 1 6
HELIX 157 157 PRO H 49 SER H 61 1 13
HELIX 158 158 VAL H 69 THR H 75 5 7
HELIX 159 159 SER H 76 LYS H 81 1 6
HELIX 160 160 HYP H 104 PHE H 108 5 5
HELIX 161 161 SER H 112 GLY H 122 1 11
HELIX 162 162 ASN H 123 GLY H 126 5 4
HELIX 163 163 PRO H 141 LYS H 146 1 6
HELIX 164 164 GLY H 154 ASN H 163 1 10
HELIX 165 165 SER H 181 GLY H 195 1 15
HELIX 166 166 ARG H 213 GLY H 233 1 21
HELIX 167 167 THR H 246 VAL H 255 1 10
HELIX 168 168 TYR H 269 GLY H 288 1 20
HELIX 169 169 MET H 297 ARG H 303 1 7
HELIX 170 170 HIS H 310 GLY H 322 1 13
HELIX 171 171 GLU H 338 ASP H 351 1 14
HELIX 172 172 ARG H 358 GLY H 361 5 4
HELIX 173 173 HIS H 383 TRP H 385 5 3
HELIX 174 174 HIS H 386 GLY H 395 1 10
HELIX 175 175 GLY H 403 GLY H 408 1 6
HELIX 176 176 GLY H 412 GLU H 433 1 22
HELIX 177 177 ASP H 436 LYS H 463 1 28
HELIX 178 178 THR I 22 GLY I 37 1 16
HELIX 179 179 GLU I 46 ALA I 50 5 5
HELIX 180 180 ASN I 54 PHE I 60 5 7
HELIX 181 181 ASP I 85 PHE I 100 1 16
HELIX 182 182 PRO I 134 ARG I 138 5 5
HELIX 183 183 THR J 22 GLY J 37 1 16
HELIX 184 184 GLU J 46 ALA J 50 5 5
HELIX 185 185 ASN J 54 PHE J 60 5 7
HELIX 186 186 ASP J 85 PHE J 100 1 16
HELIX 187 187 PRO J 134 ARG J 138 5 5
HELIX 188 188 THR K 22 GLY K 37 1 16
HELIX 189 189 GLU K 46 ALA K 50 5 5
HELIX 190 190 ASN K 54 PHE K 60 5 7
HELIX 191 191 ASP K 85 PHE K 100 1 16
HELIX 192 192 PRO K 134 ARG K 138 5 5
HELIX 193 193 THR L 22 ASN L 36 1 15
HELIX 194 194 GLU L 46 ALA L 50 5 5
HELIX 195 195 ASN L 54 PHE L 60 5 7
HELIX 196 196 ASP L 85 PHE L 100 1 16
HELIX 197 197 PRO L 134 ARG L 138 5 5
HELIX 198 198 THR M 22 GLY M 37 1 16
HELIX 199 199 GLU M 46 ALA M 50 5 5
HELIX 200 200 ASN M 54 PHE M 60 5 7
HELIX 201 201 ASP M 85 PHE M 100 1 16
HELIX 202 202 PRO M 134 ARG M 138 5 5
HELIX 203 203 THR N 22 GLY N 37 1 16
HELIX 204 204 GLU N 46 ALA N 50 5 5
HELIX 205 205 ASN N 54 PHE N 60 5 7
HELIX 206 206 ASP N 85 PHE N 100 1 16
HELIX 207 207 PRO N 134 ARG N 138 5 5
HELIX 208 208 THR O 22 GLY O 37 1 16
HELIX 209 209 GLU O 46 ALA O 50 5 5
HELIX 210 210 ASN O 54 PHE O 60 5 7
HELIX 211 211 ASP O 85 PHE O 100 1 16
HELIX 212 212 PRO O 134 ARG O 138 5 5
HELIX 213 213 THR P 22 ASN P 36 1 15
HELIX 214 214 GLU P 46 ALA P 50 5 5
HELIX 215 215 ASN P 54 PHE P 60 5 7
HELIX 216 216 ASP P 85 PHE P 100 1 16
HELIX 217 217 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 A 247 CYS B 247 1555 1555 2.08
SSBOND 2 CYS C 247 CYS D 247 1555 1555 2.08
SSBOND 3 CYS E 247 CYS F 247 1555 1555 2.07
SSBOND 4 CYS G 247 CYS H 247 1555 1555 2.09
LINK C TYR A 103 N HYP A 104 1555 1555 1.35
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 1.33
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 A 477 OQ1 KCX A 201 1555 1555 2.02
LINK MG MG A 477 OD1 ASP A 203 1555 1555 1.98
LINK MG MG A 477 O2 CAP A 476 1555 1555 2.25
LINK MG MG A 477 OE1 GLU A 204 1555 1555 2.03
LINK MG MG A 477 O3 CAP A 476 1555 1555 2.14
LINK MG MG A 477 O7 CAP A 476 1555 1555 2.11
LINK C TYR B 103 N HYP B 104 1555 1555 1.35
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 1.34
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 1.33
LINK C SMC B 369 N SER B 370 1555 1555 1.34
LINK MG MG B 476 OQ1 KCX B 201 1555 1555 1.99
LINK MG MG B 476 O2 CAP B 477 1555 1555 2.27
LINK MG MG B 476 O3 CAP B 477 1555 1555 2.07
LINK MG MG B 476 OD1 ASP B 203 1555 1555 2.03
LINK MG MG B 476 OE1 GLU B 204 1555 1555 2.01
LINK MG MG B 476 O7 CAP B 477 1555 1555 2.24
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 1.34
LINK C HYP C 151 N PRO C 152 1555 1555 1.34
LINK C THR C 200 N KCX C 201 1555 1555 1.33
LINK C KCX C 201 N ASP C 202 1555 1555 1.34
LINK C VAL C 255 N SMC C 256 1555 1555 1.33
LINK C SMC C 256 N ALA C 257 1555 1555 1.33
LINK C TRP C 368 N SMC C 369 1555 1555 1.33
LINK C SMC C 369 N SER C 370 1555 1555 1.33
LINK MG MG C 476 O3 CAP C 477 1555 1555 2.11
LINK MG MG C 476 OQ1 KCX C 201 1555 1555 1.95
LINK MG MG C 476 OD1 ASP C 203 1555 1555 1.97
LINK MG MG C 476 O2 CAP C 477 1555 1555 2.33
LINK MG MG C 476 OE1 GLU C 204 1555 1555 1.98
LINK MG MG C 476 O7 CAP C 477 1555 1555 2.17
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 1.34
LINK C THR D 200 N KCX D 201 1555 1555 1.32
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 1.33
LINK MG MG D 476 O7 CAP D 477 1555 1555 2.14
LINK MG MG D 476 O2 CAP D 477 1555 1555 2.24
LINK MG MG D 476 O3 CAP D 477 1555 1555 2.13
LINK MG MG D 476 OQ1 KCX D 201 1555 1555 1.97
LINK MG MG D 476 OE1 GLU D 204 1555 1555 2.08
LINK MG MG D 476 OD1 ASP D 203 1555 1555 1.96
LINK C TYR E 103 N HYP E 104 1555 1555 1.35
LINK C HYP E 104 N ILE E 105 1555 1555 1.33
LINK C GLY E 150 N HYP E 151 1555 1555 1.35
LINK C HYP E 151 N PRO E 152 1555 1555 1.34
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 1.33
LINK C SMC E 369 N SER E 370 1555 1555 1.33
LINK MG MG E 476 OQ1 KCX E 201 1555 1555 1.99
LINK MG MG E 476 OD1 ASP E 203 1555 1555 1.97
LINK MG MG E 476 O7 CAP E 477 1555 1555 2.14
LINK MG MG E 476 OE1 GLU E 204 1555 1555 2.05
LINK MG MG E 476 O3 CAP E 477 1555 1555 2.13
LINK MG MG E 476 O2 CAP E 477 1555 1555 2.24
LINK C TYR F 103 N HYP F 104 1555 1555 1.35
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 1.35
LINK C THR F 200 N KCX F 201 1555 1555 1.32
LINK C KCX F 201 N ASP F 202 1555 1555 1.33
LINK C VAL F 255 N SMC F 256 1555 1555 1.34
LINK C SMC F 256 N ALA F 257 1555 1555 1.33
LINK C TRP F 368 N SMC F 369 1555 1555 1.33
LINK C SMC F 369 N SER F 370 1555 1555 1.34
LINK MG MG F 476 OE1 GLU F 204 1555 1555 2.01
LINK MG MG F 476 O3 CAP F 477 1555 1555 2.16
LINK MG MG F 476 OQ1 KCX F 201 1555 1555 1.98
LINK MG MG F 476 O7 CAP F 477 1555 1555 2.13
LINK MG MG F 476 O2 CAP F 477 1555 1555 2.28
LINK MG MG F 476 OD1 ASP F 203 1555 1555 1.96
LINK C TYR G 103 N HYP G 104 1555 1555 1.35
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 1.33
LINK C TRP G 368 N SMC G 369 1555 1555 1.33
LINK C SMC G 369 N SER G 370 1555 1555 1.33
LINK MG MG G 476 OD1 ASP G 203 1555 1555 1.95
LINK MG MG G 476 O2 CAP G 477 1555 1555 2.25
LINK MG MG G 476 O7 CAP G 477 1555 1555 2.21
LINK MG MG G 476 OQ1 KCX G 201 1555 1555 1.96
LINK MG MG G 476 O3 CAP G 477 1555 1555 2.15
LINK MG MG G 476 OE1 GLU G 204 1555 1555 1.96
LINK C TYR H 103 N HYP H 104 1555 1555 1.35
LINK C HYP H 104 N ILE H 105 1555 1555 1.33
LINK C GLY H 150 N HYP H 151 1555 1555 1.34
LINK C HYP H 151 N PRO H 152 1555 1555 1.35
LINK C THR H 200 N KCX H 201 1555 1555 1.33
LINK C KCX H 201 N ASP H 202 1555 1555 1.33
LINK C VAL H 255 N SMC H 256 1555 1555 1.33
LINK C SMC H 256 N ALA H 257 1555 1555 1.33
LINK C TRP H 368 N SMC H 369 1555 1555 1.33
LINK C SMC H 369 N SER H 370 1555 1555 1.33
LINK MG MG H 476 OE1 GLU H 204 1555 1555 2.03
LINK MG MG H 476 OD1 ASP H 203 1555 1555 2.02
LINK MG MG H 476 O7 CAP H 477 1555 1555 2.13
LINK MG MG H 476 O2 CAP H 477 1555 1555 2.28
LINK MG MG H 476 OQ1 KCX H 201 1555 1555 1.97
LINK MG MG H 476 O3 CAP H 477 1555 1555 2.17
LINK C MME I 1 N MET I 2 1555 1555 1.33
LINK C MME J 1 N MET J 2 1555 1555 1.33
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 1.33
LINK C MME P 1 N MET P 2 1555 1555 1.33
CISPEP 1 LYS A 175 PRO A 176 0 -0.81
CISPEP 2 LYS B 175 PRO B 176 0 0.38
CISPEP 3 LYS C 175 PRO C 176 0 -1.96
CISPEP 4 LYS D 175 PRO D 176 0 -0.56
CISPEP 5 LYS E 175 PRO E 176 0 -1.12
CISPEP 6 LYS F 175 PRO F 176 0 -3.57
CISPEP 7 LYS G 175 PRO G 176 0 -0.77
CISPEP 8 LYS H 175 PRO H 176 0 -1.19
SITE 1 AC1 28 THR A 173 LYS A 175 LYS A 177 KCX A 201
SITE 2 AC1 28 ASP A 203 GLU A 204 HIS A 294 ARG A 295
SITE 3 AC1 28 HIS A 327 LYS A 334 LEU A 335 SER A 379
SITE 4 AC1 28 GLY A 380 GLY A 381 GLY A 403 GLY A 404
SITE 5 AC1 28 MG A 477 HOH A2125 HOH A2244 HOH A2289
SITE 6 AC1 28 HOH A2290 HOH A2291 HOH A2292 GLU B 60
SITE 7 AC1 28 THR B 65 TRP B 66 ASN B 123 HOH B2034
SITE 1 AC2 5 LYS A 177 KCX A 201 ASP A 203 GLU A 204
SITE 2 AC2 5 CAP A 476
SITE 1 AC3 4 KCX B 201 ASP B 203 GLU B 204 CAP B 477
SITE 1 AC4 30 GLU A 60 THR A 65 TRP A 66 ASN A 123
SITE 2 AC4 30 HOH A2091 HOH A2092 THR B 173 LYS B 175
SITE 3 AC4 30 LYS B 177 KCX B 201 ASP B 203 GLU B 204
SITE 4 AC4 30 HIS B 294 ARG B 295 HIS B 327 LYS B 334
SITE 5 AC4 30 LEU B 335 SER B 379 GLY B 380 GLY B 381
SITE 6 AC4 30 GLY B 403 GLY B 404 MG B 476 HOH B2115
SITE 7 AC4 30 HOH B2116 HOH B2233 HOH B2279 HOH B2280
SITE 8 AC4 30 HOH B2281 HOH B2282
SITE 1 AC5 4 KCX C 201 ASP C 203 GLU C 204 CAP C 477
SITE 1 AC6 30 THR C 173 LYS C 175 LYS C 177 KCX C 201
SITE 2 AC6 30 ASP C 203 GLU C 204 HIS C 294 ARG C 295
SITE 3 AC6 30 HIS C 327 LYS C 334 LEU C 335 SER C 379
SITE 4 AC6 30 GLY C 380 GLY C 381 GLY C 403 GLY C 404
SITE 5 AC6 30 MG C 476 HOH C2120 HOH C2121 HOH C2226
SITE 6 AC6 30 HOH C2239 HOH C2273 HOH C2274 HOH C2275
SITE 7 AC6 30 GLU D 60 THR D 65 TRP D 66 ASN D 123
SITE 8 AC6 30 HOH D2034 HOH D2085
SITE 1 AC7 5 LYS D 177 KCX D 201 ASP D 203 GLU D 204
SITE 2 AC7 5 CAP D 477
SITE 1 AC8 30 GLU C 60 THR C 65 TRP C 66 ASN C 123
SITE 2 AC8 30 HOH C2038 HOH C2088 THR D 173 LYS D 175
SITE 3 AC8 30 LYS D 177 KCX D 201 ASP D 203 GLU D 204
SITE 4 AC8 30 HIS D 294 ARG D 295 HIS D 327 LYS D 334
SITE 5 AC8 30 LEU D 335 SER D 379 GLY D 380 GLY D 381
SITE 6 AC8 30 GLY D 403 GLY D 404 MG D 476 HOH D2119
SITE 7 AC8 30 HOH D2120 HOH D2256 HOH D2257 HOH D2258
SITE 8 AC8 30 HOH D2259 HOH D2260
SITE 1 AC9 5 LYS E 177 KCX E 201 ASP E 203 GLU E 204
SITE 2 AC9 5 CAP E 477
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 E 476 HOH E2096 HOH E2205 HOH E2220
SITE 6 BC1 28 HOH E2259 HOH E2260 HOH E2261 GLU F 60
SITE 7 BC1 28 THR F 65 TRP F 66 ASN F 123 HOH F2078
SITE 1 BC2 5 LYS F 177 KCX F 201 ASP F 203 GLU F 204
SITE 2 BC2 5 CAP F 477
SITE 1 BC3 29 GLU E 60 THR E 65 TRP E 66 ASN E 123
SITE 2 BC3 29 HOH E2023 HOH E2061 THR F 173 LYS F 175
SITE 3 BC3 29 LYS F 177 KCX F 201 ASP F 203 GLU F 204
SITE 4 BC3 29 HIS F 294 ARG F 295 HIS F 327 LYS F 334
SITE 5 BC3 29 LEU F 335 SER F 379 GLY F 380 GLY F 381
SITE 6 BC3 29 GLY F 403 GLY F 404 MG F 476 HOH F2245
SITE 7 BC3 29 HOH F2246 HOH F2247 HOH F2248 HOH F2249
SITE 8 BC3 29 HOH F2250
SITE 1 BC4 5 LYS G 177 KCX G 201 ASP G 203 GLU G 204
SITE 2 BC4 5 CAP G 477
SITE 1 BC5 29 THR G 173 LYS G 175 LYS G 177 KCX G 201
SITE 2 BC5 29 ASP G 203 GLU G 204 HIS G 294 ARG G 295
SITE 3 BC5 29 HIS G 327 LYS G 334 LEU G 335 SER G 379
SITE 4 BC5 29 GLY G 380 GLY G 381 GLY G 403 GLY G 404
SITE 5 BC5 29 MG G 476 HOH G2121 HOH G2227 HOH G2279
SITE 6 BC5 29 HOH G2280 HOH G2281 HOH G2282 GLU H 60
SITE 7 BC5 29 THR H 65 TRP H 66 ASN H 123 HOH H2038
SITE 8 BC5 29 HOH H2088
SITE 1 BC6 5 LYS H 177 KCX H 201 ASP H 203 GLU H 204
SITE 2 BC6 5 CAP H 477
SITE 1 BC7 30 GLU G 60 THR G 65 TRP G 66 ASN G 123
SITE 2 BC7 30 HOH G2038 HOH G2082 THR H 173 LYS H 175
SITE 3 BC7 30 LYS H 177 KCX H 201 ASP H 203 GLU H 204
SITE 4 BC7 30 HIS H 294 ARG H 295 HIS H 327 LYS H 334
SITE 5 BC7 30 LEU H 335 SER H 379 GLY H 380 GLY H 381
SITE 6 BC7 30 GLY H 403 GLY H 404 MG H 476 HOH H2119
SITE 7 BC7 30 HOH H2120 HOH H2234 HOH H2245 HOH H2277
SITE 8 BC7 30 HOH H2278 HOH H2279
SITE 1 BC8 8 VAL A 17 LYS A 18 THR A 65 TRP A 66
SITE 2 BC8 8 THR A 67 THR A 68 HOH A2014 HOH A2293
SITE 1 BC9 2 GLU A 52 HOH A2294
SITE 1 CC1 7 ARG A 295 SER A 328 GLY A 329 GLU A 336
SITE 2 CC1 7 PHE A 345 HOH A2193 HOH A2295
SITE 1 CC2 4 LYS H 466 GLU H 468 PHE H 469 HOH H2281
SITE 1 CC3 8 ARG H 295 HIS H 298 ASP H 302 PHE H 311
SITE 2 CC3 8 SER H 328 GLU H 336 PHE H 345 HOH H2199
SITE 1 CC4 4 TYR A 226 LYS O 49 GLU O 55 HOH O2079
SITE 1 CC5 6 GLY O 37 TRP O 38 PHE O 81 GLY O 82
SITE 2 CC5 6 CYS O 83 HOH O2081
SITE 1 CC6 8 VAL C 17 LYS C 18 THR C 65 TRP C 66
SITE 2 CC6 8 THR C 67 THR C 68 HOH C2021 HOH C2040
SITE 1 CC7 5 GLY K 37 TRP K 38 ILE K 39 GLY K 82
SITE 2 CC7 5 CYS K 83
SITE 1 CC8 9 TYR B 24 GLY B 64 THR B 68 VAL B 69
SITE 2 CC8 9 ASP B 72 EDO B1476 HOH B2283 HOH B2284
SITE 3 CC8 9 HOH B2285
SITE 1 CC9 9 VAL B 17 LYS B 18 THR B 65 TRP B 66
SITE 2 CC9 9 THR B 67 THR B 68 EDO B1475 HOH B2283
SITE 3 CC9 9 HOH B2286
SITE 1 DC1 3 PHE A 469 HOH A2296 TYR B 20
SITE 1 DC2 5 HOH A2294 LYS B 466 PHE B 467 GLU B 468
SITE 2 DC2 5 PHE B 469
SITE 1 DC3 6 TYR H 226 ALA H 230 LYS J 49 GLU J 55
SITE 2 DC3 6 ASP J 69 HOH J2083
SITE 1 DC4 6 LEU G 270 GLY G 273 PHE G 274 HOH G2287
SITE 2 DC4 6 LEU H 270 THR H 271
SITE 1 DC5 8 LYS D 18 THR D 65 TRP D 66 THR D 67
SITE 2 DC5 8 THR D 68 EDO D1477 HOH D2037 HOH D2261
SITE 1 DC6 5 LYS D 466 PHE D 467 GLU D 468 PHE D 469
SITE 2 DC6 5 HOH D2262
SITE 1 DC7 6 TYR E 24 THR E 68 VAL E 69 ASP E 72
SITE 2 DC7 6 HOH E2026 HOH E2262
SITE 1 DC8 4 LYS E 466 PHE E 467 GLU E 468 PHE E 469
SITE 1 DC9 6 GLY J 37 TRP J 38 PHE J 81 GLY J 82
SITE 2 DC9 6 CYS J 83 HOH J2084
SITE 1 EC1 8 TYR D 24 THR D 68 VAL D 69 ASP D 72
SITE 2 EC1 8 EDO D1475 HOH D2036 HOH D2037 HOH D2045
SITE 1 EC2 5 ARG D 295 PHE D 311 GLY D 329 GLU D 336
SITE 2 EC2 5 HOH D2191
SITE 1 EC3 5 TYR F 226 LYS P 49 GLU P 55 HOH P2045
SITE 2 EC3 5 HOH P2077
SITE 1 EC4 6 TYR D 226 HOH D2146 LYS N 49 GLU N 55
SITE 2 EC4 6 ASP N 69 HOH N2033
SITE 1 EC5 6 GLY N 37 ILE N 39 PHE N 81 GLY N 82
SITE 2 EC5 6 CYS N 83 HOH N2072
SITE 1 EC6 7 TYR B 226 LYS B 227 HOH B2142 LYS L 49
SITE 2 EC6 7 GLU L 55 SER L 56 ASP L 69
SITE 1 EC7 5 GLY A 10 HOH A2051 GLY L 37 ILE L 39
SITE 2 EC7 5 GLY L 82
SITE 1 EC8 4 LYS A 466 GLU A 468 PHE A 469 HOH A2296
SITE 1 EC9 4 TYR C 20 GLU C 52 HOH C2277 HOH C2278
SITE 1 FC1 6 LYS C 466 PHE C 467 GLU C 468 PHE C 469
SITE 2 FC1 6 HOH C2279 HOH C2280
SITE 1 FC2 5 ARG C 295 PHE C 345 ASP C 473 HOH C2281
SITE 2 FC2 5 HOH C2282
SITE 1 FC3 3 TYR G 20 GLU G 52 HOH H2281
SITE 1 FC4 5 TYR C 226 LYS I 49 GLU I 55 HOH I2039
SITE 2 FC4 5 HOH I2075
SITE 1 FC5 5 TYR E 226 HOH E2126 LYS K 49 GLU K 55
SITE 2 FC5 5 HOH K2051
SITE 1 FC6 5 TYR G 226 LYS M 49 GLU M 55 HOH M2056
SITE 2 FC6 5 HOH M2103
SITE 1 FC7 8 GLY H 10 GLY M 37 ILE M 39 PHE M 81
SITE 2 FC7 8 GLY M 82 HOH M2104 HOH M2105 HOH M2106
SITE 1 FC8 4 LEU C 270 HOH C2276 LEU D 270 HOH D2167
SITE 1 FC9 7 LYS H 18 THR H 65 TRP H 66 THR H 67
SITE 2 FC9 7 THR H 68 HOH H2019 HOH H2280
SITE 1 GC1 1 GLU H 52
SITE 1 GC2 9 TYR G 24 GLY G 64 THR G 68 VAL G 69
SITE 2 GC2 9 ASP G 72 EDO G1476 HOH G2283 HOH G2284
SITE 3 GC2 9 HOH G2285
SITE 1 GC3 8 LYS G 18 THR G 65 TRP G 66 THR G 67
SITE 2 GC3 8 THR G 68 EDO G1475 HOH G2013 HOH G2284
SITE 1 GC4 5 LYS G 466 PHE G 467 GLU G 468 PHE G 469
SITE 2 GC4 5 HOH G2286
SITE 1 GC5 3 ARG G 295 PHE G 345 ASP G 473
SITE 1 GC6 7 LYS E 18 THR E 65 TRP E 66 THR E 67
SITE 2 GC6 7 THR E 68 HOH E2006 HOH E2026
SITE 1 GC7 7 LYS F 18 THR F 65 TRP F 66 THR F 67
SITE 2 GC7 7 THR F 68 HOH F2251 HOH F2252
SITE 1 GC8 2 GLU F 52 HOH F2253
CRYST1 121.377 177.446 122.568 90.00 117.65 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 0.008239 0.000000 0.004316 0.00000
SCALE2 0.000000 0.005636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009211 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
