HEADER OXIDOREDUCTASE 13-JUL-07 2V68
TITLE CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-
TITLE 2 SUBUNIT MUTATIONS V331A, T342I
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: RUBISCO LARGE SUBUNIT, RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE
COMPND 5 LARGE CHAIN;
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 FRAGMENT: RESIDUES 46-185;
COMPND 13 SYNONYM: RUBISCO SMALL SUBUNIT 1,RIBULOSE-1,5-BISPHOSPHATE
COMPND 14 CARBOXYLASE SMALL CHAIN;
COMPND 15 EC: 4.1.1.39;
COMPND 16 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 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 9 ORGANISM_TAXID: 3055;
SOURCE 10 STRAIN: 2137;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LARGE SUBUNIT LOOP 6 MUTATION, CO2/O2 SPECIFICITY, CARBON DIOXIDE
KEYWDS 2 FIXATION, PHOTOSYNTHESIS, TRANSIT PEPTIDE, PHOTORESPIRATION, METAL-
KEYWDS 3 BINDING, HYDROXYLATION, OXIDOREDUCTASE, METHYLATION, CHLOROPLAST,
KEYWDS 4 CALVIN CYCLE, MONOOXYGENASE, LYASE, RUBISCO, PLASTID, MAGNESIUM,
KEYWDS 5 ACETYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,I.ANDERSSON
REVDAT 7 13-DEC-23 2V68 1 REMARK LINK
REVDAT 6 17-JAN-18 2V68 1 REMARK
REVDAT 5 24-FEB-09 2V68 1 VERSN
REVDAT 4 23-OCT-07 2V68 1 REMARK
REVDAT 3 02-OCT-07 2V68 1 JRNL REMARK
REVDAT 2 28-AUG-07 2V68 1 AUTHOR
REVDAT 1 07-AUG-07 2V68 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
JRNL TITL 2 LOOP-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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 191997
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10153
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14110
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 726
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 38202
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 372
REMARK 3 SOLVENT ATOMS : 2276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.486
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.728
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 39580 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 53581 ; 1.230 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4834 ; 6.196 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1866 ;31.745 ;23.183
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6359 ;14.625 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 320 ;16.232 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5667 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30468 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 20011 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 26819 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 3037 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 10 ; 0.055 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 99 ; 0.242 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.177 ; 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): 24753 ; 0.562 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38663 ; 0.901 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 17043 ; 1.509 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14918 ; 2.424 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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): 3642 ; 0.00 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3642 ; 0.00 ; 0.50
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): 3637 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 2 B (A**2): 3637 ; 0.11 ; 0.50
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): 3624 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 3 C (A**2): 3624 ; 0.12 ; 0.50
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): 3642 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 4 D (A**2): 3642 ; 0.11 ; 0.50
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): 3641 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 5 E (A**2): 3641 ; 0.12 ; 0.50
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): 3638 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 6 F (A**2): 3638 ; 0.12 ; 0.50
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): 3640 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 7 G (A**2): 3640 ; 0.12 ; 0.50
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): 3642 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 8 H (A**2): 3642 ; 0.12 ; 0.50
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 ; 0.00 ; 0.05
REMARK 3 TIGHT THERMAL 9 I (A**2): 1039 ; 0.00 ; 0.50
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): 1039 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 10 J (A**2): 1039 ; 0.11 ; 0.50
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 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 11 K (A**2): 1037 ; 0.10 ; 0.50
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 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 12 L (A**2): 1039 ; 0.11 ; 0.50
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): 1039 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 13 M (A**2): 1039 ; 0.13 ; 0.50
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): 1037 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 14 N (A**2): 1037 ; 0.10 ; 0.50
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 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 15 O (A**2): 1037 ; 0.11 ; 0.50
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 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 16 P (A**2): 1039 ; 0.11 ; 0.50
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2V68 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1290033193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0890
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 1285694
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 20.30
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 (%): 39.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 89.11800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 125120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 150520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -731.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: 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, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, THR 342 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, THR 342 TO ILE
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 LYS A 8
REMARK 465 ALA A 9
REMARK 465 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 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 MET D 1
REMARK 465 VAL D 2
REMARK 465 PRO D 3
REMARK 465 GLN D 4
REMARK 465 THR D 5
REMARK 465 GLU D 6
REMARK 465 THR D 7
REMARK 465 LYS D 8
REMARK 465 ALA D 9
REMARK 465 GLY D 10
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 PRO E 3
REMARK 465 GLN E 4
REMARK 465 THR E 5
REMARK 465 GLU E 6
REMARK 465 THR E 7
REMARK 465 LYS E 8
REMARK 465 ALA E 9
REMARK 465 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 MET G 1
REMARK 465 VAL G 2
REMARK 465 PRO G 3
REMARK 465 GLN G 4
REMARK 465 THR G 5
REMARK 465 GLU G 6
REMARK 465 THR G 7
REMARK 465 LYS G 8
REMARK 465 ALA G 9
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 PRO H 3
REMARK 465 GLN H 4
REMARK 465 THR H 5
REMARK 465 GLU H 6
REMARK 465 THR H 7
REMARK 465 LYS H 8
REMARK 465 ALA H 9
REMARK 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 HOH C 2003 O HOH D 2184 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 11 120.67 75.94
REMARK 500 SER A 62 -80.61 -139.11
REMARK 500 THR A 65 -168.46 -128.54
REMARK 500 HIS A 153 -54.79 -137.87
REMARK 500 CYS A 172 125.50 -175.24
REMARK 500 ASN A 207 -95.67 -121.88
REMARK 500 MET A 212 108.85 -163.73
REMARK 500 TYR A 239 98.71 -68.33
REMARK 500 ALA A 296 131.12 -39.41
REMARK 500 MET A 297 -11.68 87.24
REMARK 500 ALA A 331 -49.34 71.51
REMARK 500 ASP A 357 88.73 -157.38
REMARK 500 SER B 62 -76.95 -138.85
REMARK 500 THR B 65 -168.26 -127.40
REMARK 500 HIS B 153 -53.61 -138.15
REMARK 500 CYS B 172 121.81 -171.87
REMARK 500 ASN B 207 -94.18 -118.75
REMARK 500 MET B 212 110.24 -163.98
REMARK 500 MET B 297 -11.17 90.94
REMARK 500 ALA B 331 -49.19 71.12
REMARK 500 ASP B 357 87.91 -157.01
REMARK 500 SMC B 369 50.82 39.37
REMARK 500 THR B 406 -55.02 -121.14
REMARK 500 SER C 62 -76.66 -140.06
REMARK 500 THR C 65 -169.00 -126.20
REMARK 500 HIS C 153 -57.48 -135.65
REMARK 500 CYS C 172 123.79 -173.45
REMARK 500 ASN C 207 -94.05 -124.42
REMARK 500 MET C 212 110.07 -165.37
REMARK 500 TYR C 239 97.97 -67.52
REMARK 500 ALA C 296 129.84 -38.38
REMARK 500 MET C 297 -12.73 87.67
REMARK 500 ALA C 331 -48.80 69.94
REMARK 500 ASP C 357 87.77 -160.85
REMARK 500 THR C 406 -54.36 -120.64
REMARK 500 SER D 62 -78.72 -140.82
REMARK 500 HIS D 153 -57.21 -139.16
REMARK 500 CYS D 172 124.51 -175.58
REMARK 500 ASN D 207 -93.73 -121.97
REMARK 500 MET D 212 110.32 -163.32
REMARK 500 TYR D 239 97.57 -68.25
REMARK 500 ALA D 296 132.01 -36.61
REMARK 500 MET D 297 -13.57 85.28
REMARK 500 ALA D 331 -50.45 74.39
REMARK 500 ALA E 11 110.98 53.98
REMARK 500 SER E 62 -79.05 -140.71
REMARK 500 HIS E 153 -60.19 -135.09
REMARK 500 CYS E 172 124.67 -173.34
REMARK 500 ASN E 207 -95.30 -126.56
REMARK 500 TYR E 239 99.85 -67.86
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201 OQ2
REMARK 620 2 ASP A 203 OD1 91.9
REMARK 620 3 GLU A 204 OE1 90.5 93.1
REMARK 620 4 CAP A 477 O2 94.2 105.9 160.2
REMARK 620 5 CAP A 477 O3 86.3 177.9 85.8 75.3
REMARK 620 6 CAP A 477 O7 166.0 97.8 98.9 73.6 84.1
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 OQ2
REMARK 620 2 ASP B 203 OD1 86.0
REMARK 620 3 GLU B 204 OE1 90.1 88.2
REMARK 620 4 CAP B 477 O2 99.2 108.2 161.6
REMARK 620 5 CAP B 477 O3 91.4 175.8 88.6 75.4
REMARK 620 6 CAP B 477 O7 171.5 97.3 97.8 72.4 85.8
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 KCX C 201 OQ2
REMARK 620 2 ASP C 203 OD1 98.4
REMARK 620 3 GLU C 204 OE1 93.1 90.6
REMARK 620 4 CAP C 477 O3 88.8 170.3 82.5
REMARK 620 5 CAP C 477 O2 96.4 107.7 157.8 77.6
REMARK 620 6 CAP C 477 O7 163.5 96.7 93.3 77.0 72.6
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 KCX D 201 OQ2
REMARK 620 2 ASP D 203 OD1 90.1
REMARK 620 3 GLU D 204 OE1 91.1 91.7
REMARK 620 4 CAP D 477 O3 88.1 176.7 85.7
REMARK 620 5 CAP D 477 O7 169.4 95.4 97.8 86.9
REMARK 620 6 CAP D 477 O2 96.2 104.9 161.9 78.0 73.7
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 KCX E 201 OQ2
REMARK 620 2 ASP E 203 OD1 89.0
REMARK 620 3 GLU E 204 OE1 92.2 89.7
REMARK 620 4 CAP E 477 O7 170.1 94.7 97.0
REMARK 620 5 CAP E 477 O3 87.1 176.1 90.6 89.2
REMARK 620 6 CAP E 477 O2 95.9 103.9 164.2 74.4 76.4
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 KCX F 201 OQ2
REMARK 620 2 ASP F 203 OD1 89.9
REMARK 620 3 GLU F 204 OE1 88.3 97.9
REMARK 620 4 CAP F 477 O3 80.9 170.6 84.1
REMARK 620 5 CAP F 477 O7 162.0 104.1 100.8 84.5
REMARK 620 6 CAP F 477 O2 90.4 103.1 159.0 75.0 75.5
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 KCX G 201 OQ2
REMARK 620 2 ASP G 203 OD1 97.6
REMARK 620 3 GLU G 204 OE1 94.4 95.0
REMARK 620 4 CAP G 477 O3 89.2 173.2 84.9
REMARK 620 5 CAP G 477 O2 97.7 103.9 155.8 74.5
REMARK 620 6 CAP G 477 O7 165.9 90.7 96.2 82.6 69.1
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 KCX H 201 OQ2
REMARK 620 2 ASP H 203 OD1 93.8
REMARK 620 3 GLU H 204 OE1 92.5 91.8
REMARK 620 4 CAP H 477 O7 165.9 94.0 99.0
REMARK 620 5 CAP H 477 O2 93.4 105.6 161.2 73.2
REMARK 620 6 CAP H 477 O3 85.7 178.5 86.9 86.8 75.7
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 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 476
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 A1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141
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: 1UZH RELATED DB: PDB
REMARK 900 A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO ENZYME
REMARK 900 RELATED ID: 1GK8 RELATED DB: PDB
REMARK 900 RUBISCO FROM CHLAMYDOMONAS REINHARDTII
REMARK 900 RELATED ID: 1UWA RELATED DB: PDB
REMARK 900 L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
REMARK 900 RELATED ID: 1IR2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5 -
REMARK 900 BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM GREEN ALGA,
REMARK 900 CHLAMYDOMONAS REINHARDTII COMPLEXED WITH 2-CARBOXYARABINITOL-1,5-
REMARK 900 BISPHOSPHATE ( 2-CABP)
REMARK 900 RELATED ID: 1UZD RELATED DB: PDB
REMARK 900 CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
REMARK 900 RELATED ID: 2V63 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RUBISCO FROM CHLAMYDOMONAS REINHARDTII WITH A
REMARK 900 LARGE-SUBUNIT V331A MUTATION
REMARK 900 RELATED ID: 2V67 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH A LARGE-
REMARK 900 SUBUNIT SUPRESSOR MUTATION T342I
REMARK 900 RELATED ID: 2V69 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH A LARGE-
REMARK 900 SUBUNIT MUTATION D473E
REMARK 900 RELATED ID: 2V6A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-
REMARK 900 SUBUNIT MUTATIONS V331A, 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.
REMARK 999 THE CHAINS I-P ARE ENCODED BY TWO GENES; RBCS 1, UNP
REMARK 999 P00873 AND RBCS 2, UNP P08475, THAT DIFFER IN
REMARK 999 POSITIONS 22, 47, 128, AND 132. JUDGING FROM THE
REMARK 999 ELECTRON DENSITY, THE TWO GENES ARE EXPRESSED AT
REMARK 999 APPROXIMATELY EQUAL LEVEL. SEQUENCE RBCS 1, UNP P00873
REMARK 999 HAS BEEN USED IN THIS CASE.
DBREF 2V68 A 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 B 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 C 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 D 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 E 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 F 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 G 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 H 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 2V68 I 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 J 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 K 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 L 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 M 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 N 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 O 1 140 UNP P00873 RBS1_CHLRE 46 185
DBREF 2V68 P 1 140 UNP P00873 RBS1_CHLRE 46 185
SEQADV 2V68 PRO A 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA A 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE A 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO B 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA B 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE B 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO C 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA C 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE C 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO D 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA D 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE D 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO E 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA E 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE E 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO F 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA F 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE F 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO G 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA G 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE G 342 UNP P00877 THR 342 ENGINEERED MUTATION
SEQADV 2V68 PRO H 46 UNP P00877 LEU 46 CONFLICT
SEQADV 2V68 ALA H 331 UNP P00877 VAL 331 ENGINEERED MUTATION
SEQADV 2V68 ILE H 342 UNP P00877 THR 342 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 ILE 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 ILE 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 ILE 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 ILE 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 ILE 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 ILE 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 ILE 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 ILE 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 2V68 HYP A 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP A 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX A 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC A 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC A 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP B 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP B 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX B 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC B 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC B 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP C 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP C 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX C 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC C 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC C 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP D 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP D 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX D 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC D 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC D 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP E 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP E 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX E 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC E 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC E 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP F 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP F 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX F 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC F 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC F 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP G 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP G 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX G 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC G 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC G 369 CYS S-METHYLCYSTEINE
MODRES 2V68 HYP H 104 PRO 4-HYDROXYPROLINE
MODRES 2V68 HYP H 151 PRO 4-HYDROXYPROLINE
MODRES 2V68 KCX H 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2V68 SMC H 256 CYS S-METHYLCYSTEINE
MODRES 2V68 SMC H 369 CYS S-METHYLCYSTEINE
MODRES 2V68 MME I 1 MET N-METHYL METHIONINE
MODRES 2V68 MME J 1 MET N-METHYL METHIONINE
MODRES 2V68 MME K 1 MET N-METHYL METHIONINE
MODRES 2V68 MME L 1 MET N-METHYL METHIONINE
MODRES 2V68 MME M 1 MET N-METHYL METHIONINE
MODRES 2V68 MME N 1 MET N-METHYL METHIONINE
MODRES 2V68 MME O 1 MET N-METHYL METHIONINE
MODRES 2V68 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 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 MG A 476 1
HET CAP A 477 21
HET EDO A1477 4
HET EDO A1481 4
HET EDO A1482 4
HET EDO A1483 4
HET EDO A1484 4
HET MG B 476 1
HET CAP B 477 21
HET EDO B1477 4
HET EDO B1479 4
HET EDO B1480 4
HET EDO B1481 4
HET MG C 476 1
HET CAP C 477 21
HET EDO C1477 4
HET EDO C1478 4
HET EDO C1480 4
HET EDO C1481 4
HET EDO C1482 4
HET MG D 476 1
HET CAP D 477 21
HET EDO D1477 4
HET EDO D1478 4
HET EDO D1480 4
HET EDO D1481 4
HET MG E 476 1
HET CAP E 477 21
HET EDO E1476 4
HET EDO E1478 4
HET EDO E1480 4
HET EDO F1479 4
HET MG F 476 1
HET CAP F 477 21
HET EDO F1480 4
HET EDO F1481 4
HET EDO F1482 4
HET EDO F1483 4
HET EDO F1484 4
HET MG G 476 1
HET CAP G 477 21
HET EDO G1476 4
HET EDO G1478 4
HET EDO G1480 4
HET MG H 476 1
HET CAP H 477 21
HET EDO H1476 4
HET EDO H1478 4
HET EDO H1480 4
HET EDO H1481 4
HET EDO H1482 4
HET EDO H1483 4
HET EDO I1141 4
HET EDO I1142 4
HET EDO J1141 4
HET EDO J1142 4
HET EDO K1141 4
HET EDO K1142 4
HET EDO L1141 4
HET EDO M1141 4
HET EDO N1141 4
HET EDO N1142 4
HET EDO O1141 4
HET EDO O1142 4
HET EDO P1141 4
HETNAM HYP 4-HYDROXYPROLINE
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM SMC S-METHYLCYSTEINE
HETNAM MME N-METHYL METHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HYP HYDROXYPROLINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 HYP 16(C5 H9 N O3)
FORMUL 1 KCX 8(C7 H14 N2 O4)
FORMUL 1 SMC 16(C4 H9 N O2 S)
FORMUL 9 MME 8(C6 H13 N O2 S)
FORMUL 17 MG 8(MG 2+)
FORMUL 18 CAP 8(C6 H14 O13 P2)
FORMUL 19 EDO 49(C2 H6 O2)
FORMUL 82 HOH *2276(H2 O)
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 SER A 112 GLY A 122 1 11
HELIX 6 6 ASN A 123 GLY A 126 5 4
HELIX 7 7 PRO A 141 LYS A 146 1 6
HELIX 8 8 GLY A 154 ASN A 163 1 10
HELIX 9 9 SER A 181 GLY A 195 1 15
HELIX 10 10 ARG A 213 GLY A 233 1 21
HELIX 11 11 THR A 246 ALA A 254 1 9
HELIX 12 12 TYR A 269 GLY A 288 1 20
HELIX 13 13 MET A 297 ARG A 303 1 7
HELIX 14 14 HIS A 310 GLY A 322 1 13
HELIX 15 15 GLU A 338 ASP A 351 1 14
HELIX 16 16 ARG A 358 GLY A 361 5 4
HELIX 17 17 HIS A 383 TRP A 385 5 3
HELIX 18 18 HIS A 386 GLY A 395 1 10
HELIX 19 19 GLY A 403 GLY A 408 1 6
HELIX 20 20 GLY A 412 GLU A 433 1 22
HELIX 21 21 ASP A 436 LYS A 450 1 15
HELIX 22 22 SER A 452 LYS A 463 1 12
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 SER B 112 VAL B 121 1 10
HELIX 28 28 ASN B 123 GLY B 126 5 4
HELIX 29 29 PRO B 141 LYS B 146 1 6
HELIX 30 30 GLY B 154 ASN B 163 1 10
HELIX 31 31 SER B 181 GLY B 195 1 15
HELIX 32 32 ARG B 213 GLY B 233 1 21
HELIX 33 33 THR B 246 ALA B 254 1 9
HELIX 34 34 TYR B 269 GLY B 288 1 20
HELIX 35 35 MET B 297 ARG B 303 1 7
HELIX 36 36 HIS B 310 GLY B 322 1 13
HELIX 37 37 GLU B 338 ASP B 351 1 14
HELIX 38 38 ARG B 358 GLY B 361 5 4
HELIX 39 39 HIS B 383 TRP B 385 5 3
HELIX 40 40 HIS B 386 GLY B 395 1 10
HELIX 41 41 GLY B 403 GLY B 408 1 6
HELIX 42 42 GLY B 412 GLU B 433 1 22
HELIX 43 43 ASP B 436 LYS B 450 1 15
HELIX 44 44 SER B 452 LYS B 463 1 12
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 SER C 112 GLY C 122 1 11
HELIX 50 50 ASN C 123 GLY C 126 5 4
HELIX 51 51 PRO C 141 LYS C 146 1 6
HELIX 52 52 GLY C 154 ASN C 163 1 10
HELIX 53 53 SER C 181 GLY C 195 1 15
HELIX 54 54 ARG C 213 GLY C 233 1 21
HELIX 55 55 THR C 246 ALA C 254 1 9
HELIX 56 56 GLY C 273 GLY C 288 1 16
HELIX 57 57 MET C 297 ARG C 303 1 7
HELIX 58 58 HIS C 310 GLY C 322 1 13
HELIX 59 59 GLU C 338 ASP C 351 1 14
HELIX 60 60 ARG C 358 GLY C 361 5 4
HELIX 61 61 HIS C 383 TRP C 385 5 3
HELIX 62 62 HIS C 386 GLY C 395 1 10
HELIX 63 63 GLY C 403 GLY C 408 1 6
HELIX 64 64 GLY C 412 GLU C 433 1 22
HELIX 65 65 ASP C 436 CYS C 449 1 14
HELIX 66 66 SER C 452 LYS C 463 1 12
HELIX 67 67 TYR D 20 TYR D 25 1 6
HELIX 68 68 PRO D 49 SER D 61 1 13
HELIX 69 69 VAL D 69 THR D 75 5 7
HELIX 70 70 SER D 76 LYS D 81 1 6
HELIX 71 71 SER D 112 GLY D 122 1 11
HELIX 72 72 ASN D 123 GLY D 126 5 4
HELIX 73 73 PRO D 141 LYS D 146 1 6
HELIX 74 74 GLY D 154 ASN D 163 1 10
HELIX 75 75 SER D 181 GLY D 195 1 15
HELIX 76 76 ARG D 213 GLY D 233 1 21
HELIX 77 77 THR D 246 ALA D 254 1 9
HELIX 78 78 TYR D 269 GLY D 288 1 20
HELIX 79 79 MET D 297 ARG D 303 1 7
HELIX 80 80 HIS D 310 GLY D 322 1 13
HELIX 81 81 GLU D 338 ASP D 351 1 14
HELIX 82 82 ARG D 358 GLY D 361 5 4
HELIX 83 83 HIS D 383 TRP D 385 5 3
HELIX 84 84 HIS D 386 GLY D 395 1 10
HELIX 85 85 GLY D 403 GLY D 408 1 6
HELIX 86 86 GLY D 412 GLY D 434 1 23
HELIX 87 87 ASP D 436 LYS D 463 1 28
HELIX 88 88 TYR E 20 TYR E 25 1 6
HELIX 89 89 PRO E 49 SER E 61 1 13
HELIX 90 90 VAL E 69 THR E 75 5 7
HELIX 91 91 SER E 76 LYS E 81 1 6
HELIX 92 92 SER E 112 GLY E 122 1 11
HELIX 93 93 ASN E 123 GLY E 126 5 4
HELIX 94 94 PRO E 141 LYS E 146 1 6
HELIX 95 95 GLY E 154 ASN E 163 1 10
HELIX 96 96 SER E 181 GLY E 195 1 15
HELIX 97 97 ARG E 213 GLY E 233 1 21
HELIX 98 98 THR E 246 ALA E 254 1 9
HELIX 99 99 TYR E 269 GLY E 288 1 20
HELIX 100 100 MET E 297 ARG E 303 1 7
HELIX 101 101 HIS E 310 GLY E 322 1 13
HELIX 102 102 GLU E 338 ASP E 351 1 14
HELIX 103 103 ARG E 358 GLY E 361 5 4
HELIX 104 104 HIS E 383 TRP E 385 5 3
HELIX 105 105 HIS E 386 GLY E 395 1 10
HELIX 106 106 GLY E 403 GLY E 408 1 6
HELIX 107 107 GLY E 412 GLU E 433 1 22
HELIX 108 108 ASP E 436 LYS E 463 1 28
HELIX 109 109 TYR F 20 TYR F 25 1 6
HELIX 110 110 PRO F 49 SER F 61 1 13
HELIX 111 111 VAL F 69 THR F 75 5 7
HELIX 112 112 SER F 76 LYS F 81 1 6
HELIX 113 113 SER F 112 GLY F 122 1 11
HELIX 114 114 ASN F 123 GLY F 126 5 4
HELIX 115 115 PRO F 141 LYS F 146 1 6
HELIX 116 116 GLY F 154 ASN F 163 1 10
HELIX 117 117 SER F 181 GLY F 195 1 15
HELIX 118 118 ARG F 213 GLY F 233 1 21
HELIX 119 119 THR F 246 ALA F 254 1 9
HELIX 120 120 TYR F 269 GLY F 288 1 20
HELIX 121 121 MET F 297 ARG F 303 1 7
HELIX 122 122 HIS F 310 GLY F 322 1 13
HELIX 123 123 GLU F 338 ASP F 351 1 14
HELIX 124 124 ARG F 358 GLY F 361 5 4
HELIX 125 125 HIS F 383 TRP F 385 5 3
HELIX 126 126 HIS F 386 GLY F 395 1 10
HELIX 127 127 GLY F 403 GLY F 408 1 6
HELIX 128 128 GLY F 412 GLU F 433 1 22
HELIX 129 129 ASP F 436 CYS F 449 1 14
HELIX 130 130 SER F 452 LYS F 463 1 12
HELIX 131 131 TYR G 20 TYR G 25 1 6
HELIX 132 132 PRO G 49 SER G 61 1 13
HELIX 133 133 VAL G 69 THR G 75 5 7
HELIX 134 134 SER G 76 LYS G 81 1 6
HELIX 135 135 SER G 112 GLY G 122 1 11
HELIX 136 136 ASN G 123 GLY G 126 5 4
HELIX 137 137 PRO G 141 LYS G 146 1 6
HELIX 138 138 GLY G 154 ASN G 163 1 10
HELIX 139 139 SER G 181 GLY G 195 1 15
HELIX 140 140 ARG G 213 GLY G 233 1 21
HELIX 141 141 THR G 246 ALA G 254 1 9
HELIX 142 142 TYR G 269 GLY G 288 1 20
HELIX 143 143 MET G 297 ARG G 303 1 7
HELIX 144 144 HIS G 310 GLY G 322 1 13
HELIX 145 145 GLU G 338 ASP G 351 1 14
HELIX 146 146 ARG G 358 GLY G 361 5 4
HELIX 147 147 HIS G 383 TRP G 385 5 3
HELIX 148 148 HIS G 386 GLY G 395 1 10
HELIX 149 149 GLY G 403 GLY G 408 1 6
HELIX 150 150 GLY G 412 GLU G 433 1 22
HELIX 151 151 ASP G 436 LYS G 463 1 28
HELIX 152 152 TYR H 20 TYR H 25 1 6
HELIX 153 153 PRO H 49 SER H 61 1 13
HELIX 154 154 VAL H 69 THR H 75 5 7
HELIX 155 155 SER H 76 LYS H 81 1 6
HELIX 156 156 SER H 112 GLY H 122 1 11
HELIX 157 157 ASN H 123 GLY H 126 5 4
HELIX 158 158 PRO H 141 LYS H 146 1 6
HELIX 159 159 GLY H 154 ASN H 163 1 10
HELIX 160 160 SER H 181 GLY H 195 1 15
HELIX 161 161 ARG H 213 GLY H 233 1 21
HELIX 162 162 THR H 246 ALA H 254 1 9
HELIX 163 163 TYR H 269 GLY H 288 1 20
HELIX 164 164 MET H 297 ARG H 303 1 7
HELIX 165 165 HIS H 310 GLY H 322 1 13
HELIX 166 166 GLU H 338 ASP H 351 1 14
HELIX 167 167 ARG H 358 GLY H 361 5 4
HELIX 168 168 HIS H 383 TRP H 385 5 3
HELIX 169 169 HIS H 386 GLY H 395 1 10
HELIX 170 170 GLY H 403 GLY H 408 1 6
HELIX 171 171 GLY H 412 GLU H 433 1 22
HELIX 172 172 ASP H 436 LYS H 463 1 28
HELIX 173 173 THR I 22 GLY I 37 1 16
HELIX 174 174 GLU I 46 ALA I 50 5 5
HELIX 175 175 ASN I 54 PHE I 60 5 7
HELIX 176 176 ASP I 85 PHE I 100 1 16
HELIX 177 177 PRO I 134 ARG I 138 5 5
HELIX 178 178 THR J 22 GLY J 37 1 16
HELIX 179 179 GLU J 46 ALA J 50 5 5
HELIX 180 180 ASN J 54 PHE J 60 5 7
HELIX 181 181 ASP J 85 PHE J 100 1 16
HELIX 182 182 PRO J 134 ARG J 138 5 5
HELIX 183 183 THR K 22 ASN K 36 1 15
HELIX 184 184 GLU K 46 ALA K 50 5 5
HELIX 185 185 ASN K 54 PHE K 60 5 7
HELIX 186 186 ASP K 85 PHE K 100 1 16
HELIX 187 187 PRO K 134 ARG K 138 5 5
HELIX 188 188 THR L 22 ASN L 36 1 15
HELIX 189 189 GLU L 46 ALA L 50 5 5
HELIX 190 190 ASN L 54 PHE L 60 5 7
HELIX 191 191 ASP L 85 PHE L 100 1 16
HELIX 192 192 PRO L 134 ARG L 138 5 5
HELIX 193 193 THR M 22 ASN M 36 1 15
HELIX 194 194 GLU M 46 ALA M 50 5 5
HELIX 195 195 ASN M 54 PHE M 60 5 7
HELIX 196 196 ASP M 85 PHE M 100 1 16
HELIX 197 197 PRO M 134 ARG M 138 5 5
HELIX 198 198 THR N 22 GLY N 37 1 16
HELIX 199 199 GLU N 46 ALA N 50 5 5
HELIX 200 200 ASN N 54 PHE N 60 5 7
HELIX 201 201 ASP N 85 PHE N 100 1 16
HELIX 202 202 PRO N 134 ARG N 138 5 5
HELIX 203 203 THR O 22 GLY O 37 1 16
HELIX 204 204 GLU O 46 ALA O 50 5 5
HELIX 205 205 ASN O 54 PHE O 60 5 7
HELIX 206 206 ASP O 85 PHE O 100 1 16
HELIX 207 207 PRO O 134 ARG O 138 5 5
HELIX 208 208 THR P 22 GLY P 37 1 16
HELIX 209 209 GLU P 46 ALA P 50 5 5
HELIX 210 210 ASN P 54 PHE P 60 5 7
HELIX 211 211 ASP P 85 PHE P 100 1 16
HELIX 212 212 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 ALA A 102 -1 O ILE A 98 N GLU A 88
SHEET 3 AA 5 LEU A 37 PRO A 44 -1 O ALA A 38 N VAL A 101
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 7 LEU A 169 GLY A 171 0
SHEET 2 AB 7 CYS A 399 GLN A 401 1 O LEU A 400 N GLY A 171
SHEET 3 AB 7 MET A 375 SER A 379 1 O PRO A 376 N CYS A 399
SHEET 4 AB 7 HIS A 325 HIS A 327 1 O LEU A 326 N VAL A 377
SHEET 5 AB 7 LEU A 290 HIS A 294 1 O ILE A 293 N HIS A 327
SHEET 6 AB 7 ILE A 264 ASP A 268 1 O ILE A 265 N HIS A 292
SHEET 7 AB 7 LEU A 240 ASN A 241 1 O LEU A 240 N MET A 266
SHEET 1 BA 5 ARG B 83 PRO B 89 0
SHEET 2 BA 5 TYR B 97 ALA B 102 -1 O ILE B 98 N GLU B 88
SHEET 3 BA 5 LEU B 37 PRO B 44 -1 O ALA B 38 N VAL B 101
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 7 LEU B 169 GLY B 171 0
SHEET 2 BB 7 CYS B 399 GLN B 401 1 O LEU B 400 N GLY B 171
SHEET 3 BB 7 MET B 375 SER B 379 1 O PRO B 376 N CYS B 399
SHEET 4 BB 7 HIS B 325 HIS B 327 1 O LEU B 326 N VAL B 377
SHEET 5 BB 7 LEU B 290 HIS B 294 1 O ILE B 293 N HIS B 327
SHEET 6 BB 7 ILE B 264 ASP B 268 1 O ILE B 265 N HIS B 292
SHEET 7 BB 7 LEU B 240 ASN B 241 1 O LEU B 240 N MET B 266
SHEET 1 CA 5 ARG C 83 PRO C 89 0
SHEET 2 CA 5 TYR C 97 ALA C 102 -1 O ILE C 98 N GLU C 88
SHEET 3 CA 5 LEU C 37 PRO C 44 -1 O ALA C 38 N VAL C 101
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 7 LEU C 169 GLY C 171 0
SHEET 2 CB 7 CYS C 399 GLN C 401 1 O LEU C 400 N GLY C 171
SHEET 3 CB 7 MET C 375 SER C 379 1 O PRO C 376 N CYS C 399
SHEET 4 CB 7 HIS C 325 HIS C 327 1 O LEU C 326 N VAL C 377
SHEET 5 CB 7 LEU C 290 HIS C 294 1 O ILE C 293 N HIS C 327
SHEET 6 CB 7 ILE C 264 ASP C 268 1 O ILE C 265 N HIS C 292
SHEET 7 CB 7 LEU C 240 ASN C 241 1 O LEU C 240 N MET C 266
SHEET 1 DA 5 ARG D 83 PRO D 89 0
SHEET 2 DA 5 TYR D 97 ALA D 102 -1 O ILE D 98 N GLU D 88
SHEET 3 DA 5 LEU D 37 PRO D 44 -1 O ALA D 38 N VAL D 101
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 7 LEU D 169 GLY D 171 0
SHEET 2 DB 7 CYS D 399 GLN D 401 1 O LEU D 400 N GLY D 171
SHEET 3 DB 7 MET D 375 SER D 379 1 O PRO D 376 N CYS D 399
SHEET 4 DB 7 HIS D 325 HIS D 327 1 O LEU D 326 N VAL D 377
SHEET 5 DB 7 LEU D 290 HIS D 294 1 O ILE D 293 N HIS D 327
SHEET 6 DB 7 ILE D 264 ASP D 268 1 O ILE D 265 N HIS D 292
SHEET 7 DB 7 LEU D 240 ASN D 241 1 O LEU D 240 N MET D 266
SHEET 1 EA 5 ARG E 83 PRO E 89 0
SHEET 2 EA 5 TYR E 97 ALA E 102 -1 O ILE E 98 N GLU E 88
SHEET 3 EA 5 LEU E 37 PRO E 44 -1 O ALA E 38 N VAL E 101
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 7 LEU E 169 GLY E 171 0
SHEET 2 EB 7 CYS E 399 GLN E 401 1 O LEU E 400 N GLY E 171
SHEET 3 EB 7 MET E 375 SER E 379 1 O PRO E 376 N CYS E 399
SHEET 4 EB 7 HIS E 325 HIS E 327 1 O LEU E 326 N VAL E 377
SHEET 5 EB 7 LEU E 290 HIS E 294 1 O ILE E 293 N HIS E 327
SHEET 6 EB 7 ILE E 264 ASP E 268 1 O ILE E 265 N HIS E 292
SHEET 7 EB 7 LEU E 240 ASN E 241 1 O LEU E 240 N MET E 266
SHEET 1 FA 5 ARG F 83 PRO F 89 0
SHEET 2 FA 5 TYR F 97 ALA F 102 -1 O ILE F 98 N GLU F 88
SHEET 3 FA 5 LEU F 37 PRO F 44 -1 O ALA F 38 N VAL F 101
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 7 LEU F 169 GLY F 171 0
SHEET 2 FB 7 CYS F 399 GLN F 401 1 O LEU F 400 N GLY F 171
SHEET 3 FB 7 MET F 375 SER F 379 1 O PRO F 376 N CYS F 399
SHEET 4 FB 7 HIS F 325 HIS F 327 1 O LEU F 326 N VAL F 377
SHEET 5 FB 7 LEU F 290 HIS F 294 1 O ILE F 293 N HIS F 327
SHEET 6 FB 7 ILE F 264 ASP F 268 1 O ILE F 265 N HIS F 292
SHEET 7 FB 7 LEU F 240 ASN F 241 1 O LEU F 240 N MET F 266
SHEET 1 GA 5 ARG G 83 PRO G 89 0
SHEET 2 GA 5 TYR G 97 ALA G 102 -1 O ILE G 98 N GLU G 88
SHEET 3 GA 5 LEU G 37 PRO G 44 -1 O ALA G 38 N VAL G 101
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 7 LEU G 169 GLY G 171 0
SHEET 2 GB 7 CYS G 399 GLN G 401 1 O LEU G 400 N GLY G 171
SHEET 3 GB 7 MET G 375 SER G 379 1 O PRO G 376 N CYS G 399
SHEET 4 GB 7 HIS G 325 HIS G 327 1 O LEU G 326 N VAL G 377
SHEET 5 GB 7 LEU G 290 HIS G 294 1 O ILE G 293 N HIS G 327
SHEET 6 GB 7 ILE G 264 ASP G 268 1 O ILE G 265 N HIS G 292
SHEET 7 GB 7 LEU G 240 ASN G 241 1 O LEU G 240 N MET G 266
SHEET 1 HA 5 ARG H 83 PRO H 89 0
SHEET 2 HA 5 TYR H 97 ALA H 102 -1 O ILE H 98 N GLU H 88
SHEET 3 HA 5 LEU H 37 PRO H 44 -1 O ALA H 38 N VAL H 101
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 7 LEU H 169 GLY H 171 0
SHEET 2 HB 7 CYS H 399 GLN H 401 1 O LEU H 400 N GLY H 171
SHEET 3 HB 7 MET H 375 SER H 379 1 O PRO H 376 N CYS H 399
SHEET 4 HB 7 HIS H 325 HIS H 327 1 O LEU H 326 N VAL H 377
SHEET 5 HB 7 LEU H 290 HIS H 294 1 O ILE H 293 N HIS H 327
SHEET 6 HB 7 ILE H 264 ASP H 268 1 O ILE H 265 N HIS H 292
SHEET 7 HB 7 LEU H 240 ASN H 241 1 O LEU H 240 N MET H 266
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 2.10
SSBOND 2 CYS C 247 CYS D 247 1555 1555 2.07
SSBOND 3 CYS E 247 CYS F 247 1555 1555 2.09
SSBOND 4 CYS G 247 CYS H 247 1555 1555 2.09
LINK C TYR A 103 N HYP A 104 1555 1555 1.34
LINK C HYP A 104 N ILE A 105 1555 1555 1.33
LINK C GLY A 150 N HYP A 151 1555 1555 1.34
LINK C HYP A 151 N PRO A 152 1555 1555 1.36
LINK C THR A 200 N KCX A 201 1555 1555 1.33
LINK C KCX A 201 N ASP A 202 1555 1555 1.34
LINK C VAL A 255 N SMC A 256 1555 1555 1.34
LINK C SMC A 256 N ALA A 257 1555 1555 1.33
LINK C TRP A 368 N SMC A 369 1555 1555 1.34
LINK C SMC A 369 N SER A 370 1555 1555 1.33
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 1.35
LINK C THR B 200 N KCX B 201 1555 1555 1.33
LINK C KCX B 201 N ASP B 202 1555 1555 1.34
LINK C VAL B 255 N SMC B 256 1555 1555 1.33
LINK C SMC B 256 N ALA B 257 1555 1555 1.34
LINK C TRP B 368 N SMC B 369 1555 1555 1.34
LINK C SMC B 369 N SER B 370 1555 1555 1.33
LINK C TYR C 103 N HYP C 104 1555 1555 1.35
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 1.35
LINK C THR C 200 N KCX C 201 1555 1555 1.34
LINK C KCX C 201 N ASP C 202 1555 1555 1.33
LINK C VAL C 255 N SMC C 256 1555 1555 1.33
LINK C SMC C 256 N ALA C 257 1555 1555 1.33
LINK C TRP C 368 N SMC C 369 1555 1555 1.33
LINK C SMC C 369 N SER C 370 1555 1555 1.34
LINK C TYR D 103 N HYP D 104 1555 1555 1.35
LINK C HYP D 104 N ILE D 105 1555 1555 1.33
LINK C GLY D 150 N HYP D 151 1555 1555 1.35
LINK C HYP D 151 N PRO D 152 1555 1555 1.35
LINK C THR D 200 N KCX D 201 1555 1555 1.33
LINK C KCX D 201 N ASP D 202 1555 1555 1.33
LINK C VAL D 255 N SMC D 256 1555 1555 1.34
LINK C SMC D 256 N ALA D 257 1555 1555 1.33
LINK C TRP D 368 N SMC D 369 1555 1555 1.34
LINK C SMC D 369 N SER D 370 1555 1555 1.33
LINK C TYR E 103 N HYP E 104 1555 1555 1.35
LINK C HYP E 104 N ILE E 105 1555 1555 1.34
LINK C GLY E 150 N HYP E 151 1555 1555 1.34
LINK C HYP E 151 N PRO E 152 1555 1555 1.35
LINK C THR E 200 N KCX E 201 1555 1555 1.34
LINK C KCX E 201 N ASP E 202 1555 1555 1.34
LINK C VAL E 255 N SMC E 256 1555 1555 1.33
LINK C SMC E 256 N ALA E 257 1555 1555 1.33
LINK C TRP E 368 N SMC E 369 1555 1555 1.34
LINK C SMC E 369 N SER E 370 1555 1555 1.33
LINK C TYR F 103 N HYP F 104 1555 1555 1.34
LINK C HYP F 104 N ILE F 105 1555 1555 1.33
LINK C GLY F 150 N HYP F 151 1555 1555 1.34
LINK C HYP F 151 N PRO F 152 1555 1555 1.35
LINK C THR F 200 N KCX F 201 1555 1555 1.33
LINK C KCX F 201 N ASP F 202 1555 1555 1.33
LINK C VAL F 255 N SMC F 256 1555 1555 1.33
LINK C SMC F 256 N ALA F 257 1555 1555 1.34
LINK C TRP F 368 N SMC F 369 1555 1555 1.34
LINK C SMC F 369 N SER F 370 1555 1555 1.34
LINK C TYR G 103 N HYP G 104 1555 1555 1.35
LINK C HYP G 104 N ILE G 105 1555 1555 1.34
LINK C GLY G 150 N HYP G 151 1555 1555 1.35
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 1.34
LINK C VAL G 255 N SMC G 256 1555 1555 1.34
LINK C SMC G 256 N ALA G 257 1555 1555 1.34
LINK C TRP G 368 N SMC G 369 1555 1555 1.34
LINK C SMC G 369 N SER G 370 1555 1555 1.34
LINK 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 1.36
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 1.32
LINK C SMC H 256 N ALA H 257 1555 1555 1.34
LINK C TRP H 368 N SMC H 369 1555 1555 1.33
LINK C SMC H 369 N SER H 370 1555 1555 1.34
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
LINK OQ2 KCX A 201 MG MG A 476 1555 1555 2.06
LINK OD1 ASP A 203 MG MG A 476 1555 1555 1.93
LINK OE1 GLU A 204 MG MG A 476 1555 1555 2.01
LINK MG MG A 476 O2 CAP A 477 1555 1555 2.24
LINK MG MG A 476 O3 CAP A 477 1555 1555 2.22
LINK MG MG A 476 O7 CAP A 477 1555 1555 2.22
LINK OQ2 KCX B 201 MG MG B 476 1555 1555 2.02
LINK OD1 ASP B 203 MG MG B 476 1555 1555 1.99
LINK OE1 GLU B 204 MG MG B 476 1555 1555 2.08
LINK MG MG B 476 O2 CAP B 477 1555 1555 2.16
LINK MG MG B 476 O3 CAP B 477 1555 1555 2.23
LINK MG MG B 476 O7 CAP B 477 1555 1555 2.27
LINK OQ2 KCX C 201 MG MG C 476 1555 1555 1.93
LINK OD1 ASP C 203 MG MG C 476 1555 1555 1.91
LINK OE1 GLU C 204 MG MG C 476 1555 1555 2.07
LINK MG MG C 476 O3 CAP C 477 1555 1555 2.21
LINK MG MG C 476 O2 CAP C 477 1555 1555 2.16
LINK MG MG C 476 O7 CAP C 477 1555 1555 2.35
LINK OQ2 KCX D 201 MG MG D 476 1555 1555 1.98
LINK OD1 ASP D 203 MG MG D 476 1555 1555 2.01
LINK OE1 GLU D 204 MG MG D 476 1555 1555 2.13
LINK MG MG D 476 O3 CAP D 477 1555 1555 2.11
LINK MG MG D 476 O7 CAP D 477 1555 1555 2.18
LINK MG MG D 476 O2 CAP D 477 1555 1555 2.31
LINK OQ2 KCX E 201 MG MG E 476 1555 1555 2.12
LINK OD1 ASP E 203 MG MG E 476 1555 1555 1.99
LINK OE1 GLU E 204 MG MG E 476 1555 1555 2.05
LINK MG MG E 476 O7 CAP E 477 1555 1555 2.29
LINK MG MG E 476 O3 CAP E 477 1555 1555 2.14
LINK MG MG E 476 O2 CAP E 477 1555 1555 2.20
LINK OQ2 KCX F 201 MG MG F 476 1555 1555 2.11
LINK OD1 ASP F 203 MG MG F 476 1555 1555 1.89
LINK OE1 GLU F 204 MG MG F 476 1555 1555 2.05
LINK MG MG F 476 O3 CAP F 477 1555 1555 2.19
LINK MG MG F 476 O7 CAP F 477 1555 1555 2.10
LINK MG MG F 476 O2 CAP F 477 1555 1555 2.23
LINK OQ2 KCX G 201 MG MG G 476 1555 1555 1.95
LINK OD1 ASP G 203 MG MG G 476 1555 1555 1.97
LINK OE1 GLU G 204 MG MG G 476 1555 1555 2.07
LINK MG MG G 476 O3 CAP G 477 1555 1555 2.18
LINK MG MG G 476 O2 CAP G 477 1555 1555 2.24
LINK MG MG G 476 O7 CAP G 477 1555 1555 2.30
LINK OQ2 KCX H 201 MG MG H 476 1555 1555 2.03
LINK OD1 ASP H 203 MG MG H 476 1555 1555 1.94
LINK OE1 GLU H 204 MG MG H 476 1555 1555 1.97
LINK MG MG H 476 O7 CAP H 477 1555 1555 2.20
LINK MG MG H 476 O2 CAP H 477 1555 1555 2.28
LINK MG MG H 476 O3 CAP H 477 1555 1555 2.23
CISPEP 1 LYS A 175 PRO A 176 0 -0.85
CISPEP 2 LYS B 175 PRO B 176 0 -1.92
CISPEP 3 LYS C 175 PRO C 176 0 0.16
CISPEP 4 LYS D 175 PRO D 176 0 -2.66
CISPEP 5 LYS E 175 PRO E 176 0 -2.09
CISPEP 6 LYS F 175 PRO F 176 0 0.35
CISPEP 7 LYS G 175 PRO G 176 0 -1.70
CISPEP 8 LYS H 175 PRO H 176 0 0.79
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 476 HOH A2157 HOH A2192 HOH A2204
SITE 6 AC1 28 HOH A2231 HOH A2232 HOH A2233 HOH A2234
SITE 7 AC1 28 GLU B 60 THR B 65 TRP B 66 ASN B 123
SITE 1 AC2 5 LYS A 177 KCX A 201 ASP A 203 GLU A 204
SITE 2 AC2 5 CAP A 477
SITE 1 AC3 30 GLU A 60 THR A 65 TRP A 66 ASN A 123
SITE 2 AC3 30 HOH A2028 THR B 173 LYS B 175 LYS B 177
SITE 3 AC3 30 KCX B 201 ASP B 203 GLU B 204 HIS B 294
SITE 4 AC3 30 ARG B 295 HIS B 327 LYS B 334 LEU B 335
SITE 5 AC3 30 SER B 379 GLY B 380 GLY B 381 GLY B 403
SITE 6 AC3 30 GLY B 404 MG B 476 HOH B2086 HOH B2088
SITE 7 AC3 30 HOH B2133 HOH B2208 HOH B2209 HOH B2210
SITE 8 AC3 30 HOH B2211 HOH B2212
SITE 1 AC4 4 KCX B 201 ASP B 203 GLU B 204 CAP B 477
SITE 1 AC5 29 THR C 173 LYS C 175 LYS C 177 KCX C 201
SITE 2 AC5 29 ASP C 203 GLU C 204 HIS C 294 ARG C 295
SITE 3 AC5 29 HIS C 327 LYS C 334 LEU C 335 SER C 379
SITE 4 AC5 29 GLY C 380 GLY C 381 GLY C 403 GLY C 404
SITE 5 AC5 29 MG C 476 HOH C2099 HOH C2100 HOH C2154
SITE 6 AC5 29 HOH C2225 HOH C2226 HOH C2227 HOH C2228
SITE 7 AC5 29 GLU D 60 THR D 65 TRP D 66 ASN D 123
SITE 8 AC5 29 HOH D2066
SITE 1 AC6 4 KCX C 201 ASP C 203 GLU C 204 CAP C 477
SITE 1 AC7 28 GLU C 60 THR C 65 TRP C 66 ASN C 123
SITE 2 AC7 28 THR D 173 LYS D 175 LYS D 177 KCX D 201
SITE 3 AC7 28 ASP D 203 GLU D 204 HIS D 294 ARG D 295
SITE 4 AC7 28 HIS D 327 LYS D 334 LEU D 335 SER D 379
SITE 5 AC7 28 GLY D 380 GLY D 381 GLY D 403 GLY D 404
SITE 6 AC7 28 MG D 476 HOH D2142 HOH D2172 HOH D2181
SITE 7 AC7 28 HOH D2205 HOH D2206 HOH D2207 HOH D2208
SITE 1 AC8 4 KCX D 201 ASP D 203 GLU D 204 CAP D 477
SITE 1 AC9 28 THR E 173 LYS E 175 LYS E 177 KCX E 201
SITE 2 AC9 28 ASP E 203 GLU E 204 HIS E 294 ARG E 295
SITE 3 AC9 28 HIS E 327 LYS E 334 LEU E 335 SER E 379
SITE 4 AC9 28 GLY E 380 GLY E 381 GLY E 403 GLY E 404
SITE 5 AC9 28 MG E 476 HOH E2146 HOH E2179 HOH E2220
SITE 6 AC9 28 HOH E2221 HOH E2222 HOH E2223 HOH E2224
SITE 7 AC9 28 GLU F 60 THR F 65 TRP F 66 ASN F 123
SITE 1 BC1 4 KCX E 201 ASP E 203 GLU E 204 CAP E 477
SITE 1 BC2 29 GLU E 60 THR E 65 TRP E 66 ASN E 123
SITE 2 BC2 29 HOH E2063 THR F 173 LYS F 175 LYS F 177
SITE 3 BC2 29 KCX F 201 ASP F 203 GLU F 204 HIS F 294
SITE 4 BC2 29 ARG F 295 HIS F 327 LYS F 334 LEU F 335
SITE 5 BC2 29 SER F 379 GLY F 380 GLY F 381 GLY F 403
SITE 6 BC2 29 GLY F 404 MG F 476 HOH F2088 HOH F2205
SITE 7 BC2 29 HOH F2206 HOH F2207 HOH F2208 HOH F2209
SITE 8 BC2 29 HOH F2210
SITE 1 BC3 5 LYS F 177 KCX F 201 ASP F 203 GLU F 204
SITE 2 BC3 5 CAP F 477
SITE 1 BC4 30 THR G 173 LYS G 175 LYS G 177 KCX G 201
SITE 2 BC4 30 ASP G 203 GLU G 204 HIS G 294 ARG G 295
SITE 3 BC4 30 HIS G 327 LYS G 334 LEU G 335 SER G 379
SITE 4 BC4 30 GLY G 380 GLY G 381 GLY G 403 GLY G 404
SITE 5 BC4 30 MG G 476 HOH G2085 HOH G2142 HOH G2181
SITE 6 BC4 30 HOH G2217 HOH G2218 HOH G2219 GLU H 60
SITE 7 BC4 30 THR H 65 TRP H 66 ASN H 123 HOH H2025
SITE 8 BC4 30 HOH H2027 HOH H2067
SITE 1 BC5 4 KCX G 201 ASP G 203 GLU G 204 CAP G 477
SITE 1 BC6 28 GLU G 60 THR G 65 TRP G 66 ASN G 123
SITE 2 BC6 28 HOH G2058 THR H 173 LYS H 175 LYS H 177
SITE 3 BC6 28 KCX H 201 ASP H 203 GLU H 204 HIS H 294
SITE 4 BC6 28 ARG H 295 HIS H 327 LYS H 334 LEU H 335
SITE 5 BC6 28 SER H 379 GLY H 380 GLY H 381 GLY H 403
SITE 6 BC6 28 GLY H 404 MG H 476 HOH H2183 HOH H2195
SITE 7 BC6 28 HOH H2227 HOH H2228 HOH H2229 HOH H2230
SITE 1 BC7 5 LYS H 177 KCX H 201 ASP H 203 GLU H 204
SITE 2 BC7 5 CAP H 477
SITE 1 BC8 6 LYS A 466 PHE A 467 GLU A 468 PHE A 469
SITE 2 BC8 6 HOH A2237 HOH B2213
SITE 1 BC9 6 ARG A 295 SER A 328 GLY A 329 GLU A 336
SITE 2 BC9 6 GLY A 337 PHE A 345
SITE 1 CC1 8 LYS A 18 THR A 65 TRP A 66 THR A 67
SITE 2 CC1 8 THR A 68 EDO A1481 HOH A2011 HOH A2235
SITE 1 CC2 8 TYR A 24 THR A 68 VAL A 69 ASP A 72
SITE 2 CC2 8 EDO A1483 HOH A2035 HOH A2235 HOH A2236
SITE 1 CC3 3 TYR A 20 GLU A 52 HOH B2216
SITE 1 CC4 7 TYR B 24 THR B 68 VAL B 69 ASP B 72
SITE 2 CC4 7 HOH B2027 HOH B2032 HOH B2214
SITE 1 CC5 5 LYS B 466 PHE B 467 GLU B 468 PHE B 469
SITE 2 CC5 5 HOH B2216
SITE 1 CC6 3 TYR B 20 GLU B 52 HOH B2213
SITE 1 CC7 7 LYS B 18 THR B 65 TRP B 66 THR B 67
SITE 2 CC7 7 THR B 68 HOH B2214 HOH B2215
SITE 1 CC8 1 GLU C 52
SITE 1 CC9 7 LYS C 18 THR C 65 TRP C 66 THR C 67
SITE 2 CC9 7 THR C 68 HOH C2030 HOH C2230
SITE 1 DC1 8 TYR C 24 GLY C 64 THR C 68 VAL C 69
SITE 2 DC1 8 ASP C 72 HOH C2030 HOH C2231 HOH C2232
SITE 1 DC2 5 LYS C 466 PHE C 467 GLU C 468 PHE C 469
SITE 2 DC2 5 HOH C2229
SITE 1 DC3 5 GLU C 336 GLY C 337 ASP C 473 HOH C2165
SITE 2 DC3 5 HOH C2233
SITE 1 DC4 7 TYR D 24 THR D 68 VAL D 69 ASP D 72
SITE 2 DC4 7 EDO D1480 HOH D2031 HOH D2211
SITE 1 DC5 5 LYS D 466 PHE D 467 GLU D 468 PHE D 469
SITE 2 DC5 5 HOH D2209
SITE 1 DC6 9 GLY D 16 LYS D 18 THR D 65 TRP D 66
SITE 2 DC6 9 THR D 67 THR D 68 EDO D1477 HOH D2210
SITE 3 DC6 9 HOH D2211
SITE 1 DC7 2 HOH C2229 GLU D 52
SITE 1 DC8 8 TYR E 24 THR E 68 VAL E 69 ASP E 72
SITE 2 DC8 8 LEU E 77 HOH E2031 HOH E2035 HOH E2225
SITE 1 DC9 7 LYS E 18 THR E 65 TRP E 66 THR E 67
SITE 2 DC9 7 THR E 68 HOH E2009 HOH E2225
SITE 1 EC1 1 GLU E 52
SITE 1 EC2 8 TYR F 24 THR F 68 VAL F 69 ASP F 72
SITE 2 EC2 8 LEU F 77 HOH F2027 HOH F2029 HOH F2033
SITE 1 EC3 2 TYR F 20 GLU F 52
SITE 1 EC4 6 ARG F 295 HIS F 298 PHE F 311 SER F 328
SITE 2 EC4 6 GLU F 336 PHE F 345
SITE 1 EC5 4 LYS F 466 PHE F 467 GLU F 468 PHE F 469
SITE 1 EC6 9 GLY F 16 VAL F 17 LYS F 18 THR F 65
SITE 2 EC6 9 TRP F 66 THR F 67 THR F 68 HOH F2011
SITE 3 EC6 9 HOH F2027
SITE 1 EC7 7 TYR G 24 THR G 68 VAL G 69 ASP G 72
SITE 2 EC7 7 HOH G2025 HOH G2027 HOH G2220
SITE 1 EC8 6 LYS G 18 THR G 65 TRP G 66 THR G 67
SITE 2 EC8 6 THR G 68 HOH G2220
SITE 1 EC9 5 LYS G 466 PHE G 467 GLU G 468 PHE G 469
SITE 2 EC9 5 HOH G2221
SITE 1 FC1 8 TYR H 24 THR H 68 VAL H 69 ASP H 72
SITE 2 FC1 8 EDO H1482 HOH H2033 HOH H2231 HOH H2232
SITE 1 FC2 5 LYS H 466 PHE H 467 GLU H 468 PHE H 469
SITE 2 FC2 5 EDO H1483
SITE 1 FC3 3 HOH G2221 TYR H 20 GLU H 52
SITE 1 FC4 5 ARG H 295 SER H 328 GLY H 329 GLU H 336
SITE 2 FC4 5 PHE H 345
SITE 1 FC5 9 GLY H 16 LYS H 18 THR H 65 TRP H 66
SITE 2 FC5 9 THR H 67 THR H 68 EDO H1476 HOH H2007
SITE 3 FC5 9 HOH H2231
SITE 1 FC6 3 PHE H 469 EDO H1478 HOH H2234
SITE 1 FC7 7 TYR C 226 LYS C 227 ALA C 230 LYS I 49
SITE 2 FC7 7 GLU I 55 HOH I2057 HOH I2058
SITE 1 FC8 6 GLY I 37 ILE I 39 GLY I 82 CYS I 83
SITE 2 FC8 6 ARG I 84 HOH I2017
SITE 1 FC9 6 TYR H 226 LYS H 227 HOH H2113 LYS J 49
SITE 2 FC9 6 GLU J 55 HOH J2031
SITE 1 GC1 5 GLY J 37 TRP J 38 PHE J 81 GLY J 82
SITE 2 GC1 5 CYS J 83
SITE 1 GC2 6 GLY K 37 TRP K 38 ILE K 39 PHE K 81
SITE 2 GC2 6 GLY K 82 CYS K 83
SITE 1 GC3 6 TYR E 226 HOH E2113 LYS K 49 GLU K 55
SITE 2 GC3 6 HOH K2034 HOH K2036
SITE 1 GC4 5 TYR B 226 ALA B 230 HOH B2111 LYS L 49
SITE 2 GC4 5 GLU L 55
SITE 1 GC5 5 TYR G 226 LYS G 227 LYS M 49 GLU M 55
SITE 2 GC5 5 SER M 56
SITE 1 GC6 2 ILE N 39 GLY N 82
SITE 1 GC7 4 LYS N 49 GLU N 55 ASP N 69 HOH N2031
SITE 1 GC8 5 TYR A 226 HOH A2120 LYS O 49 GLU O 55
SITE 2 GC8 5 HOH O2030
SITE 1 GC9 6 GLY O 37 TRP O 38 ILE O 39 PHE O 81
SITE 2 GC9 6 GLY O 82 CYS O 83
SITE 1 HC1 5 GLY E 10 GLY P 37 TRP P 38 ILE P 39
SITE 2 HC1 5 GLY P 82
CRYST1 120.421 178.236 122.758 90.00 117.72 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 0.008304 0.000000 0.004363 0.00000
SCALE2 0.000000 0.005611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009202 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.599000 0.765800 0.233900 -93.34000 1
MTRIX2 2 0.766100 -0.633100 0.111000 145.00000 1
MTRIX3 2 0.233100 0.112700 -0.965900 163.70000 1
MTRIX1 3 0.092550 -0.771000 -0.630100 101.40000 1
MTRIX2 3 0.292500 0.626000 -0.722900 99.72000 1
MTRIX3 3 0.095180 -0.117400 0.283400 90.63000 1
MTRIX1 4 -0.682000 0.488000 0.544700 -122.10000 1
MTRIX2 4 0.487500 -0.251800 0.836000 44.69000 1
MTRIX3 4 0.545200 0.835700 -0.066160 31.28000 1
MTRIX1 5 -0.818300 -0.476800 0.321000 -23.45000 1
MTRIX2 5 -0.477100 0.252100 -0.841900 126.30000 1
MTRIX3 5 0.320500 -0.842100 -0.433800 201.20000 1
MTRIX1 6 -0.780800 -0.290900 -0.552900 36.42000 1
MTRIX2 6 -0.287300 -0.618800 0.731100 69.41000 1
MTRIX3 6 -0.554800 0.729700 0.399600 -21.71000 1
MTRIX1 7 0.088920 0.293300 0.951900 -124.80000 1
MTRIX2 7 -0.771100 0.625200 -0.120700 26.83000 1
MTRIX3 7 -0.630500 -0.723200 0.281800 110.60000 1
MTRIX1 8 0.500000 -0.011880 -0.865900 65.28000 1
MTRIX2 8 -0.011420 -0.999900 0.007126 169.60000 1
MTRIX3 8 -0.865900 0.006323 -0.500100 110.80000 1
MTRIX1 9 0.596600 0.766900 0.236500 -93.66000 1
MTRIX2 9 0.768200 -0.631000 0.108000 145.20000 1
MTRIX3 9 0.232100 0.117300 -0.965600 163.30000 1
MTRIX1 10 0.095440 -0.770300 -0.630500 101.40000 1
MTRIX2 10 0.287200 0.627800 -0.723500 99.69000 1
MTRIX3 10 0.953100 -0.112000 0.281100 90.50000 1
MTRIX1 11 -0.680600 0.492400 0.542500 -122.20000 1
MTRIX2 11 0.491300 -0.242400 0.836500 43.92000 1
MTRIX3 11 0.543400 0.835900 -0.076900 32.40000 1
MTRIX1 12 -0.815700 -0.477800 0.326200 -23.94000 1
MTRIX2 12 -0.480700 0.246100 -0.841700 126.80000 1
MTRIX3 12 0.321800 -0.843300 -0.430400 200.90000 1
MTRIX1 13 -0.780800 -0.291600 -0.552600 36.39000 1
MTRIX2 13 -0.282900 -0.623500 0.728900 69.98000 1
MTRIX3 13 -0.557100 0.725400 0.404300 -21.90000 1
MTRIX1 14 0.088380 0.291500 0.952500 -124.80000 1
MTRIX2 14 -0.773900 0.622200 -0.118600 26.83000 1
MTRIX3 14 -0.627200 -0.726600 0.280600 110.90000 1
MTRIX1 15 0.499900 -0.011290 -0.866000 65.25000 1
MTRIX2 15 -0.010380 -0.999900 0.007043 169.50000 1
MTRIX3 15 -0.866000 0.005470 -0.499900 110.80000 1
(ATOM LINES ARE NOT SHOWN.)
END
