HEADER BIOSYNTHETIC PROTEIN 20-MAY-13 3WBK
TITLE CRYSTAL STRUCTURE ANALYSIS OF EUKARYOTIC TRANSLATION INITIATION FACTOR
TITLE 2 5B AND 1A COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 5B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 401-1002;
COMPND 5 SYNONYM: EIF-5B, TRANSLATION INITIATION FACTOR IF-2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 1A;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: UNP RESIDUES 27-153;
COMPND 11 SYNONYM: EIF-1A, EUKARYOTIC TRANSLATION INITIATION FACTOR 4C, EIF-4C;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: FUN12, YAL035W;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: B834-CODONPLUS(DE3)-RIL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 12 ORGANISM_COMMON: YEAST;
SOURCE 13 ORGANISM_TAXID: 559292;
SOURCE 14 STRAIN: ATCC 204508 / S288C;
SOURCE 15 GENE: TIF11, YMR260C, YM8156.02C;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: B834-CODONPLUS(DE3)-RIL
KEYWDS FLEXIBLE, EUKARYOTIC TRANSLATION INITIATION, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ZHENG,R.YAMAMOTO,T.OSE,J.YU,I.TANAKA,M.YAO
REVDAT 3 22-NOV-17 3WBK 1 REMARK
REVDAT 2 04-FEB-15 3WBK 1 JRNL
REVDAT 1 19-NOV-14 3WBK 0
JRNL AUTH A.ZHENG,J.YU,R.YAMAMOTO,T.OSE,I.TANAKA,M.YAO
JRNL TITL X-RAY STRUCTURES OF EIF5B AND THE EIF5B-EIF1A COMPLEX: THE
JRNL TITL 2 CONFORMATIONAL FLEXIBILITY OF EIF5B IS RESTRICTED ON THE
JRNL TITL 3 RIBOSOME BY INTERACTION WITH EIF1A
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 3090 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25478828
JRNL DOI 10.1107/S1399004714021476
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 24828
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) : 0.261
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.317
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1769
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1504
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.3540
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.4150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9309
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 159.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.35000
REMARK 3 B22 (A**2) : 1.66000
REMARK 3 B33 (A**2) : 10.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.687
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.608
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.687
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9448 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12772 ; 1.306 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1184 ; 6.026 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 401 ;33.689 ;24.988
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1780 ;18.218 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;19.763 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1510 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6882 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4757 ;10.383 ;15.672
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5934 ;16.555 ;23.490
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4691 ;11.418 ;16.085
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 602 B 2 602 626 0.230 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3WBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000096128.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR , SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24875
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.150
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 3WBI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 8.2, 12.5%(W/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 50.96950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.37500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.47100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.37500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.96950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.47100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 LYS A 1
REMARK 465 VAL A 30
REMARK 465 GLN A 31
REMARK 465 GLY A 32
REMARK 465 GLY A 33
REMARK 465 GLU A 34
REMARK 465 SER A 221
REMARK 465 LYS A 222
REMARK 465 GLN A 223
REMARK 465 LEU A 224
REMARK 465 MET A 225
REMARK 465 TYR A 226
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 LYS B 1
REMARK 465 ASN B 29
REMARK 465 VAL B 30
REMARK 465 GLN B 31
REMARK 465 GLY B 32
REMARK 465 GLY B 33
REMARK 465 GLU B 34
REMARK 465 ALA B 35
REMARK 465 GLY B 36
REMARK 465 GLU B 286
REMARK 465 LEU B 287
REMARK 465 ARG B 288
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
REMARK 465 ILE C 1
REMARK 465 TYR C 2
REMARK 465 LYS C 3
REMARK 465 GLU C 4
REMARK 465 GLU C 5
REMARK 465 GLY C 6
REMARK 465 GLN C 7
REMARK 465 GLU C 8
REMARK 465 TYR C 9
REMARK 465 ALA C 10
REMARK 465 GLN C 11
REMARK 465 ILE C 12
REMARK 465 THR C 13
REMARK 465 LYS C 14
REMARK 465 MET C 15
REMARK 465 LEU C 16
REMARK 465 GLY C 17
REMARK 465 ASN C 18
REMARK 465 GLY C 19
REMARK 465 ARG C 20
REMARK 465 VAL C 21
REMARK 465 GLU C 22
REMARK 465 ALA C 23
REMARK 465 SER C 24
REMARK 465 CYS C 25
REMARK 465 PHE C 26
REMARK 465 ASP C 27
REMARK 465 GLY C 28
REMARK 465 ASN C 29
REMARK 465 LYS C 30
REMARK 465 ARG C 31
REMARK 465 MET C 32
REMARK 465 ALA C 33
REMARK 465 HIS C 34
REMARK 465 ILE C 35
REMARK 465 ARG C 36
REMARK 465 GLY C 37
REMARK 465 LYS C 38
REMARK 465 LEU C 39
REMARK 465 ARG C 40
REMARK 465 LYS C 41
REMARK 465 LYS C 42
REMARK 465 VAL C 43
REMARK 465 TRP C 44
REMARK 465 MET C 45
REMARK 465 GLY C 46
REMARK 465 GLN C 47
REMARK 465 GLY C 48
REMARK 465 ASP C 49
REMARK 465 ILE C 50
REMARK 465 ILE C 51
REMARK 465 LEU C 52
REMARK 465 VAL C 53
REMARK 465 SER C 54
REMARK 465 LEU C 55
REMARK 465 ARG C 56
REMARK 465 ASP C 57
REMARK 465 PHE C 58
REMARK 465 GLN C 59
REMARK 465 ASP C 60
REMARK 465 ASP C 61
REMARK 465 GLN C 62
REMARK 465 CYS C 63
REMARK 465 ASP C 64
REMARK 465 VAL C 65
REMARK 465 VAL C 66
REMARK 465 HIS C 67
REMARK 465 LYS C 68
REMARK 465 TYR C 69
REMARK 465 ASN C 70
REMARK 465 LEU C 71
REMARK 465 ASP C 72
REMARK 465 GLU C 73
REMARK 465 ALA C 74
REMARK 465 ARG C 75
REMARK 465 THR C 76
REMARK 465 LEU C 77
REMARK 465 LYS C 78
REMARK 465 ASN C 79
REMARK 465 GLN C 80
REMARK 465 GLY C 81
REMARK 465 GLU C 82
REMARK 465 LEU C 83
REMARK 465 PRO C 84
REMARK 465 GLU C 85
REMARK 465 ASN C 86
REMARK 465 ALA C 87
REMARK 465 LYS C 88
REMARK 465 ILE C 89
REMARK 465 ASN C 90
REMARK 465 GLU C 91
REMARK 465 THR C 92
REMARK 465 ASP C 93
REMARK 465 ASN C 94
REMARK 465 PHE C 95
REMARK 465 GLY C 96
REMARK 465 PHE C 97
REMARK 465 GLU C 98
REMARK 465 SER C 99
REMARK 465 ASP C 100
REMARK 465 GLU C 101
REMARK 465 ASP C 102
REMARK 465 VAL C 103
REMARK 465 ASN C 104
REMARK 465 PHE C 105
REMARK 465 GLU C 106
REMARK 465 PHE C 107
REMARK 465 GLY C 108
REMARK 465 ASN C 109
REMARK 465 ALA C 110
REMARK 465 ASP C 111
REMARK 465 GLU C 112
REMARK 465 ASP C 113
REMARK 465 ASP C 114
REMARK 465 GLU C 115
REMARK 465 GLU C 116
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 80 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 PHE A 83 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 84 OG
REMARK 470 ASN A 85 CG OD1 ND2
REMARK 470 LEU A 86 CG CD1 CD2
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 470 SER A 91 OG
REMARK 470 GLU A 292 CG CD OE1 OE2
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 SER A 88 -131.92 60.41
REMARK 500 LYS A 131 16.45 81.41
REMARK 500 LYS A 190 13.49 58.62
REMARK 500 LEU A 289 -51.95 -125.39
REMARK 500 GLU A 292 -129.12 57.15
REMARK 500 ALA A 302 40.02 74.20
REMARK 500 THR A 350 -117.41 61.57
REMARK 500 THR A 397 6.80 -67.58
REMARK 500 ALA A 402 76.62 -151.34
REMARK 500 ALA A 406 43.74 -91.40
REMARK 500 ILE A 463 116.59 -167.66
REMARK 500 THR A 505 -60.42 -122.63
REMARK 500 GLU A 508 -6.36 70.58
REMARK 500 PRO A 551 152.12 -49.31
REMARK 500 LYS A 578 -55.54 71.62
REMARK 500 THR B 77 70.22 -157.02
REMARK 500 ASN B 143 8.95 58.54
REMARK 500 PHE B 243 34.72 -142.98
REMARK 500 ALA B 302 14.52 85.46
REMARK 500 LEU B 312 -126.20 47.73
REMARK 500 GLU B 313 -0.50 77.65
REMARK 500 ALA B 406 45.39 -90.00
REMARK 500 ASP B 412 -58.40 72.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WBI RELATED DB: PDB
REMARK 900 RELATED ID: 3WBJ RELATED DB: PDB
DBREF 3WBK A 1 602 UNP P39730 IF2P_YEAST 401 1002
DBREF 3WBK B 1 602 UNP P39730 IF2P_YEAST 401 1002
DBREF 3WBK C 1 127 UNP P38912 IF1A_YEAST 27 153
SEQADV 3WBK GLY A -3 UNP P39730 EXPRESSION TAG
SEQADV 3WBK SER A -2 UNP P39730 EXPRESSION TAG
SEQADV 3WBK HIS A -1 UNP P39730 EXPRESSION TAG
SEQADV 3WBK MET A 0 UNP P39730 EXPRESSION TAG
SEQADV 3WBK GLY B -3 UNP P39730 EXPRESSION TAG
SEQADV 3WBK SER B -2 UNP P39730 EXPRESSION TAG
SEQADV 3WBK HIS B -1 UNP P39730 EXPRESSION TAG
SEQADV 3WBK MET B 0 UNP P39730 EXPRESSION TAG
SEQADV 3WBK GLY C -3 UNP P38912 EXPRESSION TAG
SEQADV 3WBK SER C -2 UNP P38912 EXPRESSION TAG
SEQADV 3WBK HIS C -1 UNP P38912 EXPRESSION TAG
SEQADV 3WBK MET C 0 UNP P38912 EXPRESSION TAG
SEQRES 1 A 606 GLY SER HIS MET LYS ASP LEU ARG SER PRO ILE CYS CYS
SEQRES 2 A 606 ILE LEU GLY HIS VAL ASP THR GLY LYS THR LYS LEU LEU
SEQRES 3 A 606 ASP LYS ILE ARG GLN THR ASN VAL GLN GLY GLY GLU ALA
SEQRES 4 A 606 GLY GLY ILE THR GLN GLN ILE GLY ALA THR TYR PHE PRO
SEQRES 5 A 606 ILE ASP ALA ILE LYS ALA LYS THR LYS VAL MET ALA GLU
SEQRES 6 A 606 TYR GLU LYS GLN THR PHE ASP VAL PRO GLY LEU LEU VAL
SEQRES 7 A 606 ILE ASP THR PRO GLY HIS GLU SER PHE SER ASN LEU ARG
SEQRES 8 A 606 SER ARG GLY SER SER LEU CYS ASN ILE ALA ILE LEU VAL
SEQRES 9 A 606 ILE ASP ILE MET HIS GLY LEU GLU GLN GLN THR ILE GLU
SEQRES 10 A 606 SER ILE LYS LEU LEU ARG ASP ARG LYS ALA PRO PHE VAL
SEQRES 11 A 606 VAL ALA LEU ASN LYS ILE ASP ARG LEU TYR ASP TRP LYS
SEQRES 12 A 606 ALA ILE PRO ASN ASN SER PHE ARG ASP SER PHE ALA LYS
SEQRES 13 A 606 GLN SER ARG ALA VAL GLN GLU GLU PHE GLN SER ARG TYR
SEQRES 14 A 606 SER LYS ILE GLN LEU GLU LEU ALA GLU GLN GLY LEU ASN
SEQRES 15 A 606 SER GLU LEU TYR PHE GLN ASN LYS ASN MET SER LYS TYR
SEQRES 16 A 606 VAL SER ILE VAL PRO THR SER ALA VAL THR GLY GLU GLY
SEQRES 17 A 606 VAL PRO ASP LEU LEU TRP LEU LEU LEU GLU LEU THR GLN
SEQRES 18 A 606 LYS ARG MET SER LYS GLN LEU MET TYR LEU SER HIS VAL
SEQRES 19 A 606 GLU ALA THR ILE LEU GLU VAL LYS VAL VAL GLU GLY PHE
SEQRES 20 A 606 GLY THR THR ILE ASP VAL ILE LEU SER ASN GLY TYR LEU
SEQRES 21 A 606 ARG GLU GLY ASP ARG ILE VAL LEU CYS GLY MET ASN GLY
SEQRES 22 A 606 PRO ILE VAL THR ASN ILE ARG ALA LEU LEU THR PRO GLN
SEQRES 23 A 606 PRO LEU ARG GLU LEU ARG LEU LYS SER GLU TYR VAL HIS
SEQRES 24 A 606 HIS LYS GLU VAL LYS ALA ALA LEU GLY VAL LYS ILE ALA
SEQRES 25 A 606 ALA ASN ASP LEU GLU LYS ALA VAL SER GLY SER ARG LEU
SEQRES 26 A 606 LEU VAL VAL GLY PRO GLU ASP ASP GLU ASP GLU LEU MET
SEQRES 27 A 606 ASP ASP VAL MET ASP ASP LEU THR GLY LEU LEU ASP SER
SEQRES 28 A 606 VAL ASP THR THR GLY LYS GLY VAL VAL VAL GLN ALA SER
SEQRES 29 A 606 THR LEU GLY SER LEU GLU ALA LEU LEU ASP PHE LEU LYS
SEQRES 30 A 606 ASP MET LYS ILE PRO VAL MET SER ILE GLY LEU GLY PRO
SEQRES 31 A 606 VAL TYR LYS ARG ASP VAL MET LYS ALA SER THR MET LEU
SEQRES 32 A 606 GLU LYS ALA PRO GLU TYR ALA VAL MET LEU CYS PHE ASP
SEQRES 33 A 606 VAL LYS VAL ASP LYS GLU ALA GLU GLN TYR ALA GLU GLN
SEQRES 34 A 606 GLU GLY ILE LYS ILE PHE ASN ALA ASP VAL ILE TYR HIS
SEQRES 35 A 606 LEU PHE ASP SER PHE THR ALA TYR GLN GLU LYS LEU LEU
SEQRES 36 A 606 GLU GLU ARG ARG LYS ASP PHE LEU ASP TYR ALA ILE PHE
SEQRES 37 A 606 PRO CYS VAL LEU GLN THR LEU GLN ILE ILE ASN LYS ARG
SEQRES 38 A 606 GLY PRO MET ILE ILE GLY VAL ASP VAL LEU GLU GLY THR
SEQRES 39 A 606 LEU ARG VAL GLY THR PRO ILE CYS ALA VAL LYS THR ASP
SEQRES 40 A 606 PRO THR THR LYS GLU ARG GLN THR LEU ILE LEU GLY LYS
SEQRES 41 A 606 VAL ILE SER LEU GLU ILE ASN HIS GLN PRO VAL GLN GLU
SEQRES 42 A 606 VAL LYS LYS GLY GLN THR ALA ALA GLY VAL ALA VAL ARG
SEQRES 43 A 606 LEU GLU ASP PRO SER GLY GLN GLN PRO ILE TRP GLY ARG
SEQRES 44 A 606 HIS VAL ASP GLU ASN ASP THR LEU TYR SER LEU VAL SER
SEQRES 45 A 606 ARG ARG SER ILE ASP THR LEU LYS ASP LYS ALA PHE ARG
SEQRES 46 A 606 ASP GLN VAL ALA ARG SER ASP TRP LEU LEU LEU LYS LYS
SEQRES 47 A 606 LEU LYS VAL VAL PHE GLY ILE GLU
SEQRES 1 B 606 GLY SER HIS MET LYS ASP LEU ARG SER PRO ILE CYS CYS
SEQRES 2 B 606 ILE LEU GLY HIS VAL ASP THR GLY LYS THR LYS LEU LEU
SEQRES 3 B 606 ASP LYS ILE ARG GLN THR ASN VAL GLN GLY GLY GLU ALA
SEQRES 4 B 606 GLY GLY ILE THR GLN GLN ILE GLY ALA THR TYR PHE PRO
SEQRES 5 B 606 ILE ASP ALA ILE LYS ALA LYS THR LYS VAL MET ALA GLU
SEQRES 6 B 606 TYR GLU LYS GLN THR PHE ASP VAL PRO GLY LEU LEU VAL
SEQRES 7 B 606 ILE ASP THR PRO GLY HIS GLU SER PHE SER ASN LEU ARG
SEQRES 8 B 606 SER ARG GLY SER SER LEU CYS ASN ILE ALA ILE LEU VAL
SEQRES 9 B 606 ILE ASP ILE MET HIS GLY LEU GLU GLN GLN THR ILE GLU
SEQRES 10 B 606 SER ILE LYS LEU LEU ARG ASP ARG LYS ALA PRO PHE VAL
SEQRES 11 B 606 VAL ALA LEU ASN LYS ILE ASP ARG LEU TYR ASP TRP LYS
SEQRES 12 B 606 ALA ILE PRO ASN ASN SER PHE ARG ASP SER PHE ALA LYS
SEQRES 13 B 606 GLN SER ARG ALA VAL GLN GLU GLU PHE GLN SER ARG TYR
SEQRES 14 B 606 SER LYS ILE GLN LEU GLU LEU ALA GLU GLN GLY LEU ASN
SEQRES 15 B 606 SER GLU LEU TYR PHE GLN ASN LYS ASN MET SER LYS TYR
SEQRES 16 B 606 VAL SER ILE VAL PRO THR SER ALA VAL THR GLY GLU GLY
SEQRES 17 B 606 VAL PRO ASP LEU LEU TRP LEU LEU LEU GLU LEU THR GLN
SEQRES 18 B 606 LYS ARG MET SER LYS GLN LEU MET TYR LEU SER HIS VAL
SEQRES 19 B 606 GLU ALA THR ILE LEU GLU VAL LYS VAL VAL GLU GLY PHE
SEQRES 20 B 606 GLY THR THR ILE ASP VAL ILE LEU SER ASN GLY TYR LEU
SEQRES 21 B 606 ARG GLU GLY ASP ARG ILE VAL LEU CYS GLY MET ASN GLY
SEQRES 22 B 606 PRO ILE VAL THR ASN ILE ARG ALA LEU LEU THR PRO GLN
SEQRES 23 B 606 PRO LEU ARG GLU LEU ARG LEU LYS SER GLU TYR VAL HIS
SEQRES 24 B 606 HIS LYS GLU VAL LYS ALA ALA LEU GLY VAL LYS ILE ALA
SEQRES 25 B 606 ALA ASN ASP LEU GLU LYS ALA VAL SER GLY SER ARG LEU
SEQRES 26 B 606 LEU VAL VAL GLY PRO GLU ASP ASP GLU ASP GLU LEU MET
SEQRES 27 B 606 ASP ASP VAL MET ASP ASP LEU THR GLY LEU LEU ASP SER
SEQRES 28 B 606 VAL ASP THR THR GLY LYS GLY VAL VAL VAL GLN ALA SER
SEQRES 29 B 606 THR LEU GLY SER LEU GLU ALA LEU LEU ASP PHE LEU LYS
SEQRES 30 B 606 ASP MET LYS ILE PRO VAL MET SER ILE GLY LEU GLY PRO
SEQRES 31 B 606 VAL TYR LYS ARG ASP VAL MET LYS ALA SER THR MET LEU
SEQRES 32 B 606 GLU LYS ALA PRO GLU TYR ALA VAL MET LEU CYS PHE ASP
SEQRES 33 B 606 VAL LYS VAL ASP LYS GLU ALA GLU GLN TYR ALA GLU GLN
SEQRES 34 B 606 GLU GLY ILE LYS ILE PHE ASN ALA ASP VAL ILE TYR HIS
SEQRES 35 B 606 LEU PHE ASP SER PHE THR ALA TYR GLN GLU LYS LEU LEU
SEQRES 36 B 606 GLU GLU ARG ARG LYS ASP PHE LEU ASP TYR ALA ILE PHE
SEQRES 37 B 606 PRO CYS VAL LEU GLN THR LEU GLN ILE ILE ASN LYS ARG
SEQRES 38 B 606 GLY PRO MET ILE ILE GLY VAL ASP VAL LEU GLU GLY THR
SEQRES 39 B 606 LEU ARG VAL GLY THR PRO ILE CYS ALA VAL LYS THR ASP
SEQRES 40 B 606 PRO THR THR LYS GLU ARG GLN THR LEU ILE LEU GLY LYS
SEQRES 41 B 606 VAL ILE SER LEU GLU ILE ASN HIS GLN PRO VAL GLN GLU
SEQRES 42 B 606 VAL LYS LYS GLY GLN THR ALA ALA GLY VAL ALA VAL ARG
SEQRES 43 B 606 LEU GLU ASP PRO SER GLY GLN GLN PRO ILE TRP GLY ARG
SEQRES 44 B 606 HIS VAL ASP GLU ASN ASP THR LEU TYR SER LEU VAL SER
SEQRES 45 B 606 ARG ARG SER ILE ASP THR LEU LYS ASP LYS ALA PHE ARG
SEQRES 46 B 606 ASP GLN VAL ALA ARG SER ASP TRP LEU LEU LEU LYS LYS
SEQRES 47 B 606 LEU LYS VAL VAL PHE GLY ILE GLU
SEQRES 1 C 131 GLY SER HIS MET ILE TYR LYS GLU GLU GLY GLN GLU TYR
SEQRES 2 C 131 ALA GLN ILE THR LYS MET LEU GLY ASN GLY ARG VAL GLU
SEQRES 3 C 131 ALA SER CYS PHE ASP GLY ASN LYS ARG MET ALA HIS ILE
SEQRES 4 C 131 ARG GLY LYS LEU ARG LYS LYS VAL TRP MET GLY GLN GLY
SEQRES 5 C 131 ASP ILE ILE LEU VAL SER LEU ARG ASP PHE GLN ASP ASP
SEQRES 6 C 131 GLN CYS ASP VAL VAL HIS LYS TYR ASN LEU ASP GLU ALA
SEQRES 7 C 131 ARG THR LEU LYS ASN GLN GLY GLU LEU PRO GLU ASN ALA
SEQRES 8 C 131 LYS ILE ASN GLU THR ASP ASN PHE GLY PHE GLU SER ASP
SEQRES 9 C 131 GLU ASP VAL ASN PHE GLU PHE GLY ASN ALA ASP GLU ASP
SEQRES 10 C 131 ASP GLU GLU GLY GLU ASP GLU GLU LEU ASP ILE ASP ASP
SEQRES 11 C 131 ILE
HELIX 1 1 HIS A 13 THR A 16 5 4
HELIX 2 2 GLY A 17 GLN A 27 1 11
HELIX 3 3 ILE A 49 LYS A 57 1 9
HELIX 4 4 VAL A 58 TYR A 62 5 5
HELIX 5 5 PRO A 78 SER A 88 1 11
HELIX 6 6 GLU A 108 LYS A 122 1 15
HELIX 7 7 LYS A 131 LEU A 135 5 5
HELIX 8 8 SER A 145 LYS A 152 1 8
HELIX 9 9 SER A 154 GLN A 175 1 22
HELIX 10 10 PHE A 183 ASN A 185 5 3
HELIX 11 11 GLY A 204 GLN A 217 1 14
HELIX 12 12 ASP A 329 VAL A 348 1 20
HELIX 13 13 THR A 361 LYS A 376 1 16
HELIX 14 14 TYR A 388 THR A 397 1 10
HELIX 15 15 ALA A 402 TYR A 405 5 4
HELIX 16 16 ASP A 416 GLU A 426 1 11
HELIX 17 17 VAL A 435 ALA A 462 1 28
HELIX 18 18 SER A 568 ASP A 577 1 10
HELIX 19 19 ALA A 585 GLY A 600 1 16
HELIX 20 20 HIS B 13 THR B 16 5 4
HELIX 21 21 GLY B 17 GLN B 27 1 11
HELIX 22 22 ILE B 49 LYS B 57 1 9
HELIX 23 23 VAL B 58 TYR B 62 5 5
HELIX 24 24 GLU B 81 ARG B 87 1 7
HELIX 25 25 GLU B 108 LYS B 122 1 15
HELIX 26 26 LYS B 131 LEU B 135 5 5
HELIX 27 27 SER B 145 LYS B 152 1 8
HELIX 28 28 SER B 154 GLN B 175 1 22
HELIX 29 29 PHE B 183 ASN B 185 5 3
HELIX 30 30 GLY B 204 GLN B 217 1 14
HELIX 31 31 MET B 220 MET B 225 1 6
HELIX 32 32 ASP B 329 VAL B 337 1 9
HELIX 33 33 MET B 338 ASP B 346 1 9
HELIX 34 34 THR B 361 LYS B 376 1 16
HELIX 35 35 TYR B 388 ALA B 402 1 15
HELIX 36 36 ASP B 416 GLU B 426 1 11
HELIX 37 37 VAL B 435 TYR B 461 1 27
HELIX 38 38 SER B 568 LEU B 575 1 8
HELIX 39 39 ASP B 577 ASP B 582 1 6
HELIX 40 40 ALA B 585 GLY B 600 1 16
SHEET 1 A 7 THR A 45 PRO A 48 0
SHEET 2 A 7 GLY A 71 ILE A 75 -1 O LEU A 72 N PHE A 47
SHEET 3 A 7 ILE A 7 LEU A 11 1 N CYS A 8 O LEU A 73
SHEET 4 A 7 ILE A 96 ASP A 102 1 O ILE A 98 N CYS A 9
SHEET 5 A 7 PHE A 125 ASN A 130 1 O ALA A 128 N ILE A 101
SHEET 6 A 7 VAL A 192 PRO A 196 1 O VAL A 195 N VAL A 127
SHEET 7 A 7 SER A 179 LEU A 181 1 N GLU A 180 O VAL A 192
SHEET 1 B 8 GLY A 269 ASN A 274 0
SHEET 2 B 8 ARG A 261 GLY A 266 -1 N LEU A 264 O ILE A 271
SHEET 3 B 8 ARG A 320 VAL A 323 -1 O LEU A 322 N VAL A 263
SHEET 4 B 8 GLU A 231 VAL A 240 -1 N ALA A 232 O LEU A 321
SHEET 5 B 8 GLY A 244 ASN A 253 -1 O ASP A 248 N GLU A 236
SHEET 6 B 8 LEU A 303 ALA A 308 -1 O ILE A 307 N ILE A 247
SHEET 7 B 8 ALA A 277 THR A 280 -1 N LEU A 279 O LYS A 306
SHEET 8 B 8 VAL A 294 HIS A 295 -1 O VAL A 294 N THR A 280
SHEET 1 C 2 LEU A 256 ARG A 257 0
SHEET 2 C 2 GLU A 298 VAL A 299 -1 O VAL A 299 N LEU A 256
SHEET 1 D 4 VAL A 379 LEU A 384 0
SHEET 2 D 4 VAL A 355 ALA A 359 1 N VAL A 357 O SER A 381
SHEET 3 D 4 VAL A 407 PHE A 411 1 O LEU A 409 N VAL A 356
SHEET 4 D 4 LYS A 429 ALA A 433 1 O PHE A 431 N MET A 408
SHEET 1 E 7 GLN A 525 VAL A 527 0
SHEET 2 E 7 LEU A 512 ILE A 522 -1 N ILE A 522 O GLN A 525
SHEET 3 E 7 PRO A 496 ALA A 499 -1 N ILE A 497 O GLY A 515
SHEET 4 E 7 LEU A 563 SER A 565 -1 O TYR A 564 N CYS A 498
SHEET 5 E 7 CYS A 466 ASN A 475 -1 N LEU A 468 O LEU A 563
SHEET 6 E 7 ILE A 481 ARG A 492 -1 O ASP A 485 N GLN A 469
SHEET 7 E 7 GLU A 529 LYS A 531 -1 O VAL A 530 N LEU A 491
SHEET 1 F 5 GLN A 525 VAL A 527 0
SHEET 2 F 5 LEU A 512 ILE A 522 -1 N ILE A 522 O GLN A 525
SHEET 3 F 5 VAL A 539 GLU A 544 -1 O ARG A 542 N ILE A 518
SHEET 4 F 5 ILE A 481 ARG A 492 -1 N ILE A 482 O VAL A 541
SHEET 5 F 5 GLU A 529 LYS A 531 -1 O VAL A 530 N LEU A 491
SHEET 1 G 8 THR B 39 GLN B 40 0
SHEET 2 G 8 THR B 45 PRO B 48 -1 O TYR B 46 N THR B 39
SHEET 3 G 8 GLY B 71 ILE B 75 -1 O LEU B 72 N PHE B 47
SHEET 4 G 8 ILE B 7 LEU B 11 1 N CYS B 8 O LEU B 73
SHEET 5 G 8 ILE B 96 ASP B 102 1 O ILE B 98 N CYS B 9
SHEET 6 G 8 PHE B 125 ASN B 130 1 O VAL B 126 N LEU B 99
SHEET 7 G 8 VAL B 192 PRO B 196 1 O VAL B 195 N VAL B 127
SHEET 8 G 8 SER B 179 LEU B 181 1 N GLU B 180 O ILE B 194
SHEET 1 H 8 ILE B 271 ASN B 274 0
SHEET 2 H 8 ARG B 261 LEU B 264 -1 N ILE B 262 O THR B 273
SHEET 3 H 8 ARG B 320 VAL B 323 -1 O LEU B 322 N VAL B 263
SHEET 4 H 8 GLU B 231 VAL B 240 -1 N ALA B 232 O LEU B 321
SHEET 5 H 8 GLY B 244 ASN B 253 -1 O ILE B 250 N THR B 233
SHEET 6 H 8 GLY B 304 ALA B 308 -1 O ILE B 307 N ILE B 247
SHEET 7 H 8 ALA B 277 PRO B 281 -1 N ALA B 277 O ALA B 308
SHEET 8 H 8 TYR B 293 HIS B 295 -1 O VAL B 294 N THR B 280
SHEET 1 I 2 TYR B 255 ARG B 257 0
SHEET 2 I 2 GLU B 298 LYS B 300 -1 O VAL B 299 N LEU B 256
SHEET 1 J 4 VAL B 379 GLY B 383 0
SHEET 2 J 4 VAL B 355 GLN B 358 1 N VAL B 357 O SER B 381
SHEET 3 J 4 VAL B 407 CYS B 410 1 O LEU B 409 N VAL B 356
SHEET 4 J 4 LYS B 429 ASN B 432 1 O PHE B 431 N MET B 408
SHEET 1 K 7 GLN B 525 VAL B 527 0
SHEET 2 K 7 GLU B 508 ILE B 522 -1 N ILE B 522 O GLN B 525
SHEET 3 K 7 PRO B 496 ASP B 503 -1 N ILE B 497 O GLY B 515
SHEET 4 K 7 LEU B 563 SER B 565 -1 O TYR B 564 N CYS B 498
SHEET 5 K 7 CYS B 466 ASN B 475 -1 N LEU B 468 O LEU B 563
SHEET 6 K 7 MET B 480 ARG B 492 -1 O GLY B 483 N GLN B 472
SHEET 7 K 7 GLU B 529 LYS B 531 -1 O VAL B 530 N LEU B 491
SHEET 1 L 5 GLN B 525 VAL B 527 0
SHEET 2 L 5 GLU B 508 ILE B 522 -1 N ILE B 522 O GLN B 525
SHEET 3 L 5 VAL B 539 GLU B 544 -1 O ALA B 540 N GLU B 521
SHEET 4 L 5 MET B 480 ARG B 492 -1 N ILE B 482 O VAL B 541
SHEET 5 L 5 GLU B 529 LYS B 531 -1 O VAL B 530 N LEU B 491
SSBOND 1 CYS A 9 CYS A 94 1555 1555 2.02
SSBOND 2 CYS B 9 CYS B 94 1555 1555 2.03
CISPEP 1 GLY A 478 PRO A 479 0 -1.88
CISPEP 2 LEU B 284 ARG B 285 0 -2.51
CISPEP 3 GLU C 120 GLU C 121 0 1.12
CRYST1 101.939 120.942 132.750 90.00 90.00 90.00 P 21 21 21 8
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 0.009810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007533 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
