HEADER ISOMERASE 31-JAN-00 1EEJ
TITLE CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE,
TITLE 2 DSBC, FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEIN DISULFIDE-ISOMERASE, DSBC;
COMPND 5 EC: 5.3.4.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM;
SOURCE 5 EXPRESSION_SYSTEM: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: EUBACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 2
KEYWDS OXIDOREDUCTASE, PROTEIN DISULFIDE ISOMERASE, PROTEIN
KEYWDS 2 FOLDING, REDOX PROTEIN, REDOX-ACTIVE CENTER
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.MCCARTHY,P.W.HAEBEL,A.TORRONEN,V.RYBIN,E.N.BAKER,
AUTHOR 2 P.METCALF
REVDAT 3 24-FEB-09 1EEJ 1 VERSN
REVDAT 2 01-APR-03 1EEJ 1 JRNL
REVDAT 1 03-AUG-00 1EEJ 0
JRNL AUTH A.A.MCCARTHY,P.W.HAEBEL,A.TORRONEN,V.RYBIN,
JRNL AUTH 2 E.N.BAKER,P.METCALF
JRNL TITL CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND
JRNL TITL 2 ISOMERASE, DSBC, FROM ESCHERICHIA COLI.
JRNL REF NAT.STRUCT.BIOL. V. 7 196 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10700276
JRNL DOI 10.1038/73295
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.RYBIN,A.ZAPUN,A.TORRONEN,S.RAINA,D.MISSIAKAS,
REMARK 1 AUTH 2 T.CREIGHTON,P.METCALF
REMARK 1 TITL CRYSTALLIZATION OF DSBC, THE DISULFIDE BOND
REMARK 1 TITL 2 ISOMERASE FROM ESCHERICHIA COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 1219 1996
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444996008967
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 865666.600
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 34017
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 SET) : 0.214
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3394
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4806
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 515
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3280
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 217
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.91000
REMARK 3 B22 (A**2) : 6.84000
REMARK 3 B33 (A**2) : 0.07000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.81
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.020 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.320 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.43
REMARK 3 BSOL : 79.08
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PAR
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.P
REMARK 3 PARAMETER FILE 5 : MES.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EEJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-00.
REMARK 100 THE RCSB ID CODE IS RCSB010496.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 35436
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
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: NULL
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 550 (MME), MES , PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 29.66800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.24450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.07450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.24450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.66800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.07450
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER
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: 1710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ASP A 18 127.44 -179.25
REMARK 500 GLN A 85 75.35 -110.63
REMARK 500 ASP A 129 68.69 -102.27
REMARK 500 CYS A 163 -174.25 -172.57
REMARK 500 SER A 188 -9.11 -59.73
REMARK 500 SER A 214 -83.97 -90.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 270 DISTANCE = 5.13 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2TRX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1DSB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR
REMARK 900 DISULPHIDE BOND FORMATION IN VIVO
REMARK 900 RELATED ID: 1A2J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF REDUCED AND OXIDIZED DSBA:
REMARK 900 INVESTIGATION OF DOMAIN MOTION AND THIOLATE STABILIZATION
REMARK 900 RELATED ID: 1A2M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF REDUCED AND OXIDIZED DSBA:
REMARK 900 INVESTIGATION OF DOMAIN MOTION AND THIOLATE STABILIZATION
REMARK 900 RELATED ID: 1A2L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF REDUCED AND OXIDIZED DSBA:
REMARK 900 INVESTIGATION OF DOMAIN MOTION AND THIOLATE STABILIZATION
DBREF 1EEJ A 1 216 UNP P21892 DSBC_ECOLI 21 236
DBREF 1EEJ B 1 216 UNP P21892 DSBC_ECOLI 21 236
SEQRES 1 A 216 ASP ASP ALA ALA ILE GLN GLN THR LEU ALA LYS MET GLY
SEQRES 2 A 216 ILE LYS SER SER ASP ILE GLN PRO ALA PRO VAL ALA GLY
SEQRES 3 A 216 MET LYS THR VAL LEU THR ASN SER GLY VAL LEU TYR ILE
SEQRES 4 A 216 THR ASP ASP GLY LYS HIS ILE ILE GLN GLY PRO MET TYR
SEQRES 5 A 216 ASP VAL SER GLY THR ALA PRO VAL ASN VAL THR ASN LYS
SEQRES 6 A 216 MET LEU LEU LYS GLN LEU ASN ALA LEU GLU LYS GLU MET
SEQRES 7 A 216 ILE VAL TYR LYS ALA PRO GLN GLU LYS HIS VAL ILE THR
SEQRES 8 A 216 VAL PHE THR ASP ILE THR CYS GLY TYR CYS HIS LYS LEU
SEQRES 9 A 216 HIS GLU GLN MET ALA ASP TYR ASN ALA LEU GLY ILE THR
SEQRES 10 A 216 VAL ARG TYR LEU ALA PHE PRO ARG GLN GLY LEU ASP SER
SEQRES 11 A 216 ASP ALA GLU LYS GLU MET LYS ALA ILE TRP CYS ALA LYS
SEQRES 12 A 216 ASP LYS ASN LYS ALA PHE ASP ASP VAL MET ALA GLY LYS
SEQRES 13 A 216 SER VAL ALA PRO ALA SER CYS ASP VAL ASP ILE ALA ASP
SEQRES 14 A 216 HIS TYR ALA LEU GLY VAL GLN LEU GLY VAL SER GLY THR
SEQRES 15 A 216 PRO ALA VAL VAL LEU SER ASN GLY THR LEU VAL PRO GLY
SEQRES 16 A 216 TYR GLN PRO PRO LYS GLU MET LYS GLU PHE LEU ASP GLU
SEQRES 17 A 216 HIS GLN LYS MET THR SER GLY LYS
SEQRES 1 B 216 ASP ASP ALA ALA ILE GLN GLN THR LEU ALA LYS MET GLY
SEQRES 2 B 216 ILE LYS SER SER ASP ILE GLN PRO ALA PRO VAL ALA GLY
SEQRES 3 B 216 MET LYS THR VAL LEU THR ASN SER GLY VAL LEU TYR ILE
SEQRES 4 B 216 THR ASP ASP GLY LYS HIS ILE ILE GLN GLY PRO MET TYR
SEQRES 5 B 216 ASP VAL SER GLY THR ALA PRO VAL ASN VAL THR ASN LYS
SEQRES 6 B 216 MET LEU LEU LYS GLN LEU ASN ALA LEU GLU LYS GLU MET
SEQRES 7 B 216 ILE VAL TYR LYS ALA PRO GLN GLU LYS HIS VAL ILE THR
SEQRES 8 B 216 VAL PHE THR ASP ILE THR CYS GLY TYR CYS HIS LYS LEU
SEQRES 9 B 216 HIS GLU GLN MET ALA ASP TYR ASN ALA LEU GLY ILE THR
SEQRES 10 B 216 VAL ARG TYR LEU ALA PHE PRO ARG GLN GLY LEU ASP SER
SEQRES 11 B 216 ASP ALA GLU LYS GLU MET LYS ALA ILE TRP CYS ALA LYS
SEQRES 12 B 216 ASP LYS ASN LYS ALA PHE ASP ASP VAL MET ALA GLY LYS
SEQRES 13 B 216 SER VAL ALA PRO ALA SER CYS ASP VAL ASP ILE ALA ASP
SEQRES 14 B 216 HIS TYR ALA LEU GLY VAL GLN LEU GLY VAL SER GLY THR
SEQRES 15 B 216 PRO ALA VAL VAL LEU SER ASN GLY THR LEU VAL PRO GLY
SEQRES 16 B 216 TYR GLN PRO PRO LYS GLU MET LYS GLU PHE LEU ASP GLU
SEQRES 17 B 216 HIS GLN LYS MET THR SER GLY LYS
HET MES B1001 12
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 MES C6 H13 N O4 S
FORMUL 4 HOH *208(H2 O)
HELIX 1 1 ASP A 1 MET A 12 1 12
HELIX 2 2 VAL A 62 ALA A 73 1 12
HELIX 3 3 LEU A 74 MET A 78 5 5
HELIX 4 4 CYS A 98 GLU A 106 1 9
HELIX 5 5 GLN A 107 LEU A 114 1 8
HELIX 6 6 SER A 130 CYS A 141 1 12
HELIX 7 7 ASP A 144 ALA A 154 1 11
HELIX 8 8 ASP A 166 GLY A 178 1 13
HELIX 9 9 PRO A 198 GLY A 215 1 18
HELIX 10 10 ASP B 1 GLY B 13 1 13
HELIX 11 11 VAL B 62 LEU B 74 1 13
HELIX 12 12 GLU B 75 MET B 78 5 4
HELIX 13 13 CYS B 98 GLN B 107 1 10
HELIX 14 14 GLN B 107 LEU B 114 1 8
HELIX 15 15 SER B 130 CYS B 141 1 12
HELIX 16 16 ASP B 144 ALA B 154 1 11
HELIX 17 17 ASP B 166 GLY B 178 1 13
HELIX 18 18 PRO B 198 SER B 214 1 17
SHEET 1 A 6 SER A 16 PRO A 21 0
SHEET 2 A 6 MET A 27 THR A 32 -1 O THR A 29 N GLN A 20
SHEET 3 A 6 GLY A 35 THR A 40 -1 O GLY A 35 N THR A 32
SHEET 4 A 6 HIS A 45 GLN A 48 -1 O HIS A 45 N THR A 40
SHEET 5 A 6 MET B 51 ASP B 53 -1 N TYR B 52 O ILE A 46
SHEET 6 A 6 VAL B 60 ASN B 61 -1 O VAL B 60 N ASP B 53
SHEET 1 B 6 VAL A 60 ASN A 61 0
SHEET 2 B 6 MET A 51 ASP A 53 -1 N ASP A 53 O VAL A 60
SHEET 3 B 6 HIS B 45 ILE B 47 -1 O ILE B 46 N TYR A 52
SHEET 4 B 6 GLY B 35 THR B 40 -1 O TYR B 38 N ILE B 47
SHEET 5 B 6 MET B 27 THR B 32 -1 N LYS B 28 O ILE B 39
SHEET 6 B 6 SER B 16 PRO B 21 -1 N SER B 17 O LEU B 31
SHEET 1 C 5 ILE A 79 TYR A 81 0
SHEET 2 C 5 ILE A 116 ALA A 122 -1 O VAL A 118 N TYR A 81
SHEET 3 C 5 HIS A 88 THR A 94 1 O HIS A 88 N THR A 117
SHEET 4 C 5 ALA A 184 VAL A 186 -1 O ALA A 184 N PHE A 93
SHEET 5 C 5 LEU A 192 PRO A 194 -1 N VAL A 193 O VAL A 185
SHEET 1 D 5 ILE B 79 TYR B 81 0
SHEET 2 D 5 ILE B 116 ALA B 122 -1 O VAL B 118 N TYR B 81
SHEET 3 D 5 HIS B 88 THR B 94 1 O HIS B 88 N THR B 117
SHEET 4 D 5 ALA B 184 VAL B 186 -1 O ALA B 184 N PHE B 93
SHEET 5 D 5 LEU B 192 PRO B 194 -1 N VAL B 193 O VAL B 185
SSBOND 1 CYS A 98 CYS A 101 1555 1555 2.06
SSBOND 2 CYS A 141 CYS A 163 1555 1555 2.03
SSBOND 3 CYS B 98 CYS B 101 1555 1555 2.05
SSBOND 4 CYS B 141 CYS B 163 1555 1555 2.03
CISPEP 1 GLY A 49 PRO A 50 0 -0.07
CISPEP 2 THR A 182 PRO A 183 0 -0.29
CISPEP 3 GLY B 49 PRO B 50 0 0.24
CISPEP 4 THR B 182 PRO B 183 0 -0.41
SITE 1 AC1 8 SER B 17 LYS B 82 PRO B 84 GLN B 85
SITE 2 AC1 8 GLU B 86 ASP B 166 ASP B 169 HOH B1111
CRYST1 59.336 78.149 94.489 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 0.016853 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012796 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010583 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
