HEADER OXIDOREDUCTASE 15-SEP-01 1JZD
TITLE DSBC-DSBDALPHA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DSBC + N-TERMINAL 4 RESIDUES FROM HIS-TAG;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: DSBDALPHA;
COMPND 11 SYNONYM: C-TYPE CYTOCHROME BIOGENESIS PROTEIN CYCZ, INNER MEMBRANE
COMPND 12 COPPER TOLERANCE PROTEIN;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: DSBC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX HT;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 562;
SOURCE 13 GENE: DSBD;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA Z;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS THIOL DISULFIDE OXIDOREDUCTASE, REACTION INTERMEDIATE, PROTEIN-
KEYWDS 2 PROTEIN COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.W.HAEBEL,D.GOLDSTONE,F.KATZEN,J.BECKWITH,P.METCALF
REVDAT 4 16-AUG-23 1JZD 1 REMARK
REVDAT 3 27-OCT-21 1JZD 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JZD 1 VERSN
REVDAT 1 08-MAR-03 1JZD 0
JRNL AUTH P.W.HAEBEL,D.GOLDSTONE,F.KATZEN,J.BECKWITH,P.METCALF
JRNL TITL THE DISULFIDE BOND ISOMERASE DSBC IS ACTIVATED BY AN
JRNL TITL 2 IMMUNOGLOBULIN-FOLD THIOL OXIDOREDUCTASE: CRYSTAL STRUCTURE
JRNL TITL 3 OF THE DSBC-DSBDALPHA COMPLEX.
JRNL REF EMBO J. V. 21 4774 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 12234918
JRNL DOI 10.1093/EMBOJ/CDF489
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3047250.920
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 24849
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) : 0.234
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1268
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3825
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 216
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4223
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.47000
REMARK 3 B22 (A**2) : 1.47000
REMARK 3 B33 (A**2) : -2.95000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 1.580 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.670 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.280 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.470 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 39.19
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-01; 04-JUL-01; 16-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100
REMARK 200 PH : 4.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; N
REMARK 200 RADIATION SOURCE : ESRF; EMBL/DESY, HAMBURG;
REMARK 200 ROTATING ANODE
REMARK 200 BEAMLINE : ID29; BW7B; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98; 0.83; 1.5418
REMARK 200 MONOCHROMATOR : NULL; NULL; NULL
REMARK 200 OPTICS : NULL; NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4;
REMARK 200 MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24849
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1EEJ (DSBC MONOMER)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PH 4.9, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.16800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.45500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.45500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.58400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.45500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.45500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 172.75200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.45500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.45500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.58400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.45500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.45500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 172.75200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 115.16800
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 LYS A 216
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 GLY B 215
REMARK 465 LYS B 216
REMARK 465 GLY C 1
REMARK 465 LEU C 2
REMARK 465 PHE C 3
REMARK 465 ASP C 4
REMARK 465 ALA C 5
REMARK 465 PRO C 6
REMARK 465 GLY C 7
REMARK 465 ASN C 126
REMARK 465 ALA C 127
REMARK 465 ALA C 128
REMARK 465 PRO C 129
REMARK 465 GLN C 130
REMARK 465 PRO C 131
REMARK 465 VAL C 132
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 ARG C 8 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU C 67 CG CD OE1 OE2
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 C ALA C 124 ND2 ASN C 125 1.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O TYR A 81 O ASN C 125 5655 1.65
REMARK 500 C TYR A 81 O ASN C 125 5655 1.65
REMARK 500 CB LYS A 82 O ALA C 124 5655 1.82
REMARK 500 NZ LYS A 82 OD1 ASN C 125 5655 2.00
REMARK 500 N LYS A 82 O ASN C 125 5655 2.04
REMARK 500 CG1 VAL A 80 N ASN C 125 5655 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 82 CB LYS A 82 CG 0.179
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 215 N - CA - C ANGL. DEV. = 15.9 DEGREES
REMARK 500 VAL C 123 N - CA - C ANGL. DEV. = 26.4 DEGREES
REMARK 500 ALA C 124 CB - CA - C ANGL. DEV. = -10.8 DEGREES
REMARK 500 ALA C 124 N - CA - C ANGL. DEV. = 33.4 DEGREES
REMARK 500 ASN C 125 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASN C 125 N - CA - C ANGL. DEV. = 24.4 DEGREES
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 -2 -70.03 -36.43
REMARK 500 MET A -1 -55.06 -11.53
REMARK 500 THR A 57 -70.76 -67.95
REMARK 500 LYS A 82 139.19 -33.00
REMARK 500 GLN A 85 65.29 -107.49
REMARK 500 TRP A 140 5.50 -68.06
REMARK 500 LYS A 156 -156.05 -129.15
REMARK 500 PRO A 160 177.45 -43.88
REMARK 500 ALA A 161 78.00 179.75
REMARK 500 SER A 214 11.01 -155.86
REMARK 500 ILE B 14 37.06 -146.88
REMARK 500 SER B 16 21.92 -77.76
REMARK 500 GLU B 86 105.33 -53.58
REMARK 500 PHE B 123 81.56 -155.00
REMARK 500 PRO B 160 89.23 -58.44
REMARK 500 SER C 9 -132.39 -117.77
REMARK 500 GLN C 26 -122.66 59.64
REMARK 500 ASP C 57 165.55 176.78
REMARK 500 GLU C 69 -18.01 -49.11
REMARK 500 PHE C 70 -69.36 -108.18
REMARK 500 ASP C 79 -57.53 63.30
REMARK 500 ALA C 106 5.86 -64.26
REMARK 500 ALA C 124 -8.17 -143.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EEJ RELATED DB: PDB
REMARK 900 RELATED ID: 1JZO RELATED DB: PDB
DBREF 1JZD A 1 216 UNP P21892 DSBC_ECOLI 18 236
DBREF 1JZD B 1 216 UNP P21892 DSBC_ECOLI 18 236
DBREF 1JZD C 1 132 UNP P36655 DSBD_ECOLI 20 151
SEQADV 1JZD GLY A -3 UNP P21892 EXPRESSION TAG
SEQADV 1JZD ALA A -2 UNP P21892 EXPRESSION TAG
SEQADV 1JZD MET A -1 UNP P21892 EXPRESSION TAG
SEQADV 1JZD ALA A 0 UNP P21892 EXPRESSION TAG
SEQADV 1JZD SER A 101 UNP P21892 CYS 121 ENGINEERED MUTATION
SEQADV 1JZD GLY B -3 UNP P21892 EXPRESSION TAG
SEQADV 1JZD ALA B -2 UNP P21892 EXPRESSION TAG
SEQADV 1JZD MET B -1 UNP P21892 EXPRESSION TAG
SEQADV 1JZD ALA B 0 UNP P21892 EXPRESSION TAG
SEQADV 1JZD SER B 101 UNP P21892 CYS 121 ENGINEERED MUTATION
SEQADV 1JZD ALA C 103 UNP P36655 CYS 122 ENGINEERED MUTATION
SEQRES 1 A 220 GLY ALA MET ALA ASP ASP ALA ALA ILE GLN GLN THR LEU
SEQRES 2 A 220 ALA LYS MET GLY ILE LYS SER SER ASP ILE GLN PRO ALA
SEQRES 3 A 220 PRO VAL ALA GLY MET LYS THR VAL LEU THR ASN SER GLY
SEQRES 4 A 220 VAL LEU TYR ILE THR ASP ASP GLY LYS HIS ILE ILE GLN
SEQRES 5 A 220 GLY PRO MET TYR ASP VAL SER GLY THR ALA PRO VAL ASN
SEQRES 6 A 220 VAL THR ASN LYS MET LEU LEU LYS GLN LEU ASN ALA LEU
SEQRES 7 A 220 GLU LYS GLU MET ILE VAL TYR LYS ALA PRO GLN GLU LYS
SEQRES 8 A 220 HIS VAL ILE THR VAL PHE THR ASP ILE THR CYS GLY TYR
SEQRES 9 A 220 SER HIS LYS LEU HIS GLU GLN MET ALA ASP TYR ASN ALA
SEQRES 10 A 220 LEU GLY ILE THR VAL ARG TYR LEU ALA PHE PRO ARG GLN
SEQRES 11 A 220 GLY LEU ASP SER ASP ALA GLU LYS GLU MET LYS ALA ILE
SEQRES 12 A 220 TRP CYS ALA LYS ASP LYS ASN LYS ALA PHE ASP ASP VAL
SEQRES 13 A 220 MET ALA GLY LYS SER VAL ALA PRO ALA SER CYS ASP VAL
SEQRES 14 A 220 ASP ILE ALA ASP HIS TYR ALA LEU GLY VAL GLN LEU GLY
SEQRES 15 A 220 VAL SER GLY THR PRO ALA VAL VAL LEU SER ASN GLY THR
SEQRES 16 A 220 LEU VAL PRO GLY TYR GLN PRO PRO LYS GLU MET LYS GLU
SEQRES 17 A 220 PHE LEU ASP GLU HIS GLN LYS MET THR SER GLY LYS
SEQRES 1 B 220 GLY ALA MET ALA ASP ASP ALA ALA ILE GLN GLN THR LEU
SEQRES 2 B 220 ALA LYS MET GLY ILE LYS SER SER ASP ILE GLN PRO ALA
SEQRES 3 B 220 PRO VAL ALA GLY MET LYS THR VAL LEU THR ASN SER GLY
SEQRES 4 B 220 VAL LEU TYR ILE THR ASP ASP GLY LYS HIS ILE ILE GLN
SEQRES 5 B 220 GLY PRO MET TYR ASP VAL SER GLY THR ALA PRO VAL ASN
SEQRES 6 B 220 VAL THR ASN LYS MET LEU LEU LYS GLN LEU ASN ALA LEU
SEQRES 7 B 220 GLU LYS GLU MET ILE VAL TYR LYS ALA PRO GLN GLU LYS
SEQRES 8 B 220 HIS VAL ILE THR VAL PHE THR ASP ILE THR CYS GLY TYR
SEQRES 9 B 220 SER HIS LYS LEU HIS GLU GLN MET ALA ASP TYR ASN ALA
SEQRES 10 B 220 LEU GLY ILE THR VAL ARG TYR LEU ALA PHE PRO ARG GLN
SEQRES 11 B 220 GLY LEU ASP SER ASP ALA GLU LYS GLU MET LYS ALA ILE
SEQRES 12 B 220 TRP CYS ALA LYS ASP LYS ASN LYS ALA PHE ASP ASP VAL
SEQRES 13 B 220 MET ALA GLY LYS SER VAL ALA PRO ALA SER CYS ASP VAL
SEQRES 14 B 220 ASP ILE ALA ASP HIS TYR ALA LEU GLY VAL GLN LEU GLY
SEQRES 15 B 220 VAL SER GLY THR PRO ALA VAL VAL LEU SER ASN GLY THR
SEQRES 16 B 220 LEU VAL PRO GLY TYR GLN PRO PRO LYS GLU MET LYS GLU
SEQRES 17 B 220 PHE LEU ASP GLU HIS GLN LYS MET THR SER GLY LYS
SEQRES 1 C 132 GLY LEU PHE ASP ALA PRO GLY ARG SER GLN PHE VAL PRO
SEQRES 2 C 132 ALA ASP GLN ALA PHE ALA PHE ASP PHE GLN GLN ASN GLN
SEQRES 3 C 132 HIS ASP LEU ASN LEU THR TRP GLN ILE LYS ASP GLY TYR
SEQRES 4 C 132 TYR LEU TYR ARG LYS GLN ILE ARG ILE THR PRO GLU HIS
SEQRES 5 C 132 ALA LYS ILE ALA ASP VAL GLN LEU PRO GLN GLY VAL TRP
SEQRES 6 C 132 HIS GLU ASP GLU PHE TYR GLY LYS SER GLU ILE TYR ARG
SEQRES 7 C 132 ASP ARG LEU THR LEU PRO VAL THR ILE ASN GLN ALA SER
SEQRES 8 C 132 ALA GLY ALA THR LEU THR VAL THR TYR GLN GLY ALA ALA
SEQRES 9 C 132 ASP ALA GLY PHE CYS TYR PRO PRO GLU THR LYS THR VAL
SEQRES 10 C 132 PRO LEU SER GLU VAL VAL ALA ASN ASN ALA ALA PRO GLN
SEQRES 11 C 132 PRO VAL
FORMUL 4 HOH *124(H2 O)
HELIX 1 1 GLY A -3 ASP A 2 1 6
HELIX 2 2 ASP A 2 MET A 12 1 11
HELIX 3 3 VAL A 62 LEU A 74 1 13
HELIX 4 4 GLU A 75 MET A 78 5 4
HELIX 5 5 CYS A 98 GLU A 106 1 9
HELIX 6 6 GLN A 107 LEU A 114 1 8
HELIX 7 7 SER A 130 TRP A 140 1 11
HELIX 8 8 ASP A 144 LYS A 156 1 13
HELIX 9 9 ILE A 167 GLY A 178 1 12
HELIX 10 10 PRO A 198 GLY A 215 1 18
HELIX 11 11 ASP B 2 MET B 12 1 11
HELIX 12 12 VAL B 62 LEU B 67 1 6
HELIX 13 13 LEU B 67 LEU B 74 1 8
HELIX 14 14 GLU B 75 MET B 78 5 4
HELIX 15 15 CYS B 98 GLN B 107 1 10
HELIX 16 16 GLN B 107 LEU B 114 1 8
HELIX 17 17 SER B 130 ALA B 142 1 13
HELIX 18 18 ASP B 144 GLY B 155 1 12
HELIX 19 19 ASP B 166 LEU B 177 1 12
HELIX 20 20 PRO B 198 SER B 214 1 17
HELIX 21 21 PRO C 13 ALA C 17 1 5
HELIX 22 22 LYS C 44 ILE C 46 5 3
SHEET 1 A 6 ASP A 18 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 LEU A 37 N VAL A 30
SHEET 4 A 6 HIS A 45 GLN A 48 -1 O ILE A 47 N TYR A 38
SHEET 5 A 6 MET B 51 ASP B 53 -1 O TYR B 52 N 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 GLN B 48 -1 O ILE B 46 N TYR A 52
SHEET 4 B 6 GLY B 35 THR B 40 -1 N TYR B 38 O ILE B 47
SHEET 5 B 6 MET B 27 THR B 32 -1 N VAL B 30 O LEU B 37
SHEET 6 B 6 ASP B 18 PRO B 21 -1 N ASP B 18 O LEU B 31
SHEET 1 C 5 ILE A 79 VAL A 80 0
SHEET 2 C 5 ILE A 116 ALA A 122 -1 O TYR A 120 N ILE A 79
SHEET 3 C 5 HIS A 88 THR A 94 1 N ILE A 90 O THR A 117
SHEET 4 C 5 ALA A 184 VAL A 186 -1 O VAL A 186 N THR A 91
SHEET 5 C 5 LEU A 192 VAL A 193 -1 O VAL A 193 N 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 N HIS B 88 O THR B 117
SHEET 4 D 5 ALA B 184 VAL B 186 -1 O VAL B 186 N THR B 91
SHEET 5 D 5 LEU B 192 PRO B 194 -1 O VAL B 193 N VAL B 185
SHEET 1 E 4 ARG C 47 VAL C 58 0
SHEET 2 E 4 ASP C 79 TYR C 100 -1 O ASN C 88 N LYS C 54
SHEET 3 E 4 ASP C 28 ILE C 35 -1 N LEU C 31 O LEU C 83
SHEET 4 E 4 PHE C 18 ASN C 25 -1 N ASN C 25 O ASP C 28
SHEET 1 F 3 ARG C 47 VAL C 58 0
SHEET 2 F 3 ASP C 79 TYR C 100 -1 O ASN C 88 N LYS C 54
SHEET 3 F 3 GLU C 113 PRO C 118 -1 O VAL C 117 N LEU C 96
SHEET 1 G 5 VAL C 64 ASP C 68 0
SHEET 2 G 5 GLY C 72 TYR C 77 -1 O SER C 74 N HIS C 66
SHEET 3 G 5 TYR C 39 TYR C 42 -1 N LEU C 41 O TYR C 77
SHEET 4 G 5 GLY C 102 ALA C 104 -1 O ALA C 103 N TYR C 40
SHEET 5 G 5 PHE C 108 CYS C 109 -1 O PHE C 108 N ALA C 104
SSBOND 1 CYS B 141 CYS B 163 1555 1555 2.23
CISPEP 1 GLY A 49 PRO A 50 0 0.08
CISPEP 2 THR A 182 PRO A 183 0 -0.06
CISPEP 3 GLY B 49 PRO B 50 0 1.18
CISPEP 4 THR B 182 PRO B 183 0 -0.25
CRYST1 68.910 68.910 230.336 90.00 90.00 90.00 P 41 21 2 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 0.014512 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014512 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
