HEADER PROTEIN BINDING 07-JUL-14 4TXV
TITLE CRYSTAL STRUCTURE OF THE MIXED DISULFIDE INTERMEDIATE BETWEEN
TITLE 2 THIOREDOXIN-LIKE TLPAS(C110S) AND SUBUNIT II OF CYTOCHROME C OXIDASE
TITLE 3 COXBPD (C233S)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN TLPA;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 40-217;
COMPND 5 SYNONYM: CYTOCHROME C BIOGENESIS PROTEIN TLPA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 123-264;
COMPND 12 EC: 1.9.3.1;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM DIAZOEFFICIENS;
SOURCE 3 ORGANISM_TAXID: 224911;
SOURCE 4 STRAIN: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
SOURCE 5 GENE: TLPA, BLL1380;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM DIAZOEFFICIENS (STRAIN JCM 10833
SOURCE 11 / IAM 13628 / NBRC 14792 / USDA 110);
SOURCE 12 ORGANISM_TAXID: 224911;
SOURCE 13 STRAIN: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
SOURCE 14 GENE: COXB;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PPROEXHTA-HIS6-COXBPDC233S
KEYWDS THIOREDOXIN, MIXED DISULPHIDE, CYTOCHROME C OXIDASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR N.QUADE,H.K.ABICHT,H.HENNECKE,R.GLOCKSHUBER
REVDAT 7 20-DEC-23 4TXV 1 REMARK
REVDAT 6 13-JUN-18 4TXV 1 SOURCE DBREF SEQADV
REVDAT 5 06-SEP-17 4TXV 1 REMARK ATOM
REVDAT 4 10-DEC-14 4TXV 1
REVDAT 3 03-DEC-14 4TXV 1 JRNL
REVDAT 2 15-OCT-14 4TXV 1 JRNL
REVDAT 1 01-OCT-14 4TXV 0
JRNL AUTH H.K.ABICHT,M.A.SCHARER,N.QUADE,R.LEDERMANN,E.MOHORKO,
JRNL AUTH 2 G.CAPITANI,H.HENNECKE,R.GLOCKSHUBER
JRNL TITL HOW PERIPLASMIC THIOREDOXIN TLPA REDUCES BACTERIAL COPPER
JRNL TITL 2 CHAPERONE SCOI AND CYTOCHROME OXIDASE SUBUNIT II (COXB)
JRNL TITL 3 PRIOR TO METALLATION.
JRNL REF J.BIOL.CHEM. V. 289 32431 2014
JRNL REFN ESSN 1083-351X
JRNL PMID 25274631
JRNL DOI 10.1074/JBC.M114.607127
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 45680
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2304
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3123
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4823
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 444
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.20000
REMARK 3 B22 (A**2) : -0.65000
REMARK 3 B33 (A**2) : 1.85000
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): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.465
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4934 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4824 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6689 ; 1.825 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11143 ; 0.882 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 623 ; 6.759 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;35.669 ;24.745
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 843 ;16.154 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;22.377 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 748 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5506 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1043 ; 0.001 ; 0.020
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): 2507 ; 3.146 ; 3.565
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2506 ; 3.145 ; 3.564
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3125 ; 4.317 ; 5.318
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 : 1.20
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4TXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45680
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.480
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.81700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.620
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIUES 1JFU AND 1M56
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG2000 MME, 0.8M FORMIC
REMARK 280 ACID/NAOH, 0.1 M NA-CACODYLATE, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292K
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 37.41500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.68500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.68500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.41500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.82000
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: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ALA A 38
REMARK 465 PRO A 39
REMARK 465 THR A 40
REMARK 465 LYS A 216
REMARK 465 ALA A 217
REMARK 465 ALA A 218
REMARK 465 ALA A 219
REMARK 465 ALA A 220
REMARK 465 LEU A 221
REMARK 465 GLY B 121
REMARK 465 ALA B 122
REMARK 465 SER B 265
REMARK 465 GLY B 266
REMARK 465 GLY B 267
REMARK 465 THR B 268
REMARK 465 GLY B 269
REMARK 465 THR B 270
REMARK 465 TYR B 271
REMARK 465 ALA B 272
REMARK 465 SER B 273
REMARK 465 ALA B 274
REMARK 465 ALA B 275
REMARK 465 GLY B 276
REMARK 465 PRO B 277
REMARK 465 THR B 278
REMARK 465 GLN B 279
REMARK 465 ALA C 38
REMARK 465 PRO C 39
REMARK 465 ALA C 218
REMARK 465 ALA C 219
REMARK 465 ALA C 220
REMARK 465 LEU C 221
REMARK 465 GLY D 121
REMARK 465 ALA D 122
REMARK 465 PHE D 123
REMARK 465 LEU D 124
REMARK 465 GLU D 125
REMARK 465 ALA D 161
REMARK 465 GLN D 162
REMARK 465 ASP D 163
REMARK 465 LYS D 164
REMARK 465 GLN D 165
REMARK 465 PRO D 166
REMARK 465 ARG D 167
REMARK 465 GLY D 266
REMARK 465 GLY D 267
REMARK 465 THR D 268
REMARK 465 GLY D 269
REMARK 465 THR D 270
REMARK 465 TYR D 271
REMARK 465 ALA D 272
REMARK 465 SER D 273
REMARK 465 ALA D 274
REMARK 465 ALA D 275
REMARK 465 GLY D 276
REMARK 465 PRO D 277
REMARK 465 THR D 278
REMARK 465 GLN D 279
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 OD1 ASN D 180 O HOH D 301 2.09
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 ASP A 140 61.44 66.16
REMARK 500 PRO A 141 -19.12 -40.28
REMARK 500 TYR A 158 73.02 -154.42
REMARK 500 ASP B 191 -59.58 -124.74
REMARK 500 ASP B 236 79.74 66.95
REMARK 500 HIS B 237 -1.01 64.81
REMARK 500 ALA C 44 -8.75 -59.01
REMARK 500 ARG C 94 150.72 -47.40
REMARK 500 ASP C 140 74.16 -119.14
REMARK 500 ASP D 236 34.83 -82.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 214 GLY A 215 -148.17
REMARK 500 LYS B 235 ASP B 236 129.19
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 C 414 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH D 405 DISTANCE = 5.89 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TXO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MIXED DISULFIDE COMPLEX OF THIOREDOXIN-
REMARK 900 LIKE TLPAS(C110S) AND COPPER CHAPERONE SCOIS(C74S)
DBREF 4TXV A 38 221 UNP P43221 TLPA_BRADU 38 221
DBREF 4TXV B 123 279 UNP H7C6E5 H7C6E5_BRADU 123 279
DBREF 4TXV C 38 221 UNP P43221 TLPA_BRADU 38 221
DBREF 4TXV D 123 279 UNP H7C6E5 H7C6E5_BRADU 123 279
SEQADV 4TXV SER A 110 UNP P43221 CYS 110 ENGINEERED MUTATION
SEQADV 4TXV GLY B 121 UNP H7C6E5 EXPRESSION TAG
SEQADV 4TXV ALA B 122 UNP H7C6E5 EXPRESSION TAG
SEQADV 4TXV SER B 233 UNP H7C6E5 CYS 233 ENGINEERED MUTATION
SEQADV 4TXV SER C 110 UNP P43221 CYS 110 ENGINEERED MUTATION
SEQADV 4TXV GLY D 121 UNP H7C6E5 EXPRESSION TAG
SEQADV 4TXV ALA D 122 UNP H7C6E5 EXPRESSION TAG
SEQADV 4TXV SER D 233 UNP H7C6E5 CYS 233 ENGINEERED MUTATION
SEQRES 1 A 184 ALA PRO THR GLY ASP PRO ALA CYS ARG ALA ALA VAL ALA
SEQRES 2 A 184 THR ALA GLN LYS ILE ALA PRO LEU ALA HIS GLY GLU VAL
SEQRES 3 A 184 ALA ALA LEU THR MET ALA SER ALA PRO LEU LYS LEU PRO
SEQRES 4 A 184 ASP LEU ALA PHE GLU ASP ALA ASP GLY LYS PRO LYS LYS
SEQRES 5 A 184 LEU SER ASP PHE ARG GLY LYS THR LEU LEU VAL ASN LEU
SEQRES 6 A 184 TRP ALA THR TRP CYS VAL PRO SER ARG LYS GLU MET PRO
SEQRES 7 A 184 ALA LEU ASP GLU LEU GLN GLY LYS LEU SER GLY PRO ASN
SEQRES 8 A 184 PHE GLU VAL VAL ALA ILE ASN ILE ASP THR ARG ASP PRO
SEQRES 9 A 184 GLU LYS PRO LYS THR PHE LEU LYS GLU ALA ASN LEU THR
SEQRES 10 A 184 ARG LEU GLY TYR PHE ASN ASP GLN LYS ALA LYS VAL PHE
SEQRES 11 A 184 GLN ASP LEU LYS ALA ILE GLY ARG ALA LEU GLY MET PRO
SEQRES 12 A 184 THR SER VAL LEU VAL ASP PRO GLN GLY CYS GLU ILE ALA
SEQRES 13 A 184 THR ILE ALA GLY PRO ALA GLU TRP ALA SER GLU ASP ALA
SEQRES 14 A 184 LEU LYS LEU ILE ARG ALA ALA THR GLY LYS ALA ALA ALA
SEQRES 15 A 184 ALA LEU
SEQRES 1 B 159 GLY ALA PHE LEU GLU LEU ASP VAL PRO LYS ALA ASP LEU
SEQRES 2 B 159 THR ILE LYS ALA THR GLY LYS GLN TRP TYR TRP SER TYR
SEQRES 3 B 159 ALA TYR PRO ASP ASN GLY LYS PHE GLU PHE ASP SER LEU
SEQRES 4 B 159 MET ALA GLN ASP LYS GLN PRO ARG LEU LEU GLY VAL ASP
SEQRES 5 B 159 ASN GLU MET VAL VAL PRO VAL ASN LYS VAL ILE ARG VAL
SEQRES 6 B 159 GLN VAL THR GLY ALA ASP VAL ILE HIS ALA PHE ALA LEU
SEQRES 7 B 159 PRO ALA PHE GLY VAL LYS ILE ASP ALA ILE PRO GLY ARG
SEQRES 8 B 159 LEU ASN GLU THR TRP PHE LYS ALA ALA LYS THR GLY MET
SEQRES 9 B 159 PHE TYR GLY GLN CYS SER GLU LEU SER GLY LYS ASP HIS
SEQRES 10 B 159 ALA PHE MET PRO ILE ALA ILE ARG VAL VAL GLU ASP LYS
SEQRES 11 B 159 GLU PHE ALA SER TRP VAL GLU THR ALA LYS LYS LYS PHE
SEQRES 12 B 159 ALA SER GLY GLY THR GLY THR TYR ALA SER ALA ALA GLY
SEQRES 13 B 159 PRO THR GLN
SEQRES 1 C 184 ALA PRO THR GLY ASP PRO ALA CYS ARG ALA ALA VAL ALA
SEQRES 2 C 184 THR ALA GLN LYS ILE ALA PRO LEU ALA HIS GLY GLU VAL
SEQRES 3 C 184 ALA ALA LEU THR MET ALA SER ALA PRO LEU LYS LEU PRO
SEQRES 4 C 184 ASP LEU ALA PHE GLU ASP ALA ASP GLY LYS PRO LYS LYS
SEQRES 5 C 184 LEU SER ASP PHE ARG GLY LYS THR LEU LEU VAL ASN LEU
SEQRES 6 C 184 TRP ALA THR TRP CYS VAL PRO SER ARG LYS GLU MET PRO
SEQRES 7 C 184 ALA LEU ASP GLU LEU GLN GLY LYS LEU SER GLY PRO ASN
SEQRES 8 C 184 PHE GLU VAL VAL ALA ILE ASN ILE ASP THR ARG ASP PRO
SEQRES 9 C 184 GLU LYS PRO LYS THR PHE LEU LYS GLU ALA ASN LEU THR
SEQRES 10 C 184 ARG LEU GLY TYR PHE ASN ASP GLN LYS ALA LYS VAL PHE
SEQRES 11 C 184 GLN ASP LEU LYS ALA ILE GLY ARG ALA LEU GLY MET PRO
SEQRES 12 C 184 THR SER VAL LEU VAL ASP PRO GLN GLY CYS GLU ILE ALA
SEQRES 13 C 184 THR ILE ALA GLY PRO ALA GLU TRP ALA SER GLU ASP ALA
SEQRES 14 C 184 LEU LYS LEU ILE ARG ALA ALA THR GLY LYS ALA ALA ALA
SEQRES 15 C 184 ALA LEU
SEQRES 1 D 159 GLY ALA PHE LEU GLU LEU ASP VAL PRO LYS ALA ASP LEU
SEQRES 2 D 159 THR ILE LYS ALA THR GLY LYS GLN TRP TYR TRP SER TYR
SEQRES 3 D 159 ALA TYR PRO ASP ASN GLY LYS PHE GLU PHE ASP SER LEU
SEQRES 4 D 159 MET ALA GLN ASP LYS GLN PRO ARG LEU LEU GLY VAL ASP
SEQRES 5 D 159 ASN GLU MET VAL VAL PRO VAL ASN LYS VAL ILE ARG VAL
SEQRES 6 D 159 GLN VAL THR GLY ALA ASP VAL ILE HIS ALA PHE ALA LEU
SEQRES 7 D 159 PRO ALA PHE GLY VAL LYS ILE ASP ALA ILE PRO GLY ARG
SEQRES 8 D 159 LEU ASN GLU THR TRP PHE LYS ALA ALA LYS THR GLY MET
SEQRES 9 D 159 PHE TYR GLY GLN CYS SER GLU LEU SER GLY LYS ASP HIS
SEQRES 10 D 159 ALA PHE MET PRO ILE ALA ILE ARG VAL VAL GLU ASP LYS
SEQRES 11 D 159 GLU PHE ALA SER TRP VAL GLU THR ALA LYS LYS LYS PHE
SEQRES 12 D 159 ALA SER GLY GLY THR GLY THR TYR ALA SER ALA ALA GLY
SEQRES 13 D 159 PRO THR GLN
FORMUL 5 HOH *444(H2 O)
HELIX 1 AA1 ASP A 42 ALA A 44 5 3
HELIX 2 AA2 CYS A 45 ALA A 56 1 12
HELIX 3 AA3 PRO A 57 ALA A 59 5 3
HELIX 4 AA4 HIS A 60 ALA A 64 5 5
HELIX 5 AA5 SER A 91 ARG A 94 5 4
HELIX 6 AA6 CYS A 107 GLU A 113 1 7
HELIX 7 AA7 GLU A 113 SER A 125 1 13
HELIX 8 AA8 GLU A 142 ALA A 151 1 10
HELIX 9 AA9 ALA A 164 ILE A 173 1 10
HELIX 10 AB1 SER A 203 GLY A 215 1 13
HELIX 11 AB2 PRO B 199 GLY B 202 5 4
HELIX 12 AB3 GLU B 248 PHE B 263 1 16
HELIX 13 AB4 ASP C 42 ALA C 44 5 3
HELIX 14 AB5 CYS C 45 ALA C 56 1 12
HELIX 15 AB6 PRO C 57 ALA C 59 5 3
HELIX 16 AB7 HIS C 60 ALA C 64 5 5
HELIX 17 AB8 SER C 91 ARG C 94 5 4
HELIX 18 AB9 CYS C 107 SER C 125 1 19
HELIX 19 AC1 GLU C 142 ASN C 152 1 11
HELIX 20 AC2 ALA C 164 ILE C 173 1 10
HELIX 21 AC3 SER C 203 GLY C 215 1 13
HELIX 22 AC4 PRO D 199 GLY D 202 5 4
HELIX 23 AC5 GLU D 248 PHE D 263 1 16
SHEET 1 AA1 6 THR A 67 MET A 68 0
SHEET 2 AA1 6 GLU A 191 ILE A 195 -1 O THR A 194 N THR A 67
SHEET 3 AA1 6 THR A 181 VAL A 185 -1 N LEU A 184 O ILE A 192
SHEET 4 AA1 6 THR A 97 TRP A 103 -1 N VAL A 100 O VAL A 183
SHEET 5 AA1 6 PHE A 129 ASN A 135 1 O ILE A 134 N ASN A 101
SHEET 6 AA1 6 PHE A 159 ASN A 160 1 O PHE A 159 N ASN A 135
SHEET 1 AA2 2 ALA A 79 GLU A 81 0
SHEET 2 AA2 2 PRO A 87 LYS A 89 -1 O LYS A 88 N PHE A 80
SHEET 1 AA3 5 GLU B 155 SER B 158 0
SHEET 2 AA3 5 TYR B 143 ALA B 147 -1 N TRP B 144 O SER B 158
SHEET 3 AA3 5 LEU B 133 LYS B 140 -1 N THR B 138 O SER B 145
SHEET 4 AA3 5 VAL B 182 GLY B 189 1 O ARG B 184 N LEU B 133
SHEET 5 AA3 5 ASN B 213 LYS B 218 -1 O PHE B 217 N ILE B 183
SHEET 1 AA4 3 MET B 175 PRO B 178 0
SHEET 2 AA4 3 ALA B 243 VAL B 247 1 O ALA B 243 N MET B 175
SHEET 3 AA4 3 GLY B 223 TYR B 226 -1 N GLY B 223 O VAL B 246
SHEET 1 AA5 2 HIS B 194 LEU B 198 0
SHEET 2 AA5 2 VAL B 203 ALA B 207 -1 O ILE B 205 N PHE B 196
SHEET 1 AA6 6 THR C 67 MET C 68 0
SHEET 2 AA6 6 GLU C 191 ILE C 195 -1 O THR C 194 N THR C 67
SHEET 3 AA6 6 THR C 181 VAL C 185 -1 N SER C 182 O ILE C 195
SHEET 4 AA6 6 THR C 97 TRP C 103 -1 N VAL C 100 O VAL C 183
SHEET 5 AA6 6 PHE C 129 ASN C 135 1 O ILE C 134 N ASN C 101
SHEET 6 AA6 6 PHE C 159 ASN C 160 1 O PHE C 159 N ASN C 135
SHEET 1 AA7 2 ALA C 79 GLU C 81 0
SHEET 2 AA7 2 PRO C 87 LYS C 89 -1 O LYS C 88 N PHE C 80
SHEET 1 AA8 2 GLY C 178 MET C 179 0
SHEET 2 AA8 2 CYS D 229 SER D 230 -1 O CYS D 229 N MET C 179
SHEET 1 AA9 5 GLU D 155 SER D 158 0
SHEET 2 AA9 5 TYR D 143 ALA D 147 -1 N TRP D 144 O SER D 158
SHEET 3 AA9 5 LEU D 133 LYS D 140 -1 N THR D 138 O SER D 145
SHEET 4 AA9 5 VAL D 182 GLY D 189 1 O GLN D 186 N ALA D 137
SHEET 5 AA9 5 ASN D 213 LYS D 218 -1 O PHE D 217 N ILE D 183
SHEET 1 AB1 3 MET D 175 PRO D 178 0
SHEET 2 AB1 3 ALA D 243 VAL D 247 1 O ALA D 243 N MET D 175
SHEET 3 AB1 3 GLY D 223 TYR D 226 -1 N GLY D 223 O VAL D 246
SHEET 1 AB2 2 HIS D 194 LEU D 198 0
SHEET 2 AB2 2 VAL D 203 ALA D 207 -1 O ILE D 205 N PHE D 196
SSBOND 1 CYS A 45 CYS A 190 1555 1555 2.11
SSBOND 2 CYS A 107 CYS B 229 1555 1555 2.95
SSBOND 3 CYS C 45 CYS C 190 1555 1555 2.03
SSBOND 4 CYS C 107 CYS D 229 1555 1555 2.94
CISPEP 1 MET A 179 PRO A 180 0 -7.74
CISPEP 2 GLN B 141 TRP B 142 0 -5.40
CISPEP 3 GLN B 165 PRO B 166 0 4.66
CISPEP 4 MET C 179 PRO C 180 0 -7.92
CISPEP 5 GLN D 141 TRP D 142 0 -5.14
CRYST1 74.830 81.640 109.370 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 0.013364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009143 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
