HEADER OXIDOREDUCTASE 13-JUL-12 4G38
TITLE MUTATIONAL ANALYSIS OF SULFITE REDUCTASE HEMOPROTEIN REVEALS THE
TITLE 2 MECHANISM FOR COORDINATED ELECTRON AND PROTON TRANSFER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SULFITE REDUCTASE [NADPH] HEMOPROTEIN BETA-COMPONENT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SULFITE REDUCTASE HEMOPROTEIN (UNP RESIDUES 74-570);
COMPND 5 SYNONYM: SIR-HP, SIRHP;
COMPND 6 EC: 1.8.1.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2763, CYSI, JW2733;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: LMG194;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD/MYC-HISA
KEYWDS SNIRR, OXIDOREDUCTASE, SULFITE REDUCTASE FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.W.SMITH,M.E.STROUPE
REVDAT 4 28-FEB-24 4G38 1 COMPND REMARK SEQADV FORMUL
REVDAT 4 2 1 LINK
REVDAT 3 17-JUL-19 4G38 1 REMARK
REVDAT 2 06-MAR-13 4G38 1 JRNL
REVDAT 1 26-DEC-12 4G38 0
JRNL AUTH K.W.SMITH,M.E.STROUPE
JRNL TITL MUTATIONAL ANALYSIS OF SULFITE REDUCTASE HEMOPROTEIN REVEALS
JRNL TITL 2 THE MECHANISM FOR COORDINATED ELECTRON AND PROTON TRANSFER.
JRNL REF BIOCHEMISTRY V. 51 9857 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 23153334
JRNL DOI 10.1021/BI300947A
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 57746
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.450
REMARK 3 FREE R VALUE TEST SET COUNT : 1993
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 22.7698 - 3.7536 0.99 4314 155 0.1512 0.1931
REMARK 3 2 3.7536 - 2.9815 1.00 4162 150 0.1474 0.1639
REMARK 3 3 2.9815 - 2.6052 0.99 4094 150 0.1571 0.1753
REMARK 3 4 2.6052 - 2.3673 0.99 4051 148 0.1443 0.1919
REMARK 3 5 2.3673 - 2.1978 0.99 4035 154 0.1359 0.1673
REMARK 3 6 2.1978 - 2.0683 0.99 4047 132 0.1352 0.1696
REMARK 3 7 2.0683 - 1.9648 0.98 4003 143 0.1311 0.1672
REMARK 3 8 1.9648 - 1.8793 0.97 3956 141 0.1229 0.1671
REMARK 3 9 1.8793 - 1.8070 0.97 3921 142 0.1191 0.1761
REMARK 3 10 1.8070 - 1.7446 0.96 3894 135 0.1160 0.1735
REMARK 3 11 1.7446 - 1.6901 0.96 3889 141 0.1182 0.1693
REMARK 3 12 1.6901 - 1.6418 0.95 3836 134 0.1229 0.1927
REMARK 3 13 1.6418 - 1.5986 0.95 3831 139 0.1391 0.1916
REMARK 3 14 1.5986 - 1.5596 0.92 3720 129 0.1520 0.2061
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 43.05
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.94170
REMARK 3 B22 (A**2) : -2.97550
REMARK 3 B33 (A**2) : -1.96620
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 3726
REMARK 3 ANGLE : 1.656 5071
REMARK 3 CHIRALITY : 0.083 546
REMARK 3 PLANARITY : 0.006 658
REMARK 3 DIHEDRAL : 14.529 1380
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073681.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57746
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.21400
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 24.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 65 MM KPI/22% PEG 8000, PH 7.6, VAPOR
REMARK 280 DIFFUSION, HANGING 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 33.16350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.73150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.08550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.73150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.16350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.08550
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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 HIS A 5
REMARK 465 PRO A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 8
REMARK 465 LEU A 9
REMARK 465 VAL A 10
REMARK 465 VAL A 11
REMARK 465 GLU A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 LEU A 15
REMARK 465 THR A 16
REMARK 465 ASP A 17
REMARK 465 ALA A 18
REMARK 465 GLU A 19
REMARK 465 ARG A 20
REMARK 465 MET A 21
REMARK 465 LYS A 22
REMARK 465 HIS A 23
REMARK 465 GLU A 24
REMARK 465 SER A 25
REMARK 465 ASN A 26
REMARK 465 TYR A 27
REMARK 465 LEU A 28
REMARK 465 ARG A 29
REMARK 465 GLY A 30
REMARK 465 THR A 31
REMARK 465 ILE A 32
REMARK 465 ALA A 33
REMARK 465 GLU A 34
REMARK 465 ASP A 35
REMARK 465 LEU A 36
REMARK 465 ASN A 37
REMARK 465 ASP A 38
REMARK 465 GLY A 39
REMARK 465 LEU A 40
REMARK 465 THR A 41
REMARK 465 GLY A 42
REMARK 465 GLY A 43
REMARK 465 PHE A 44
REMARK 465 LYS A 45
REMARK 465 GLY A 46
REMARK 465 ASP A 47
REMARK 465 ASN A 48
REMARK 465 PHE A 49
REMARK 465 LEU A 50
REMARK 465 LEU A 51
REMARK 465 ILE A 52
REMARK 465 ARG A 53
REMARK 465 PHE A 54
REMARK 465 HIS A 55
REMARK 465 GLY A 56
REMARK 465 MET A 57
REMARK 465 TYR A 58
REMARK 465 GLN A 59
REMARK 465 GLN A 60
REMARK 465 ASP A 61
REMARK 465 ASP A 62
REMARK 465 ARG A 63
REMARK 465 ASP A 64
REMARK 465 ILE A 65
REMARK 465 ARG A 66
REMARK 465 ALA A 67
REMARK 465 GLU A 68
REMARK 465 ARG A 69
REMARK 465 ALA A 70
REMARK 465 GLU A 71
REMARK 465 GLN A 72
REMARK 465 LYS A 73
REMARK 465 LEU A 74
REMARK 465 GLU A 75
REMARK 465 PRO A 76
REMARK 465 ARG A 77
REMARK 465 HIS A 78
REMARK 465 ALA A 79
REMARK 465 MET A 80
REMARK 465 LYS A 127
REMARK 465 LYS A 128
REMARK 465 ASN A 129
REMARK 465 VAL A 130
REMARK 465 LYS A 131
REMARK 465 ARG A 184
REMARK 465 THR A 185
REMARK 465 ARG A 186
REMARK 465 ALA A 187
REMARK 465 TYR A 188
REMARK 465 ALA A 189
REMARK 465 GLU A 190
REMARK 465 ILE A 191
REMARK 465 TRP A 192
REMARK 465 LEU A 193
REMARK 465 ASP A 194
REMARK 465 GLN A 195
REMARK 465 GLU A 196
REMARK 465 LYS A 197
REMARK 465 VAL A 198
REMARK 465 ALA A 199
REMARK 465 THR A 200
REMARK 465 THR A 201
REMARK 465 ASP A 202
REMARK 465 GLU A 203
REMARK 465 GLU A 204
REMARK 465 PRO A 205
REMARK 465 ILE A 206
REMARK 465 LEU A 207
REMARK 465 GLY A 208
REMARK 465 GLN A 209
REMARK 465 THR A 210
REMARK 465 TYR A 211
REMARK 465 LEU A 212
REMARK 465 PRO A 213
REMARK 465 ARG A 214
REMARK 465 ARG A 299
REMARK 465 THR A 300
REMARK 465 ASP A 301
REMARK 465 ARG A 302
REMARK 465 LYS A 303
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 A 152 O HOH A 1120 1.99
REMARK 500 OE1 GLU A 417 O HOH A 1121 2.04
REMARK 500 ND2 ASN A 243 O HOH A 1118 2.16
REMARK 500 O HOH A 1118 O HOH A 1119 2.18
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 LEU A 86 74.07 -160.35
REMARK 500 ASN A 243 40.80 102.79
REMARK 500 ASP A 353 -124.60 69.47
REMARK 500 ASN A 364 14.42 59.01
REMARK 500 ALA A 372 -4.84 75.34
REMARK 500 SER A 436 -146.14 54.86
REMARK 500 ALA A 447 -75.62 -131.16
REMARK 500 ASP A 563 76.69 -159.54
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 ALA A 241 GLU A 242 143.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 602 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 362 O
REMARK 620 2 ASN A 395 O 137.5
REMARK 620 3 ASN A 397 OD1 76.5 87.8
REMARK 620 4 HOH A 702 O 87.6 120.5 149.5
REMARK 620 5 HOH A 749 O 137.3 74.4 78.1 97.5
REMARK 620 6 HOH A 816 O 152.6 64.8 126.9 65.0 51.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 603 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 434 SG
REMARK 620 2 SF4 A 603 S2 112.0
REMARK 620 3 SF4 A 603 S3 106.8 109.1
REMARK 620 4 SF4 A 603 S4 123.7 101.9 102.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 603 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 440 SG
REMARK 620 2 SF4 A 603 S1 105.1
REMARK 620 3 SF4 A 603 S3 122.7 100.9
REMARK 620 4 SF4 A 603 S4 119.1 105.0 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 603 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 479 SG
REMARK 620 2 SF4 A 603 S1 106.1
REMARK 620 3 SF4 A 603 S2 120.1 101.4
REMARK 620 4 SF4 A 603 S4 121.1 104.9 100.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 603 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 483 SG
REMARK 620 2 SF4 A 603 S1 122.4
REMARK 620 3 SF4 A 603 S2 103.1 102.2
REMARK 620 4 SF4 A 603 S3 117.4 102.5 107.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SRM A 604 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 A 601 O1
REMARK 620 2 SRM A 604 NA 93.8
REMARK 620 3 SRM A 604 NB 83.4 91.0
REMARK 620 4 SRM A 604 NC 98.6 167.3 87.8
REMARK 620 5 SRM A 604 ND 105.1 88.3 171.5 91.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM A 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AOP RELATED DB: PDB
REMARK 900 WILD-TYPE SULFITE REDUCTASE HEMOPROTEIN
REMARK 900 RELATED ID: 4G39 RELATED DB: PDB
DBREF 4G38 A 74 570 UNP P17846 CYSI_ECOLI 74 570
SEQADV 4G38 TRP A 149 UNP P17846 ASN 149 ENGINEERED MUTATION
SEQRES 1 A 570 MET SER GLU LYS HIS PRO GLY PRO LEU VAL VAL GLU GLY
SEQRES 2 A 570 LYS LEU THR ASP ALA GLU ARG MET LYS HIS GLU SER ASN
SEQRES 3 A 570 TYR LEU ARG GLY THR ILE ALA GLU ASP LEU ASN ASP GLY
SEQRES 4 A 570 LEU THR GLY GLY PHE LYS GLY ASP ASN PHE LEU LEU ILE
SEQRES 5 A 570 ARG PHE HIS GLY MET TYR GLN GLN ASP ASP ARG ASP ILE
SEQRES 6 A 570 ARG ALA GLU ARG ALA GLU GLN LYS LEU GLU PRO ARG HIS
SEQRES 7 A 570 ALA MET LEU LEU ARG CYS ARG LEU PRO GLY GLY VAL ILE
SEQRES 8 A 570 THR THR LYS GLN TRP GLN ALA ILE ASP LYS PHE ALA GLY
SEQRES 9 A 570 GLU ASN THR ILE TYR GLY SER ILE ARG LEU THR ASN ARG
SEQRES 10 A 570 GLN THR PHE GLN PHE HIS GLY ILE LEU LYS LYS ASN VAL
SEQRES 11 A 570 LYS PRO VAL HIS GLN MET LEU HIS SER VAL GLY LEU ASP
SEQRES 12 A 570 ALA LEU ALA THR ALA TRP ASP MET ASN ARG ASN VAL LEU
SEQRES 13 A 570 CYS THR SER ASN PRO TYR GLU SER GLN LEU HIS ALA GLU
SEQRES 14 A 570 ALA TYR GLU TRP ALA LYS LYS ILE SER GLU HIS LEU LEU
SEQRES 15 A 570 PRO ARG THR ARG ALA TYR ALA GLU ILE TRP LEU ASP GLN
SEQRES 16 A 570 GLU LYS VAL ALA THR THR ASP GLU GLU PRO ILE LEU GLY
SEQRES 17 A 570 GLN THR TYR LEU PRO ARG LYS PHE LYS THR THR VAL VAL
SEQRES 18 A 570 ILE PRO PRO GLN ASN ASP ILE ASP LEU HIS ALA ASN ASP
SEQRES 19 A 570 MET ASN PHE VAL ALA ILE ALA GLU ASN GLY LYS LEU VAL
SEQRES 20 A 570 GLY PHE ASN LEU LEU VAL GLY GLY GLY LEU SER ILE GLU
SEQRES 21 A 570 HIS GLY ASN LYS LYS THR TYR ALA ARG THR ALA SER GLU
SEQRES 22 A 570 PHE GLY TYR LEU PRO LEU GLU HIS THR LEU ALA VAL ALA
SEQRES 23 A 570 GLU ALA VAL VAL THR THR GLN ARG ASP TRP GLY ASN ARG
SEQRES 24 A 570 THR ASP ARG LYS ASN ALA LYS THR LYS TYR THR LEU GLU
SEQRES 25 A 570 ARG VAL GLY VAL GLU THR PHE LYS ALA GLU VAL GLU ARG
SEQRES 26 A 570 ARG ALA GLY ILE LYS PHE GLU PRO ILE ARG PRO TYR GLU
SEQRES 27 A 570 PHE THR GLY ARG GLY ASP ARG ILE GLY TRP VAL LYS GLY
SEQRES 28 A 570 ILE ASP ASP ASN TRP HIS LEU THR LEU PHE ILE GLU ASN
SEQRES 29 A 570 GLY ARG ILE LEU ASP TYR PRO ALA ARG PRO LEU LYS THR
SEQRES 30 A 570 GLY LEU LEU GLU ILE ALA LYS ILE HIS LYS GLY ASP PHE
SEQRES 31 A 570 ARG ILE THR ALA ASN GLN ASN LEU ILE ILE ALA GLY VAL
SEQRES 32 A 570 PRO GLU SER GLU LYS ALA LYS ILE GLU LYS ILE ALA LYS
SEQRES 33 A 570 GLU SER GLY LEU MET ASN ALA VAL THR PRO GLN ARG GLU
SEQRES 34 A 570 ASN SER MET ALA CYS VAL SER PHE PRO THR CYS PRO LEU
SEQRES 35 A 570 ALA MET ALA GLU ALA GLU ARG PHE LEU PRO SER PHE ILE
SEQRES 36 A 570 ASP ASN ILE ASP ASN LEU MET ALA LYS HIS GLY VAL SER
SEQRES 37 A 570 ASP GLU HIS ILE VAL MET ARG VAL THR GLY CYS PRO ASN
SEQRES 38 A 570 GLY CYS GLY ARG ALA MET LEU ALA GLU VAL GLY LEU VAL
SEQRES 39 A 570 GLY LYS ALA PRO GLY ARG TYR ASN LEU HIS LEU GLY GLY
SEQRES 40 A 570 ASN ARG ILE GLY THR ARG ILE PRO ARG MET TYR LYS GLU
SEQRES 41 A 570 ASN ILE THR GLU PRO GLU ILE LEU ALA SER LEU ASP GLU
SEQRES 42 A 570 LEU ILE GLY ARG TRP ALA LYS GLU ARG GLU ALA GLY GLU
SEQRES 43 A 570 GLY PHE GLY ASP PHE THR VAL ARG ALA GLY ILE ILE ARG
SEQRES 44 A 570 PRO VAL LEU ASP PRO ALA ARG ASP LEU TRP ASP
HET PO4 A 601 5
HET K A 602 1
HET SF4 A 603 8
HET SRM A 604 63
HETNAM PO4 PHOSPHATE ION
HETNAM K POTASSIUM ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM SRM SIROHEME
FORMUL 2 PO4 O4 P 3-
FORMUL 3 K K 1+
FORMUL 4 SF4 FE4 S4
FORMUL 5 SRM C42 H44 FE N4 O16
FORMUL 6 HOH *564(H2 O)
HELIX 1 1 LEU A 86 GLY A 88 5 3
HELIX 2 2 THR A 93 THR A 107 1 15
HELIX 3 3 VAL A 133 SER A 139 1 7
HELIX 4 4 GLU A 163 GLN A 165 5 3
HELIX 5 5 LEU A 166 LEU A 181 1 16
HELIX 6 6 ASP A 229 ASN A 233 5 5
HELIX 7 7 HIS A 281 GLY A 297 1 17
HELIX 8 8 LYS A 306 GLY A 315 1 10
HELIX 9 9 GLY A 315 GLY A 328 1 14
HELIX 10 10 ILE A 362 ASN A 364 5 3
HELIX 11 11 LEU A 375 HIS A 386 1 12
HELIX 12 12 GLU A 407 SER A 418 1 12
HELIX 13 13 THR A 425 ASN A 430 1 6
HELIX 14 14 PHE A 450 HIS A 465 1 16
HELIX 15 15 ARG A 485 ALA A 489 5 5
HELIX 16 16 GLU A 524 ARG A 542 1 19
HELIX 17 17 GLY A 547 ALA A 555 1 9
HELIX 18 18 ASP A 563 LEU A 568 1 6
SHEET 1 A 2 CYS A 84 ARG A 85 0
SHEET 2 A 2 ASP A 143 ALA A 144 -1 O ASP A 143 N ARG A 85
SHEET 1 B 5 VAL A 90 THR A 92 0
SHEET 2 B 5 ASP A 389 ILE A 392 -1 O PHE A 390 N ILE A 91
SHEET 3 B 5 LEU A 398 PRO A 404 -1 O ILE A 399 N ARG A 391
SHEET 4 B 5 ASN A 355 LEU A 360 -1 N LEU A 358 O ILE A 400
SHEET 5 B 5 GLY A 347 LYS A 350 -1 N GLY A 347 O THR A 359
SHEET 1 C 3 PHE A 120 GLN A 121 0
SHEET 2 C 3 ILE A 112 LEU A 114 -1 N ARG A 113 O GLN A 121
SHEET 3 C 3 ARG A 366 ILE A 367 -1 O ILE A 367 N ILE A 112
SHEET 1 D 5 LEU A 156 CYS A 157 0
SHEET 2 D 5 THR A 218 VAL A 221 1 O VAL A 220 N LEU A 156
SHEET 3 D 5 MET A 235 ALA A 241 1 O ALA A 239 N VAL A 221
SHEET 4 D 5 LEU A 246 VAL A 253 -1 O ASN A 250 N VAL A 238
SHEET 5 D 5 SER A 272 PRO A 278 -1 O SER A 272 N VAL A 253
SHEET 1 E 2 ASP A 369 TYR A 370 0
SHEET 2 E 2 ARG A 373 PRO A 374 -1 O ARG A 373 N TYR A 370
SHEET 1 F 5 SER A 431 ALA A 433 0
SHEET 2 F 5 MET A 474 THR A 477 1 O VAL A 476 N MET A 432
SHEET 3 F 5 VAL A 491 ALA A 497 1 O GLY A 495 N THR A 477
SHEET 4 F 5 ARG A 500 LEU A 505 -1 O HIS A 504 N GLY A 492
SHEET 5 F 5 ARG A 516 THR A 523 -1 O TYR A 518 N LEU A 503
LINK O ILE A 362 K K A 602 1555 1555 2.86
LINK O ASN A 395 K K A 602 1555 1555 2.78
LINK OD1 ASN A 397 K K A 602 1555 1555 2.78
LINK SG CYS A 434 FE1 SF4 A 603 1555 1555 2.35
LINK SG CYS A 440 FE2 SF4 A 603 1555 1555 2.29
LINK SG CYS A 479 FE3 SF4 A 603 1555 1555 2.31
LINK SG CYS A 483 FE4 SF4 A 603 1555 1555 2.22
LINK O1 PO4 A 601 FE SRM A 604 1555 1555 2.09
LINK K K A 602 O HOH A 702 1555 1555 2.86
LINK K K A 602 O HOH A 749 1555 1555 3.24
LINK K K A 602 O HOH A 816 1555 1555 2.99
CISPEP 1 PRO A 223 PRO A 224 0 8.42
CISPEP 2 PHE A 437 PRO A 438 0 10.15
SITE 1 AC1 7 ARG A 83 ARG A 117 ARG A 153 LYS A 215
SITE 2 AC1 7 LYS A 217 SRM A 604 HOH A 908
SITE 1 AC2 6 ILE A 362 ASN A 395 GLN A 396 ASN A 397
SITE 2 AC2 6 HOH A 702 HOH A 816
SITE 1 AC3 9 CYS A 434 CYS A 440 ALA A 443 THR A 477
SITE 2 AC3 9 GLY A 478 CYS A 479 ASN A 481 GLY A 482
SITE 3 AC3 9 CYS A 483
SITE 1 AC4 38 LEU A 81 ARG A 83 ARG A 113 THR A 115
SITE 2 AC4 38 ASN A 116 ARG A 117 THR A 119 GLN A 121
SITE 3 AC4 38 HIS A 123 LYS A 215 LYS A 217 GLY A 256
SITE 4 AC4 38 LEU A 257 SER A 258 GLN A 396 ALA A 433
SITE 5 AC4 38 CYS A 434 VAL A 435 THR A 439 CYS A 440
SITE 6 AC4 38 PRO A 441 LEU A 442 ASN A 481 GLY A 482
SITE 7 AC4 38 CYS A 483 ARG A 485 PO4 A 601 HOH A 731
SITE 8 AC4 38 HOH A 743 HOH A 792 HOH A 810 HOH A 912
SITE 9 AC4 38 HOH A 925 HOH A 936 HOH A1108 HOH A1158
SITE 10 AC4 38 HOH A1205 HOH A1254
CRYST1 66.327 76.171 81.463 90.00 90.00 90.00 P 21 21 21 4
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 0.015077 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013128 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012276 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
