HEADER ADOMET BINDING PROTEIN 03-AUG-09 3IIX
TITLE X-RAY STRUCTURE OF THE FEFE-HYDROGENASE MATURASE HYDE FROM T. MARITIMA
TITLE 2 IN COMPLEX WITH METHIONINE AND 5'DEOXYADENOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: [FEFE] HYDROGENASE MATURASE SUBUNIT HYDE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.8.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA MSB8;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 GENE: TM_1269, THEMA_07990, TMARI_1274;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ADOMET RADICAL, SAM RADICAL, ADOMET CLEAVAGE, FE4S4 CLUSTER, HYDE,
KEYWDS 2 HYDROGENASE, MATURATION, BETA BARREL, DEOXYADENOSINE, ADOMET BINDING
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NICOLET,P.AMARA,J.M.MOUESCA,J.C.FONTECILLA-CAMPS
REVDAT 4 22-NOV-23 3IIX 1 REMARK
REVDAT 3 08-NOV-23 3IIX 1 REMARK
REVDAT 2 12-APR-23 3IIX 1 COMPND SOURCE REMARK DBREF
REVDAT 2 2 1 SEQADV SEQRES HET HETNAM
REVDAT 2 3 1 HETSYN FORMUL LINK SITE
REVDAT 2 4 1 ATOM
REVDAT 1 22-SEP-09 3IIX 0
JRNL AUTH Y.NICOLET,P.AMARA,J.-M.MOUESCA,J.C.FONTECILLA-CAMPS
JRNL TITL UNEXPECTED ELECTRON TRANSFER MECHANISM UPON ADOMET CLEAVAGE
JRNL TITL 2 IN RADICAL SAM PROTEINS
JRNL REF PROC.NATL.ACAD.SCI.USA 2009
JRNL REFN ESSN 1091-6490
JRNL PMID 19706452
JRNL DOI 10.1073/PNAS.0904385106
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 88534
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4675
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) : 1.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4903
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 250
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2739
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 466
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.78000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.74000
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): 0.045
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.043
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.439
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3167 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2260 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4364 ; 1.675 ; 2.068
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5557 ; 1.256 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 394 ;18.802 ; 5.152
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;33.744 ;23.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 558 ;12.431 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;15.557 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 519 ; 0.146 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3302 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 595 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 657 ; 0.254 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2675 ; 0.205 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1581 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1630 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 358 ; 0.184 ; 0.200
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): 9 ; 0.087 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 82 ; 0.243 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 41 ; 0.164 ; 0.200
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): 1857 ; 1.234 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 722 ; 0.498 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2964 ; 1.730 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1456 ; 2.366 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1366 ; 3.156 ; 4.500
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): 5925 ; 1.365 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 475 ; 5.033 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5330 ; 2.594 ; 3.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. THE FRIEDEL MATES HAVE BEEN SEPARATED
REMARK 3 DURING DATA PROCESSING TO EXTRACT THE ANOMALOUS SIGNAL.
REMARK 4
REMARK 4 3IIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054468.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88534
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 58.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.46
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3CIW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LISO4, TRIS PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 25.52700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.09600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.46250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.09600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.52700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.46250
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 VAL A 348
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 MET A 1 CG SD CE
REMARK 470 ARG A 4 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 5 CD OE1 OE2
REMARK 470 GLU A 8 CD OE1 OE2
REMARK 470 LYS A 9 CE NZ
REMARK 470 ARG A 12 NE CZ NH1 NH2
REMARK 470 GLU A 14 CG CD OE1 OE2
REMARK 470 ARG A 29 CZ NH1 NH2
REMARK 470 LYS A 37 CE NZ
REMARK 470 GLU A 143 CD OE1 OE2
REMARK 470 LYS A 188 CD CE NZ
REMARK 470 LYS A 242 CE NZ
REMARK 470 LYS A 243 CE NZ
REMARK 470 LYS A 315 CE NZ
REMARK 470 LYS A 333 CD CE NZ
REMARK 470 ARG A 336 CD NE CZ NH1 NH2
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 O HOH A 615 O HOH A 750 2.01
REMARK 500 OE1 GLU A 150 O HOH A 754 2.08
REMARK 500 O HOH A 715 O HOH A 717 2.11
REMARK 500 O HOH A 358 O HOH A 622 2.14
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 ASN A 78 48.62 -88.28
REMARK 500 ASN A 78 48.19 -88.20
REMARK 500 GLU A 161 -58.67 77.88
REMARK 500 THR A 175 -155.27 -151.98
REMARK 500 ALA A 196 -154.80 -120.92
REMARK 500 ASP A 235 30.45 -98.69
REMARK 500 ASN A 288 13.49 -141.43
REMARK 500 TYR A 303 79.29 -115.34
REMARK 500 LYS A 309 119.91 -39.51
REMARK 500 ASP A 337 -161.20 -128.38
REMARK 500 GLU A 346 -156.76 -140.60
REMARK 500 GLU A 346 -158.05 -139.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CPS A 1702
REMARK 610 CPS A 1703
REMARK 610 CPS A 1704
REMARK 610 CPS A 1705
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 SF4 A2460 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 63 SG
REMARK 620 2 SF4 A2460 S1 114.0
REMARK 620 3 SF4 A2460 S2 119.5 105.6
REMARK 620 4 SF4 A2460 S4 106.5 104.1 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 SG
REMARK 620 2 SF4 A2460 S2 106.7
REMARK 620 3 SF4 A2460 S3 116.8 105.8
REMARK 620 4 SF4 A2460 S4 118.8 104.5 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2460 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 70 SG
REMARK 620 2 SF4 A2460 S1 120.3
REMARK 620 3 SF4 A2460 S2 110.8 105.2
REMARK 620 4 SF4 A2460 S3 108.6 105.1 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A2460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A1401 N
REMARK 620 2 SF4 A2460 S1 93.0
REMARK 620 3 SF4 A2460 S3 162.8 99.8
REMARK 620 4 SF4 A2460 S4 92.3 97.2 97.5
REMARK 620 5 MET A1401 SD 80.8 87.7 88.2 171.8
REMARK 620 6 MET A1401 OXT 72.0 162.6 93.3 92.4 81.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MET A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5AD A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 1704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 1705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HOH A 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HOH A 354
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CIW RELATED DB: PDB
REMARK 900 RELATED ID: 3CIX RELATED DB: PDB
REMARK 900 RELATED ID: 3IIZ RELATED DB: PDB
DBREF 3IIX A 1 348 UNP Q9X0Z6 HYDE_THEMA 1 348
SEQADV 3IIX OTY A 114 UNP Q9X0Z6 TYR 114 MODIFIED RESIDUE
SEQRES 1 A 348 MET THR GLY ARG GLU ILE LEU GLU LYS LEU GLU ARG ARG
SEQRES 2 A 348 GLU PHE THR ARG GLU VAL LEU LYS GLU ALA LEU SER ILE
SEQRES 3 A 348 ASN ASP ARG GLY PHE ASN GLU ALA LEU PHE LYS LEU ALA
SEQRES 4 A 348 ASP GLU ILE ARG ARG LYS TYR VAL GLY ASP GLU VAL HIS
SEQRES 5 A 348 ILE ARG ALA ILE ILE GLU PHE SER ASN VAL CYS ARG LYS
SEQRES 6 A 348 ASN CYS LEU TYR CYS GLY LEU ARG ARG ASP ASN LYS ASN
SEQRES 7 A 348 LEU LYS ARG TYR ARG MET THR PRO GLU GLU ILE VAL GLU
SEQRES 8 A 348 ARG ALA ARG LEU ALA VAL GLN PHE GLY ALA LYS THR ILE
SEQRES 9 A 348 VAL LEU GLN SER GLY GLU ASP PRO TYR OTY MET PRO ASP
SEQRES 10 A 348 VAL ILE SER ASP ILE VAL LYS GLU ILE LYS LYS MET GLY
SEQRES 11 A 348 VAL ALA VAL THR LEU SER LEU GLY GLU TRP PRO ARG GLU
SEQRES 12 A 348 TYR TYR GLU LYS TRP LYS GLU ALA GLY ALA ASP ARG TYR
SEQRES 13 A 348 LEU LEU ARG HIS GLU THR ALA ASN PRO VAL LEU HIS ARG
SEQRES 14 A 348 LYS LEU ARG PRO ASP THR SER PHE GLU ASN ARG LEU ASN
SEQRES 15 A 348 CSO LEU LEU THR LEU LYS GLU LEU GLY TYR GLU THR GLY
SEQRES 16 A 348 ALA GLY SER MET VAL GLY LEU PRO GLY GLN THR ILE ASP
SEQRES 17 A 348 ASP LEU VAL ASP ASP LEU LEU PHE LEU LYS GLU HIS ASP
SEQRES 18 A 348 PHE ASP MET VAL GLY ILE GLY PRO PHE ILE PRO HIS PRO
SEQRES 19 A 348 ASP THR PRO LEU ALA ASN GLU LYS LYS GLY ASP PHE THR
SEQRES 20 A 348 LEU THR LEU LYS MET VAL ALA LEU THR ARG ILE LEU LEU
SEQRES 21 A 348 PRO ASP SER ASN ILE PRO ALA THR THR ALA MET GLY THR
SEQRES 22 A 348 ILE VAL PRO GLY GLY ARG GLU ILE THR LEU ARG CYS GLY
SEQRES 23 A 348 ALA ASN VAL ILE MET PRO ASN TRP THR PRO SER PRO TYR
SEQRES 24 A 348 ARG GLN LEU TYR GLN LEU TYR PRO GLY LYS ILE CSS VAL
SEQRES 25 A 348 PHE GLU LYS ASP THR ALA CYS ILE PRO CSO VAL MET LYS
SEQRES 26 A 348 MET ILE GLU LEU LEU GLY ARG LYS PRO GLY ARG ASP TRP
SEQRES 27 A 348 GLY GLY ARG LYS ARG VAL PHE GLU THR VAL
MODRES 3IIX CSO A 183 CYS MODIFIED RESIDUE
MODRES 3IIX CSS A 311 CYS MODIFIED RESIDUE
MODRES 3IIX CSO A 322 CYS MODIFIED RESIDUE
HET OTY A 114 13
HET CSO A 183 7
HET CSS A 311 7
HET CSO A 322 10
HET SF4 A2460 8
HET MET A1401 9
HET 5AD A1501 18
HET CPS A1701 42
HET CPS A1702 35
HET CPS A1703 29
HET CPS A1704 25
HET CPS A1705 22
HET S3H A1801 3
HET CL A 349 1
HET CL A 350 1
HET CL A 351 2
HET CO3 A 352 4
HETNAM OTY 2-HYDROXY-L-TYROSINE
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM CSS S-MERCAPTOCYSTEINE
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM MET METHIONINE
HETNAM 5AD 5'-DEOXYADENOSINE
HETNAM CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-
HETNAM 2 CPS PROPANESULFONATE
HETNAM S3H TRISULFANE
HETNAM CL CHLORIDE ION
HETNAM CO3 CARBONATE ION
HETSYN CPS CHAPS
FORMUL 1 OTY C9 H11 N O4
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 1 CSS C3 H7 N O2 S2
FORMUL 2 SF4 FE4 S4
FORMUL 3 MET C5 H11 N O2 S
FORMUL 4 5AD C10 H13 N5 O3
FORMUL 5 CPS 5(C32 H58 N2 O7 S)
FORMUL 10 S3H H2 S3
FORMUL 11 CL 3(CL 1-)
FORMUL 14 CO3 C O3 2-
FORMUL 15 HOH *466(H2 O)
HELIX 1 1 THR A 2 ARG A 12 1 11
HELIX 2 2 THR A 16 ILE A 26 1 11
HELIX 3 3 ASP A 28 GLY A 48 1 21
HELIX 4 4 THR A 85 PHE A 99 1 15
HELIX 5 5 ASP A 111 MET A 115 5 5
HELIX 6 6 PRO A 116 LYS A 128 1 13
HELIX 7 7 PRO A 141 GLY A 152 1 12
HELIX 8 8 ASN A 164 ARG A 172 1 9
HELIX 9 9 SER A 176 LEU A 190 1 15
HELIX 10 10 THR A 206 ASP A 221 1 16
HELIX 11 11 ASP A 245 LEU A 260 1 16
HELIX 12 12 THR A 268 VAL A 275 1 8
HELIX 13 13 GLY A 277 ARG A 284 1 8
HELIX 14 14 TYR A 299 TYR A 303 5 5
HELIX 15 15 ALA A 318 LEU A 330 1 13
SHEET 1 A 7 MET A 224 VAL A 225 0
SHEET 2 A 7 GLU A 193 ALA A 196 1 N ALA A 196 O MET A 224
SHEET 3 A 7 ARG A 155 LEU A 157 1 N TYR A 156 O GLY A 195
SHEET 4 A 7 ALA A 132 SER A 136 1 N LEU A 135 O LEU A 157
SHEET 5 A 7 THR A 103 SER A 108 1 N ILE A 104 O THR A 134
SHEET 6 A 7 GLU A 50 SER A 60 1 N ALA A 55 O VAL A 105
SHEET 7 A 7 VAL A 289 ILE A 290 1 O ILE A 290 N HIS A 52
SHEET 1 B 7 MET A 224 VAL A 225 0
SHEET 2 B 7 GLU A 193 ALA A 196 1 N ALA A 196 O MET A 224
SHEET 3 B 7 ARG A 155 LEU A 157 1 N TYR A 156 O GLY A 195
SHEET 4 B 7 ALA A 132 SER A 136 1 N LEU A 135 O LEU A 157
SHEET 5 B 7 THR A 103 SER A 108 1 N ILE A 104 O THR A 134
SHEET 6 B 7 GLU A 50 SER A 60 1 N ALA A 55 O VAL A 105
SHEET 7 B 7 LYS A 333 PRO A 334 1 O LYS A 333 N VAL A 51
SHEET 1 C 2 MET A 199 VAL A 200 0
SHEET 2 C 2 GLY A 228 PRO A 229 1 O GLY A 228 N VAL A 200
LINK C TYR A 113 N OTY A 114 1555 1555 1.33
LINK C OTY A 114 N MET A 115 1555 1555 1.34
LINK C ASN A 182 N CSO A 183 1555 1555 1.34
LINK C CSO A 183 N LEU A 184 1555 1555 1.33
LINK C ILE A 310 N CSS A 311 1555 1555 1.32
LINK C CSS A 311 N VAL A 312 1555 1555 1.33
LINK SG CYS A 319 S3 S3H A1801 1555 1555 1.96
LINK C PRO A 321 N CSO A 322 1555 1555 1.32
LINK C CSO A 322 N VAL A 323 1555 1555 1.34
LINK SG CYS A 63 FE3 SF4 A2460 1555 1555 2.27
LINK SG CYS A 67 FE1 SF4 A2460 1555 1555 2.32
LINK SG CYS A 70 FE4 SF4 A2460 1555 1555 2.29
LINK N MET A1401 FE2 SF4 A2460 1555 1555 2.24
LINK SD MET A1401 FE2 SF4 A2460 1555 1555 2.67
LINK OXT MET A1401 FE2 SF4 A2460 1555 1555 2.27
CISPEP 1 MET A 115 PRO A 116 0 -5.99
CISPEP 2 SER A 297 PRO A 298 0 5.95
SITE 1 AC1 5 CYS A 63 CYS A 67 CYS A 70 GLY A 109
SITE 2 AC1 5 MET A1401
SITE 1 AC2 11 SER A 108 SER A 136 GLY A 138 ARG A 180
SITE 2 AC2 11 TYR A 303 HOH A 474 HOH A 480 HOH A 483
SITE 3 AC2 11 HOH A 493 5AD A1501 SF4 A2460
SITE 1 AC3 13 TYR A 69 GLN A 107 ARG A 159 GLU A 161
SITE 2 AC3 13 MET A 199 PRO A 229 ILE A 231 LEU A 305
SITE 3 AC3 13 TYR A 306 HOH A 480 HOH A 501 HOH A 587
SITE 4 AC3 13 MET A1401
SITE 1 AC4 19 GLN A 98 PHE A 99 GLY A 100 PRO A 276
SITE 2 AC4 19 GLY A 277 GLU A 280 ARG A 284 MET A 324
SITE 3 AC4 19 LEU A 330 HOH A 392 HOH A 421 HOH A 477
SITE 4 AC4 19 HOH A 504 HOH A 512 HOH A 513 HOH A 663
SITE 5 AC4 19 HOH A 694 CPS A1704 CPS A1705
SITE 1 AC5 15 LYS A 37 ASP A 40 LYS A 170 ARG A 284
SITE 2 AC5 15 SER A 297 LYS A 315 ASP A 316 THR A 317
SITE 3 AC5 15 HOH A 362 HOH A 543 HOH A 577 HOH A 664
SITE 4 AC5 15 HOH A 721 HOH A 723 HOH A 792
SITE 1 AC6 11 ARG A 29 GLU A 33 THR A 247 LEU A 250
SITE 2 AC6 11 HOH A 354 HOH A 403 HOH A 566 HOH A 570
SITE 3 AC6 11 HOH A 583 HOH A 809 CPS A1704
SITE 1 AC7 10 THR A 317 ALA A 318 HOH A 449 HOH A 466
SITE 2 AC7 10 HOH A 583 HOH A 731 HOH A 735 HOH A 759
SITE 3 AC7 10 CPS A1701 CPS A1703
SITE 1 AC8 11 LYS A 128 MET A 324 LYS A 325 GLU A 328
SITE 2 AC8 11 HOH A 361 HOH A 457 HOH A 612 HOH A 694
SITE 3 AC8 11 HOH A 705 HOH A 804 CPS A1701
SITE 1 AC9 1 CYS A 319
SITE 1 BC1 2 CYS A 319 HOH A 538
SITE 1 BC2 3 ARG A 279 CYS A 319 CSO A 322
SITE 1 BC4 5 THR A 268 ALA A 270 TYR A 306 HOH A 572
SITE 2 BC4 5 HOH A 587
SITE 1 BC5 3 ARG A 54 THR A 134 ARG A 155
SITE 1 BC6 6 ARG A 159 PRO A 266 MET A 291 HOH A 544
SITE 2 BC6 6 HOH A 714 HOH A 752
SITE 1 BC7 5 PHE A 246 HOH A 460 HOH A 529 HOH A 687
SITE 2 BC7 5 CPS A1703
CRYST1 51.054 78.925 86.192 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 0.019587 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END