HEADER OXIDOREDUCTASE 29-SEP-10 2XSJ
TITLE STRUCTURE OF DESULFORUBIDIN FROM DESULFOMICROBIUM NORVEGICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SULFITE REDUCTASE ALPHA SUBUNIT;
COMPND 3 CHAIN: A, D;
COMPND 4 EC: 1.8.99.3;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SULFITE REDUCTASE BETA SUBUNIT;
COMPND 7 CHAIN: B, E;
COMPND 8 EC: 1.8.99.3;
COMPND 9 OTHER_DETAILS: COVALENT BOND BETWEEN THE SG OF CYS 104C/E AND THE 20-
COMPND 10 MESO CARBON OF THE CATALYTIC SIROHEME PORPHYRIN RING;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: SULFUR RELAY PROTEIN, TUSE/DSRC/DSVC FAMILY;
COMPND 13 CHAIN: C, F;
COMPND 14 EC: 1.8.99.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOMICROBIUM NORVEGICUM;
SOURCE 3 ORGANISM_TAXID: 52561;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: DESULFOMICROBIUM NORVEGICUM;
SOURCE 6 ORGANISM_TAXID: 52561;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: DESULFOMICROBIUM NORVEGICUM;
SOURCE 9 ORGANISM_TAXID: 52561
KEYWDS DISSIMILATORY SULFITE REDUCTASE, SULFUR METABOLISM, DSRABC,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.F.OLIVEIRA,A.R.KHAN,I.A.C.PEREIRA,M.ARCHER
REVDAT 4 20-DEC-23 2XSJ 1 REMARK
REVDAT 3 06-DEC-23 2XSJ 1 COMPND REMARK FORMUL LINK
REVDAT 2 14-SEP-11 2XSJ 1 JRNL DBREF
REVDAT 1 24-AUG-11 2XSJ 0
JRNL AUTH T.F.OLIVEIRA,E.FRANKLIN,J.P.AFONSO,A.R.KHAN,N.J.OLDHAM,
JRNL AUTH 2 I.A.C.PEREIRA,M.ARCHER
JRNL TITL STRUCTURAL INSIGHTS INTO DISSIMILATORY SULFITE REDUCTASES:
JRNL TITL 2 STRUCTURE OF DESULFORUBIDIN FROM DESULFOMICROBIUM NORVEGICUM
JRNL REF FRONT.MICROBIOL. V. 2 71 2011
JRNL REFN ESSN 1664-302X
JRNL PMID 21833321
JRNL DOI 10.3389/FMICB.2011.00071
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 78140
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4114
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5005
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 231
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14614
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 324
REMARK 3 SOLVENT ATOMS : 1041
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.49000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 2.29000
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): 0.423
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.544
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15415 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20940 ; 1.560 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1844 ; 6.460 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 708 ;36.458 ;24.011
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2532 ;16.777 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;19.942 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2163 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11882 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 9181 ; 0.617 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14772 ; 1.230 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6234 ; 2.153 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6072 ; 3.453 ; 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): 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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 437 5
REMARK 3 1 D 2 D 437 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1744 ; 0.06 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1744 ; 0.06 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1712 ; 0.21 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 1712 ; 0.21 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1744 ; 0.65 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1744 ; 0.65 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1712 ; 1.07 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 1712 ; 1.07 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 2 B 386 5
REMARK 3 1 E 2 E 386 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 1536 ; 0.06 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 E (A): 1536 ; 0.06 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 B (A): 1486 ; 0.20 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 E (A): 1486 ; 0.20 ; 5.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 1536 ; 0.71 ; 2.00
REMARK 3 MEDIUM THERMAL 2 E (A**2): 1536 ; 0.71 ; 2.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 1486 ; 1.05 ; 10.00
REMARK 3 LOOSE THERMAL 2 E (A**2): 1486 ; 1.05 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 2 C 105 5
REMARK 3 1 F 2 F 105 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 C (A): 416 ; 0.10 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 F (A): 416 ; 0.10 ; 0.50
REMARK 3 LOOSE POSITIONAL 3 C (A): 409 ; 0.46 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 F (A): 409 ; 0.46 ; 5.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 416 ; 1.47 ; 2.00
REMARK 3 MEDIUM THERMAL 3 F (A**2): 416 ; 1.47 ; 2.00
REMARK 3 LOOSE THERMAL 3 C (A**2): 409 ; 1.82 ; 10.00
REMARK 3 LOOSE THERMAL 3 F (A**2): 409 ; 1.82 ; 10.00
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 2XSJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1290045053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79925
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.530
REMARK 200 RESOLUTION RANGE LOW (A) : 45.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.800
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 ENTRY 2V4J
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1 M BISTRIS PROPANE PH
REMARK 280 7.5 AND 0.2 M K/NA TARTRATE
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 49.67000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.67000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.54500
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 55250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -478.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 MET E 1
REMARK 465 MET F 1
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 D 2045 O HOH F 2004 2.13
REMARK 500 NZ LYS D 57 N HIS D 64 2.13
REMARK 500 O ASP B 219 O HOH B 2114 2.17
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 LEU A 336 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG D 31 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 305 NE - CZ - NH2 ANGL. DEV. = -3.2 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 PHE A 97 56.34 -153.58
REMARK 500 ARG A 182 49.57 -157.92
REMARK 500 ASP A 242 -159.83 -100.88
REMARK 500 VAL A 280 -73.27 -130.53
REMARK 500 MET A 307 -14.54 96.23
REMARK 500 LYS A 332 155.24 179.62
REMARK 500 GLU A 352 112.53 -160.14
REMARK 500 PRO A 411 46.10 -94.18
REMARK 500 ARG B 71 -69.79 73.82
REMARK 500 THR B 140 -163.76 -104.24
REMARK 500 THR B 145 -152.72 -124.74
REMARK 500 HIS B 150 -18.81 -151.66
REMARK 500 THR B 156 -174.38 -172.93
REMARK 500 CYS B 198 39.98 -141.31
REMARK 500 ILE B 298 -67.76 54.24
REMARK 500 TRP B 318 57.20 33.86
REMARK 500 TYR B 339 -9.71 80.79
REMARK 500 ARG B 371 -168.69 53.56
REMARK 500 PRO D 18 125.08 -39.38
REMARK 500 PHE D 97 53.14 -150.88
REMARK 500 ARG D 182 43.89 -159.86
REMARK 500 ASP D 189 86.42 -66.50
REMARK 500 ASP D 242 -154.94 -107.04
REMARK 500 VAL D 280 -68.42 -130.11
REMARK 500 MET D 307 -15.18 89.19
REMARK 500 LEU D 345 -50.97 -121.13
REMARK 500 PRO D 411 42.08 -96.23
REMARK 500 GLU E 48 167.15 179.72
REMARK 500 ARG E 71 -72.74 67.36
REMARK 500 PHE E 130 61.38 -150.24
REMARK 500 THR E 140 -162.09 -104.53
REMARK 500 THR E 145 -156.78 -121.45
REMARK 500 HIS E 150 -25.49 -154.61
REMARK 500 THR E 156 179.30 178.80
REMARK 500 MET E 192 81.27 54.15
REMARK 500 CYS E 193 58.73 -95.60
REMARK 500 PHE E 265 30.88 73.05
REMARK 500 ILE E 298 -73.94 61.59
REMARK 500 TRP E 318 59.12 33.60
REMARK 500 TYR E 339 -12.64 77.45
REMARK 500 ILE E 364 -52.58 -14.19
REMARK 500 ARG E 371 -166.15 54.48
REMARK 500 GLN E 380 61.25 -104.01
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 SF4 A 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 177 SG
REMARK 620 2 SF4 A 502 S2 106.6
REMARK 620 3 SF4 A 502 S3 110.8 107.2
REMARK 620 4 SF4 A 502 S4 123.1 104.1 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 183 SG
REMARK 620 2 SF4 A 502 S1 107.9
REMARK 620 3 SF4 A 502 S3 124.5 103.2
REMARK 620 4 SF4 A 502 S4 109.2 106.9 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 221 SG
REMARK 620 2 SF4 A 502 S1 94.7
REMARK 620 3 SF4 A 502 S2 126.7 106.3
REMARK 620 4 SF4 A 502 S4 117.2 105.5 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 225 SG
REMARK 620 2 SF4 A 502 S1 115.9
REMARK 620 3 SF4 A 502 S2 110.0 106.3
REMARK 620 4 SF4 A 502 S3 115.0 103.0 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SRM A 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 225 SG
REMARK 620 2 SRM A 503 NA 101.6
REMARK 620 3 SRM A 503 NB 90.7 89.6
REMARK 620 4 SRM A 503 NC 79.3 179.1 90.4
REMARK 620 5 SRM A 503 ND 91.0 90.2 178.3 89.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 284 SG
REMARK 620 2 SF4 A 501 S1 109.3
REMARK 620 3 SF4 A 501 S2 110.1 105.8
REMARK 620 4 SF4 A 501 S4 120.7 101.9 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 303 SG
REMARK 620 2 SF4 A 501 S2 113.5
REMARK 620 3 SF4 A 501 S3 108.1 103.5
REMARK 620 4 SF4 A 501 S4 115.7 108.1 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 306 SG
REMARK 620 2 SF4 A 501 S1 106.1
REMARK 620 3 SF4 A 501 S2 115.1 107.7
REMARK 620 4 SF4 A 501 S3 119.9 103.6 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 309 SG
REMARK 620 2 SF4 A 501 S1 118.5
REMARK 620 3 SF4 A 501 S3 111.3 103.9
REMARK 620 4 SF4 A 501 S4 112.2 101.8 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 151 SG
REMARK 620 2 SF4 B 502 S1 170.0
REMARK 620 3 SF4 B 502 S2 101.0 69.3
REMARK 620 4 SF4 B 502 S3 115.3 66.2 102.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 188 SG
REMARK 620 2 SF4 B 502 S1 123.0
REMARK 620 3 SF4 B 502 S2 92.3 108.9
REMARK 620 4 SF4 B 502 S4 120.9 100.5 110.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 189 SG
REMARK 620 2 SF4 B 502 S2 107.1
REMARK 620 3 SF4 B 502 S3 109.2 103.0
REMARK 620 4 SF4 B 502 S4 173.0 70.3 65.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 193 SG
REMARK 620 2 SF4 B 502 S1 103.9
REMARK 620 3 SF4 B 502 S3 107.9 104.2
REMARK 620 4 SF4 B 502 S4 130.8 103.6 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SRM B 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 193 SG
REMARK 620 2 SRM B 503 NA 88.5
REMARK 620 3 SRM B 503 NB 93.5 90.7
REMARK 620 4 SRM B 503 NC 90.5 178.8 88.9
REMARK 620 5 SRM B 503 ND 85.5 89.3 179.0 91.1
REMARK 620 6 SO3 B 504 S 174.2 87.0 90.2 94.1 90.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 231 SG
REMARK 620 2 SF4 B 501 S2 121.8
REMARK 620 3 SF4 B 501 S3 109.7 105.4
REMARK 620 4 SF4 B 501 S4 107.8 103.2 108.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 263 SG
REMARK 620 2 SF4 B 501 S1 107.6
REMARK 620 3 SF4 B 501 S3 115.5 103.6
REMARK 620 4 SF4 B 501 S4 172.2 64.6 68.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 266 SG
REMARK 620 2 SF4 B 501 S1 121.1
REMARK 620 3 SF4 B 501 S2 163.5 66.1
REMARK 620 4 SF4 B 501 S3 120.7 104.2 67.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 269 SG
REMARK 620 2 SF4 B 501 S1 112.0
REMARK 620 3 SF4 B 501 S2 121.6 105.1
REMARK 620 4 SF4 B 501 S4 110.4 103.1 102.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 177 SG
REMARK 620 2 SF4 D 502 S2 105.3
REMARK 620 3 SF4 D 502 S3 109.2 107.2
REMARK 620 4 SF4 D 502 S4 125.1 103.9 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 183 SG
REMARK 620 2 SF4 D 502 S1 105.7
REMARK 620 3 SF4 D 502 S3 126.4 102.9
REMARK 620 4 SF4 D 502 S4 108.6 106.8 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 221 SG
REMARK 620 2 SF4 D 502 S1 97.3
REMARK 620 3 SF4 D 502 S2 125.5 106.0
REMARK 620 4 SF4 D 502 S4 116.0 105.9 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 225 SG
REMARK 620 2 SF4 D 502 S1 116.1
REMARK 620 3 SF4 D 502 S2 107.4 106.8
REMARK 620 4 SF4 D 502 S3 116.0 103.9 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SRM D 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 225 SG
REMARK 620 2 SRM D 503 NA 103.7
REMARK 620 3 SRM D 503 NB 90.0 88.6
REMARK 620 4 SRM D 503 NC 77.6 178.6 91.0
REMARK 620 5 SRM D 503 ND 91.7 91.2 178.3 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 284 SG
REMARK 620 2 SF4 D 501 S1 107.1
REMARK 620 3 SF4 D 501 S2 113.3 106.6
REMARK 620 4 SF4 D 501 S4 119.4 101.8 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 303 SG
REMARK 620 2 SF4 D 501 S2 113.2
REMARK 620 3 SF4 D 501 S3 110.2 104.4
REMARK 620 4 SF4 D 501 S4 114.0 107.4 107.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 306 SG
REMARK 620 2 SF4 D 501 S1 106.4
REMARK 620 3 SF4 D 501 S2 113.5 107.3
REMARK 620 4 SF4 D 501 S3 120.5 103.0 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 309 SG
REMARK 620 2 SF4 D 501 S1 118.8
REMARK 620 3 SF4 D 501 S3 107.4 104.4
REMARK 620 4 SF4 D 501 S4 115.2 102.2 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 151 SG
REMARK 620 2 SF4 E 502 S1 116.3
REMARK 620 3 SF4 E 502 S3 107.5 109.2
REMARK 620 4 SF4 E 502 S4 115.5 104.1 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 188 SG
REMARK 620 2 SF4 E 502 S1 117.3
REMARK 620 3 SF4 E 502 S2 123.3 101.0
REMARK 620 4 SF4 E 502 S3 96.9 107.5 110.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 189 SG
REMARK 620 2 SF4 E 502 S2 122.2
REMARK 620 3 SF4 E 502 S3 103.4 110.8
REMARK 620 4 SF4 E 502 S4 111.6 104.1 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 193 SG
REMARK 620 2 SF4 E 502 S1 135.0
REMARK 620 3 SF4 E 502 S2 101.6 104.2
REMARK 620 4 SF4 E 502 S4 106.0 102.7 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SRM E 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 193 SG
REMARK 620 2 SRM E 503 NA 87.8
REMARK 620 3 SRM E 503 NB 93.7 91.1
REMARK 620 4 SRM E 503 NC 91.0 178.7 88.4
REMARK 620 5 SRM E 503 ND 85.2 88.6 178.9 91.8
REMARK 620 6 SO3 E 504 S 174.4 90.1 91.5 91.2 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 231 SG
REMARK 620 2 SF4 E 501 S2 106.5
REMARK 620 3 SF4 E 501 S3 123.7 105.3
REMARK 620 4 SF4 E 501 S4 108.9 106.4 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 263 SG
REMARK 620 2 SF4 E 501 S1 110.3
REMARK 620 3 SF4 E 501 S2 117.1 105.0
REMARK 620 4 SF4 E 501 S3 113.2 104.1 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 266 SG
REMARK 620 2 SF4 E 501 S1 122.2
REMARK 620 3 SF4 E 501 S2 120.4 105.5
REMARK 620 4 SF4 E 501 S4 98.7 101.8 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 269 SG
REMARK 620 2 SF4 E 501 S1 109.9
REMARK 620 3 SF4 E 501 S3 119.4 106.0
REMARK 620 4 SF4 E 501 S4 112.0 103.6 104.6
REMARK 620 N 1 2 3
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO3 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO3 E 504
DBREF 2XSJ A 1 62 PDB 2XSJ 2XSJ 1 62
DBREF 2XSJ A 63 437 UNP Q93UT1 Q93UT1_DESNO 1 375
DBREF 2XSJ B 1 271 UNP Q93UT0 Q93UT0_DESNO 1 271
DBREF 2XSJ B 272 386 PDB 2XSJ 2XSJ 272 386
DBREF 2XSJ C 1 105 PDB 2XSJ 2XSJ 1 105
DBREF 2XSJ D 1 62 PDB 2XSJ 2XSJ 1 62
DBREF 2XSJ D 63 437 UNP Q93UT1 Q93UT1_DESNO 1 375
DBREF 2XSJ E 1 271 UNP Q93UT0 Q93UT0_DESNO 1 271
DBREF 2XSJ E 272 386 PDB 2XSJ 2XSJ 272 386
DBREF 2XSJ F 1 105 PDB 2XSJ 2XSJ 1 105
SEQRES 1 A 437 MET ALA LYS HIS ALA THR PRO LEU LEU ASP GLN LEU GLN
SEQRES 2 A 437 SER GLY PRO TRP PRO SER PHE VAL ALA ASP ILE LYS GLU
SEQRES 3 A 437 GLU ALA GLU ARG ARG HIS SER ASN GLN ASP ASN VAL GLU
SEQRES 4 A 437 TYR GLN ILE PRO VAL ASP VAL CYS ASP ASP LEU LEU GLY
SEQRES 5 A 437 ILE LEU GLU LEU LYS TYR SER ASP GLY THR THR HIS TRP
SEQRES 6 A 437 LYS HIS GLY GLY ILE VAL GLY VAL PHE GLY TYR GLY GLY
SEQRES 7 A 437 GLY VAL ILE GLY ARG TYR CYS ASP GLN PRO GLN MET PHE
SEQRES 8 A 437 PRO GLY VAL ALA HIS PHE HIS THR VAL ARG VAL ALA GLN
SEQRES 9 A 437 PRO ALA GLY MET TYR TYR THR THR ASP PHE LEU LYS GLN
SEQRES 10 A 437 LEU CYS ASP LEU TRP ASP MET ARG GLY SER GLY LEU THR
SEQRES 11 A 437 ASN MET HIS GLY ALA THR GLY ASP ILE VAL LEU LEU GLY
SEQRES 12 A 437 THR THR THR PRO GLN LEU GLU GLU PHE TYR PHE GLU LEU
SEQRES 13 A 437 THR HIS LYS MET ASN ASN ASP LEU GLY GLY SER GLY SER
SEQRES 14 A 437 ASN LEU ARG THR PRO ALA SER CYS LEU GLY ASP SER ARG
SEQRES 15 A 437 CYS GLU TRP ALA CYS TYR ASP ALA GLN GLU LEU CYS TYR
SEQRES 16 A 437 GLN MET THR GLN GLU TYR GLN ASP GLU LEU HIS ARG PRO
SEQRES 17 A 437 ALA PHE PRO TYR LYS PHE LYS PHE LYS PHE ASP GLY CYS
SEQRES 18 A 437 PRO ASN GLY CYS VAL ALA SER ILE ALA ARG SER ASP MET
SEQRES 19 A 437 SER PHE ILE GLY THR TRP ARG ASP ASP ILE ARG ILE ASP
SEQRES 20 A 437 GLN GLU ALA VAL ALA ALA TYR VAL GLY GLY GLU ILE GLN
SEQRES 21 A 437 PRO ASN GLY GLY ALA HIS SER GLY LYS ASP TRP GLY ALA
SEQRES 22 A 437 PHE ASP ILE GLN LYS GLU VAL ILE ASP LEU CYS PRO THR
SEQRES 23 A 437 GLU CYS MET TRP MET GLU ASP GLY LYS LEU GLN ILE ASN
SEQRES 24 A 437 ASN ARG GLU CYS THR ARG CYS MET HIS CYS LEU ASN VAL
SEQRES 25 A 437 MET PRO ARG ALA LEU ARG ILE GLY ASN ASP ARG GLY LEU
SEQRES 26 A 437 SER ILE LEU VAL GLY ALA LYS ALA PRO ILE LEU ASP GLY
SEQRES 27 A 437 ALA GLN MET GLY SER LEU LEU VAL PRO PHE ILE LYS VAL
SEQRES 28 A 437 GLU ASP PRO TYR ASP GLU ILE LYS GLU ILE ILE GLU GLY
SEQRES 29 A 437 ILE TRP GLU TRP TRP MET GLU GLU GLY LYS ASN ARG GLU
SEQRES 30 A 437 ARG LEU GLY GLU LEU ILE LYS ARG GLN GLY LEU ALA LYS
SEQRES 31 A 437 ALA ILE ALA ALA VAL GLY LEU THR PRO VAL PRO GLN HIS
SEQRES 32 A 437 VAL MET GLU PRO ARG HIS ASN PRO TYR ILE PHE TRP LYS
SEQRES 33 A 437 GLU LYS ASP VAL GLU GLY GLY TRP ASP ARG ASP ILE ALA
SEQRES 34 A 437 ASP TYR ARG LYS HIS HIS GLN ARG
SEQRES 1 B 386 MET ALA PHE VAL SER SER GLY TYR ASN PRO GLU LYS PRO
SEQRES 2 B 386 MET GLU ASN ARG ILE SER ASP ILE GLY PRO ARG HIS ALA
SEQRES 3 B 386 SER ASP PHE PHE PRO PRO VAL ILE ALA LYS ASN LYS GLY
SEQRES 4 B 386 GLN TRP LEU TRP HIS GLU ILE CYS GLU PRO GLY ILE LEU
SEQRES 5 B 386 MET HIS LYS ALA GLU SER GLY ASP GLU VAL TYR THR VAL
SEQRES 6 B 386 ARG CYS GLY GLY ALA ARG LEU MET SER VAL GLY HIS ILE
SEQRES 7 B 386 ARG GLU ILE CYS ALA ILE ALA ASP LYS PHE CYS GLY GLY
SEQRES 8 B 386 HIS LEU ARG PHE THR THR ARG ASN ASN ILE GLU PHE MET
SEQRES 9 B 386 VAL THR THR LEU ASP GLU ALA LYS LYS LEU LYS GLU TYR
SEQRES 10 B 386 LEU ASN ALA GLN LYS PHE GLU GLY GLY SER PHE LYS PHE
SEQRES 11 B 386 PRO VAL GLY GLY THR GLY ALA GLY ILE THR ASN ILE VAL
SEQRES 12 B 386 HIS THR GLN GLY TRP VAL HIS CYS HIS THR PRO ALA THR
SEQRES 13 B 386 ASP ALA SER GLY THR VAL LYS VAL VAL LEU ASP GLU LEU
SEQRES 14 B 386 PHE GLU GLU PHE GLY GLN MET ARG MET PRO ALA GLN VAL
SEQRES 15 B 386 ARG ILE SER MET ALA CYS CYS LEU ASN MET CYS GLY ALA
SEQRES 16 B 386 VAL HIS CYS SER ASP ILE ALA ILE LEU GLY TYR HIS ARG
SEQRES 17 B 386 LYS PRO PRO VAL ILE ASP HIS GLU TRP LEU ASP ASN LEU
SEQRES 18 B 386 CYS GLU ILE PRO LEU ALA VAL ALA ALA CYS PRO VAL GLY
SEQRES 19 B 386 ALA ILE ARG PRO THR LYS LYS GLU ILE VAL THR GLU LYS
SEQRES 20 B 386 GLY GLU THR LYS THR VAL ASN THR VAL ALA ILE LYS ASN
SEQRES 21 B 386 GLU ARG CYS MET PHE CYS GLY ASN CYS TYR THR MET CYS
SEQRES 22 B 386 PRO SER LEU PRO LEU SER ASP GLN THR GLY ASP GLY LEU
SEQRES 23 B 386 VAL ILE MET ALA GLY GLY LYS VAL SER ASN ARG ILE SER
SEQRES 24 B 386 ASN PRO LYS PHE SER LYS VAL VAL VAL ALA PHE ILE PRO
SEQRES 25 B 386 ASN GLU PRO PRO ARG TRP PRO ARG LEU ALA SER VAL ILE
SEQRES 26 B 386 ARG GLN ILE VAL GLU ALA TYR ALA ALA ASP ALA ARG LYS
SEQRES 27 B 386 TYR GLU ARG VAL GLY ASP TRP ALA GLU ARG ILE GLY TRP
SEQRES 28 B 386 GLU ARG PHE PHE GLU LYS CYS GLU LEU ASP PHE SER ILE
SEQRES 29 B 386 HIS MET ILE ASP ASP PHE ARG ASP PRO ALA TYR TYR THR
SEQRES 30 B 386 TRP ARG GLN THR THR ASN PHE LYS PHE
SEQRES 1 C 105 MET ALA MET ILE GLU PHE LYS GLY LYS SER PHE GLU ILE
SEQRES 2 C 105 ASP GLU ASP GLY PHE LEU LEU LYS PHE GLU ASP TRP GLY
SEQRES 3 C 105 PRO GLU TRP ALA GLU TYR VAL LYS GLU SER GLU GLY ILE
SEQRES 4 C 105 SER GLU ILE THR GLU ALA HIS GLN GLN ILE LEU ASP PHE
SEQRES 5 C 105 LEU GLN ASP TYR TYR LYS LYS ASN GLY ILE ALA PRO MET
SEQRES 6 C 105 VAL ARG ILE LEU SER LYS SER THR GLY TYR LYS LEU LYS
SEQRES 7 C 105 GLN ILE TYR GLU LEU PHE PRO SER GLY PRO GLY LYS GLY
SEQRES 8 C 105 ALA CYS LYS MET ALA GLY LEU PRO LYS PRO THR GLY CYS
SEQRES 9 C 105 VAL
SEQRES 1 D 437 MET ALA LYS HIS ALA THR PRO LEU LEU ASP GLN LEU GLN
SEQRES 2 D 437 SER GLY PRO TRP PRO SER PHE VAL ALA ASP ILE LYS GLU
SEQRES 3 D 437 GLU ALA GLU ARG ARG HIS SER ASN GLN ASP ASN VAL GLU
SEQRES 4 D 437 TYR GLN ILE PRO VAL ASP VAL CYS ASP ASP LEU LEU GLY
SEQRES 5 D 437 ILE LEU GLU LEU LYS TYR SER ASP GLY THR THR HIS TRP
SEQRES 6 D 437 LYS HIS GLY GLY ILE VAL GLY VAL PHE GLY TYR GLY GLY
SEQRES 7 D 437 GLY VAL ILE GLY ARG TYR CYS ASP GLN PRO GLN MET PHE
SEQRES 8 D 437 PRO GLY VAL ALA HIS PHE HIS THR VAL ARG VAL ALA GLN
SEQRES 9 D 437 PRO ALA GLY MET TYR TYR THR THR ASP PHE LEU LYS GLN
SEQRES 10 D 437 LEU CYS ASP LEU TRP ASP MET ARG GLY SER GLY LEU THR
SEQRES 11 D 437 ASN MET HIS GLY ALA THR GLY ASP ILE VAL LEU LEU GLY
SEQRES 12 D 437 THR THR THR PRO GLN LEU GLU GLU PHE TYR PHE GLU LEU
SEQRES 13 D 437 THR HIS LYS MET ASN ASN ASP LEU GLY GLY SER GLY SER
SEQRES 14 D 437 ASN LEU ARG THR PRO ALA SER CYS LEU GLY ASP SER ARG
SEQRES 15 D 437 CYS GLU TRP ALA CYS TYR ASP ALA GLN GLU LEU CYS TYR
SEQRES 16 D 437 GLN MET THR GLN GLU TYR GLN ASP GLU LEU HIS ARG PRO
SEQRES 17 D 437 ALA PHE PRO TYR LYS PHE LYS PHE LYS PHE ASP GLY CYS
SEQRES 18 D 437 PRO ASN GLY CYS VAL ALA SER ILE ALA ARG SER ASP MET
SEQRES 19 D 437 SER PHE ILE GLY THR TRP ARG ASP ASP ILE ARG ILE ASP
SEQRES 20 D 437 GLN GLU ALA VAL ALA ALA TYR VAL GLY GLY GLU ILE GLN
SEQRES 21 D 437 PRO ASN GLY GLY ALA HIS SER GLY LYS ASP TRP GLY ALA
SEQRES 22 D 437 PHE ASP ILE GLN LYS GLU VAL ILE ASP LEU CYS PRO THR
SEQRES 23 D 437 GLU CYS MET TRP MET GLU ASP GLY LYS LEU GLN ILE ASN
SEQRES 24 D 437 ASN ARG GLU CYS THR ARG CYS MET HIS CYS LEU ASN VAL
SEQRES 25 D 437 MET PRO ARG ALA LEU ARG ILE GLY ASN ASP ARG GLY LEU
SEQRES 26 D 437 SER ILE LEU VAL GLY ALA LYS ALA PRO ILE LEU ASP GLY
SEQRES 27 D 437 ALA GLN MET GLY SER LEU LEU VAL PRO PHE ILE LYS VAL
SEQRES 28 D 437 GLU ASP PRO TYR ASP GLU ILE LYS GLU ILE ILE GLU GLY
SEQRES 29 D 437 ILE TRP GLU TRP TRP MET GLU GLU GLY LYS ASN ARG GLU
SEQRES 30 D 437 ARG LEU GLY GLU LEU ILE LYS ARG GLN GLY LEU ALA LYS
SEQRES 31 D 437 ALA ILE ALA ALA VAL GLY LEU THR PRO VAL PRO GLN HIS
SEQRES 32 D 437 VAL MET GLU PRO ARG HIS ASN PRO TYR ILE PHE TRP LYS
SEQRES 33 D 437 GLU LYS ASP VAL GLU GLY GLY TRP ASP ARG ASP ILE ALA
SEQRES 34 D 437 ASP TYR ARG LYS HIS HIS GLN ARG
SEQRES 1 E 386 MET ALA PHE VAL SER SER GLY TYR ASN PRO GLU LYS PRO
SEQRES 2 E 386 MET GLU ASN ARG ILE SER ASP ILE GLY PRO ARG HIS ALA
SEQRES 3 E 386 SER ASP PHE PHE PRO PRO VAL ILE ALA LYS ASN LYS GLY
SEQRES 4 E 386 GLN TRP LEU TRP HIS GLU ILE CYS GLU PRO GLY ILE LEU
SEQRES 5 E 386 MET HIS LYS ALA GLU SER GLY ASP GLU VAL TYR THR VAL
SEQRES 6 E 386 ARG CYS GLY GLY ALA ARG LEU MET SER VAL GLY HIS ILE
SEQRES 7 E 386 ARG GLU ILE CYS ALA ILE ALA ASP LYS PHE CYS GLY GLY
SEQRES 8 E 386 HIS LEU ARG PHE THR THR ARG ASN ASN ILE GLU PHE MET
SEQRES 9 E 386 VAL THR THR LEU ASP GLU ALA LYS LYS LEU LYS GLU TYR
SEQRES 10 E 386 LEU ASN ALA GLN LYS PHE GLU GLY GLY SER PHE LYS PHE
SEQRES 11 E 386 PRO VAL GLY GLY THR GLY ALA GLY ILE THR ASN ILE VAL
SEQRES 12 E 386 HIS THR GLN GLY TRP VAL HIS CYS HIS THR PRO ALA THR
SEQRES 13 E 386 ASP ALA SER GLY THR VAL LYS VAL VAL LEU ASP GLU LEU
SEQRES 14 E 386 PHE GLU GLU PHE GLY GLN MET ARG MET PRO ALA GLN VAL
SEQRES 15 E 386 ARG ILE SER MET ALA CYS CYS LEU ASN MET CYS GLY ALA
SEQRES 16 E 386 VAL HIS CYS SER ASP ILE ALA ILE LEU GLY TYR HIS ARG
SEQRES 17 E 386 LYS PRO PRO VAL ILE ASP HIS GLU TRP LEU ASP ASN LEU
SEQRES 18 E 386 CYS GLU ILE PRO LEU ALA VAL ALA ALA CYS PRO VAL GLY
SEQRES 19 E 386 ALA ILE ARG PRO THR LYS LYS GLU ILE VAL THR GLU LYS
SEQRES 20 E 386 GLY GLU THR LYS THR VAL ASN THR VAL ALA ILE LYS ASN
SEQRES 21 E 386 GLU ARG CYS MET PHE CYS GLY ASN CYS TYR THR MET CYS
SEQRES 22 E 386 PRO SER LEU PRO LEU SER ASP GLN THR GLY ASP GLY LEU
SEQRES 23 E 386 VAL ILE MET ALA GLY GLY LYS VAL SER ASN ARG ILE SER
SEQRES 24 E 386 ASN PRO LYS PHE SER LYS VAL VAL VAL ALA PHE ILE PRO
SEQRES 25 E 386 ASN GLU PRO PRO ARG TRP PRO ARG LEU ALA SER VAL ILE
SEQRES 26 E 386 ARG GLN ILE VAL GLU ALA TYR ALA ALA ASP ALA ARG LYS
SEQRES 27 E 386 TYR GLU ARG VAL GLY ASP TRP ALA GLU ARG ILE GLY TRP
SEQRES 28 E 386 GLU ARG PHE PHE GLU LYS CYS GLU LEU ASP PHE SER ILE
SEQRES 29 E 386 HIS MET ILE ASP ASP PHE ARG ASP PRO ALA TYR TYR THR
SEQRES 30 E 386 TRP ARG GLN THR THR ASN PHE LYS PHE
SEQRES 1 F 105 MET ALA MET ILE GLU PHE LYS GLY LYS SER PHE GLU ILE
SEQRES 2 F 105 ASP GLU ASP GLY PHE LEU LEU LYS PHE GLU ASP TRP GLY
SEQRES 3 F 105 PRO GLU TRP ALA GLU TYR VAL LYS GLU SER GLU GLY ILE
SEQRES 4 F 105 SER GLU ILE THR GLU ALA HIS GLN GLN ILE LEU ASP PHE
SEQRES 5 F 105 LEU GLN ASP TYR TYR LYS LYS ASN GLY ILE ALA PRO MET
SEQRES 6 F 105 VAL ARG ILE LEU SER LYS SER THR GLY TYR LYS LEU LYS
SEQRES 7 F 105 GLN ILE TYR GLU LEU PHE PRO SER GLY PRO GLY LYS GLY
SEQRES 8 F 105 ALA CYS LYS MET ALA GLY LEU PRO LYS PRO THR GLY CYS
SEQRES 9 F 105 VAL
HET SF4 A 501 8
HET SF4 A 502 8
HET SRM A 503 63
HET SF4 B 501 8
HET SF4 B 502 8
HET SRM B 503 63
HET SO3 B 504 4
HET SF4 D 501 8
HET SF4 D 502 8
HET SRM D 503 63
HET SF4 E 501 8
HET SF4 E 502 8
HET SRM E 503 63
HET SO3 E 504 4
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM SRM SIROHEME
HETNAM SO3 SULFITE ION
FORMUL 7 SF4 8(FE4 S4)
FORMUL 9 SRM 4(C42 H44 FE N4 O16)
FORMUL 13 SO3 2(O3 S 2-)
FORMUL 21 HOH *1041(H2 O)
HELIX 1 1 LEU A 8 SER A 14 5 7
HELIX 2 2 SER A 19 ASN A 34 1 16
HELIX 3 3 ASP A 45 GLY A 61 1 17
HELIX 4 4 PHE A 91 ALA A 95 5 5
HELIX 5 5 THR A 112 GLY A 126 1 15
HELIX 6 6 PRO A 147 ASN A 161 1 15
HELIX 7 7 LEU A 178 ARG A 182 5 5
HELIX 8 8 ASP A 189 TYR A 201 1 13
HELIX 9 9 TYR A 201 ARG A 207 1 7
HELIX 10 10 ALA A 227 SER A 232 1 6
HELIX 11 11 ASP A 247 GLY A 256 1 10
HELIX 12 12 GLN A 260 ALA A 265 5 6
HELIX 13 13 ASP A 275 VAL A 280 1 6
HELIX 14 14 ASN A 300 CYS A 303 5 4
HELIX 15 15 MET A 307 MET A 313 1 7
HELIX 16 16 TYR A 355 GLY A 373 1 19
HELIX 17 17 ARG A 378 GLY A 387 1 10
HELIX 18 18 GLY A 387 VAL A 395 1 9
HELIX 19 19 VAL A 400 HIS A 403 5 4
HELIX 20 20 LYS A 416 VAL A 420 5 5
HELIX 21 21 ASP A 427 HIS A 435 1 9
HELIX 22 22 HIS B 25 PHE B 29 5 5
HELIX 23 23 PRO B 31 LYS B 38 1 8
HELIX 24 24 VAL B 75 CYS B 89 1 15
HELIX 25 25 THR B 107 ASN B 119 1 13
HELIX 26 26 GLN B 146 CYS B 151 1 6
HELIX 27 27 ASP B 157 PHE B 170 1 14
HELIX 28 28 GLU B 171 PHE B 173 5 3
HELIX 29 29 ALA B 195 SER B 199 5 5
HELIX 30 30 TRP B 217 CYS B 222 1 6
HELIX 31 31 GLU B 223 ALA B 230 1 8
HELIX 32 32 ASN B 260 CYS B 263 5 4
HELIX 33 33 GLY B 267 CYS B 273 1 7
HELIX 34 34 TRP B 318 ALA B 336 1 19
HELIX 35 35 ARG B 341 GLY B 350 1 10
HELIX 36 36 GLY B 350 CYS B 358 1 9
HELIX 37 37 SER B 363 ILE B 367 5 5
HELIX 38 38 ARG B 371 THR B 377 5 7
HELIX 39 39 LYS C 21 TRP C 25 5 5
HELIX 40 40 GLU C 28 LYS C 34 1 7
HELIX 41 41 THR C 43 GLY C 61 1 19
HELIX 42 42 MET C 65 GLY C 74 1 10
HELIX 43 43 LYS C 76 PHE C 84 1 9
HELIX 44 44 SER C 86 GLY C 91 1 6
HELIX 45 45 GLY C 91 GLY C 97 1 7
HELIX 46 46 LEU D 8 SER D 14 5 7
HELIX 47 47 SER D 19 ASN D 34 1 16
HELIX 48 48 ASP D 45 GLY D 61 1 17
HELIX 49 49 PHE D 91 ALA D 95 5 5
HELIX 50 50 THR D 112 GLY D 126 1 15
HELIX 51 51 PRO D 147 ASN D 161 1 15
HELIX 52 52 LEU D 178 ARG D 182 5 5
HELIX 53 53 ASP D 189 TYR D 201 1 13
HELIX 54 54 TYR D 201 ARG D 207 1 7
HELIX 55 55 ALA D 227 SER D 232 1 6
HELIX 56 56 ASP D 247 GLY D 256 1 10
HELIX 57 57 GLN D 260 ALA D 265 5 6
HELIX 58 58 ASP D 275 VAL D 280 1 6
HELIX 59 59 ASN D 300 CYS D 303 5 4
HELIX 60 60 MET D 307 MET D 313 1 7
HELIX 61 61 TYR D 355 GLY D 373 1 19
HELIX 62 62 ARG D 378 GLY D 387 1 10
HELIX 63 63 GLY D 387 VAL D 395 1 9
HELIX 64 64 VAL D 400 HIS D 403 5 4
HELIX 65 65 LYS D 416 VAL D 420 5 5
HELIX 66 66 ASP D 427 HIS D 435 1 9
HELIX 67 67 HIS E 25 PHE E 29 5 5
HELIX 68 68 PRO E 31 LYS E 38 1 8
HELIX 69 69 VAL E 75 CYS E 89 1 15
HELIX 70 70 THR E 107 ASN E 119 1 13
HELIX 71 71 GLN E 146 HIS E 150 5 5
HELIX 72 72 ASP E 157 PHE E 170 1 14
HELIX 73 73 GLU E 171 PHE E 173 5 3
HELIX 74 74 ALA E 195 SER E 199 5 5
HELIX 75 75 ASP E 214 CYS E 222 1 9
HELIX 76 76 GLU E 223 ALA E 230 1 8
HELIX 77 77 ASN E 260 CYS E 263 5 4
HELIX 78 78 GLY E 267 CYS E 273 1 7
HELIX 79 79 TRP E 318 ALA E 336 1 19
HELIX 80 80 ARG E 341 GLY E 350 1 10
HELIX 81 81 GLY E 350 CYS E 358 1 9
HELIX 82 82 SER E 363 ILE E 367 5 5
HELIX 83 83 PRO E 373 TRP E 378 1 6
HELIX 84 84 LYS F 21 TRP F 25 5 5
HELIX 85 85 GLU F 28 LYS F 34 1 7
HELIX 86 86 THR F 43 GLY F 61 1 19
HELIX 87 87 MET F 65 GLY F 74 1 10
HELIX 88 88 LYS F 76 PHE F 84 1 9
HELIX 89 89 SER F 86 GLY F 91 1 6
HELIX 90 90 GLY F 91 GLY F 97 1 7
SHEET 1 AA 5 VAL A 80 ILE A 81 0
SHEET 2 AA 5 THR A 99 VAL A 102 -1 O THR A 99 N ILE A 81
SHEET 3 AA 5 ILE A 139 LEU A 142 -1 O ILE A 139 N VAL A 102
SHEET 4 AA 5 LEU A 129 ASN A 131 -1 O LEU A 129 N LEU A 142
SHEET 5 AA 5 LEU B 72 SER B 74 -1 O MET B 73 N THR A 130
SHEET 1 AB 6 TYR A 109 THR A 111 0
SHEET 2 AB 6 HIS B 92 PHE B 95 -1 O LEU B 93 N TYR A 110
SHEET 3 AB 6 ILE B 101 VAL B 105 -1 O GLU B 102 N ARG B 94
SHEET 4 AB 6 GLU B 61 CYS B 67 -1 O TYR B 63 N VAL B 105
SHEET 5 AB 6 ILE B 51 ALA B 56 -1 O LEU B 52 N THR B 64
SHEET 6 AB 6 TRP B 41 GLU B 48 -1 N LEU B 42 O LYS B 55
SHEET 1 AC 5 ALA A 175 SER A 176 0
SHEET 2 AC 5 PHE A 216 ASP A 219 1 O PHE A 216 N ALA A 175
SHEET 3 AC 5 MET A 234 TRP A 240 1 O MET A 234 N LYS A 217
SHEET 4 AC 5 ARG A 323 VAL A 329 -1 O GLY A 324 N THR A 239
SHEET 5 AC 5 SER A 343 ILE A 349 -1 O SER A 343 N VAL A 329
SHEET 1 AD 2 ARG A 245 ILE A 246 0
SHEET 2 AD 2 LEU A 317 ARG A 318 -1 O ARG A 318 N ARG A 245
SHEET 1 AE 2 MET A 289 GLU A 292 0
SHEET 2 AE 2 LYS A 295 ILE A 298 -1 O LYS A 295 N GLU A 292
SHEET 1 BA 4 ILE B 184 ALA B 187 0
SHEET 2 BA 4 ILE B 201 TYR B 206 1 O ILE B 201 N SER B 185
SHEET 3 BA 4 GLY B 285 ALA B 290 -1 O GLY B 285 N TYR B 206
SHEET 4 BA 4 LYS B 305 PRO B 312 -1 O LYS B 305 N ALA B 290
SHEET 1 BB 2 ILE B 236 VAL B 244 0
SHEET 2 BB 2 THR B 250 ILE B 258 -1 O LYS B 251 N ILE B 243
SHEET 1 CA 2 MET C 3 PHE C 6 0
SHEET 2 CA 2 LYS C 9 GLU C 12 -1 O LYS C 9 N PHE C 6
SHEET 1 DA 5 VAL D 80 ILE D 81 0
SHEET 2 DA 5 THR D 99 VAL D 102 -1 O THR D 99 N ILE D 81
SHEET 3 DA 5 ILE D 139 LEU D 142 -1 O ILE D 139 N VAL D 102
SHEET 4 DA 5 LEU D 129 ASN D 131 -1 O LEU D 129 N LEU D 142
SHEET 5 DA 5 LEU E 72 SER E 74 -1 O MET E 73 N THR D 130
SHEET 1 DB 6 TYR D 109 THR D 111 0
SHEET 2 DB 6 HIS E 92 PHE E 95 -1 O LEU E 93 N TYR D 110
SHEET 3 DB 6 ILE E 101 VAL E 105 -1 O GLU E 102 N ARG E 94
SHEET 4 DB 6 GLU E 61 CYS E 67 -1 O TYR E 63 N VAL E 105
SHEET 5 DB 6 ILE E 51 ALA E 56 -1 O LEU E 52 N THR E 64
SHEET 6 DB 6 TRP E 41 GLU E 48 -1 N LEU E 42 O LYS E 55
SHEET 1 DC 5 ALA D 175 SER D 176 0
SHEET 2 DC 5 PHE D 216 ASP D 219 1 O PHE D 216 N ALA D 175
SHEET 3 DC 5 MET D 234 TRP D 240 1 O MET D 234 N LYS D 217
SHEET 4 DC 5 ARG D 323 VAL D 329 -1 O GLY D 324 N THR D 239
SHEET 5 DC 5 SER D 343 ILE D 349 -1 O SER D 343 N VAL D 329
SHEET 1 DD 2 ARG D 245 ILE D 246 0
SHEET 2 DD 2 LEU D 317 ARG D 318 -1 O ARG D 318 N ARG D 245
SHEET 1 DE 2 MET D 289 GLU D 292 0
SHEET 2 DE 2 LYS D 295 ILE D 298 -1 O LYS D 295 N GLU D 292
SHEET 1 EA 4 ILE E 184 ALA E 187 0
SHEET 2 EA 4 ILE E 201 TYR E 206 1 O ILE E 201 N SER E 185
SHEET 3 EA 4 GLY E 285 ALA E 290 -1 O GLY E 285 N TYR E 206
SHEET 4 EA 4 LYS E 305 PRO E 312 -1 O LYS E 305 N ALA E 290
SHEET 1 EB 2 ILE E 236 VAL E 244 0
SHEET 2 EB 2 THR E 250 ILE E 258 -1 O LYS E 251 N ILE E 243
SHEET 1 FA 2 MET F 3 PHE F 6 0
SHEET 2 FA 2 LYS F 9 GLU F 12 -1 O LYS F 9 N PHE F 6
SSBOND 1 CYS B 222 CYS B 273 1555 1555 2.04
SSBOND 2 CYS E 222 CYS E 273 1555 1555 2.05
LINK CHA SRM B 503 SG CYS C 104 1555 1555 1.80
LINK CHA SRM E 503 SG CYS F 104 1555 1555 1.80
LINK SG CYS A 177 FE1 SF4 A 502 1555 1555 2.30
LINK SG CYS A 183 FE2 SF4 A 502 1555 1555 2.29
LINK SG CYS A 221 FE3 SF4 A 502 1555 1555 2.26
LINK SG CYS A 225 FE4 SF4 A 502 1555 1555 2.26
LINK SG CYS A 225 FE SRM A 503 1555 1555 2.48
LINK SG CYS A 284 FE3 SF4 A 501 1555 1555 2.29
LINK SG CYS A 303 FE1 SF4 A 501 1555 1555 2.30
LINK SG CYS A 306 FE4 SF4 A 501 1555 1555 2.28
LINK SG CYS A 309 FE2 SF4 A 501 1555 1555 2.28
LINK SG CYS B 151 FE4 SF4 B 502 1555 1555 2.33
LINK SG CYS B 188 FE3 SF4 B 502 1555 1555 2.38
LINK SG CYS B 189 FE1 SF4 B 502 1555 1555 2.29
LINK SG CYS B 193 FE2 SF4 B 502 1555 1555 2.32
LINK SG CYS B 193 FE SRM B 503 1555 1555 2.44
LINK SG CYS B 231 FE1 SF4 B 501 1555 1555 2.28
LINK SG CYS B 263 FE2 SF4 B 501 1555 1555 2.31
LINK SG CYS B 266 FE4 SF4 B 501 1555 1555 2.31
LINK SG CYS B 269 FE3 SF4 B 501 1555 1555 2.28
LINK FE SRM B 503 S SO3 B 504 1555 1555 2.29
LINK SG CYS D 177 FE1 SF4 D 502 1555 1555 2.33
LINK SG CYS D 183 FE2 SF4 D 502 1555 1555 2.29
LINK SG CYS D 221 FE3 SF4 D 502 1555 1555 2.26
LINK SG CYS D 225 FE4 SF4 D 502 1555 1555 2.27
LINK SG CYS D 225 FE SRM D 503 1555 1555 2.52
LINK SG CYS D 284 FE3 SF4 D 501 1555 1555 2.32
LINK SG CYS D 303 FE1 SF4 D 501 1555 1555 2.32
LINK SG CYS D 306 FE4 SF4 D 501 1555 1555 2.32
LINK SG CYS D 309 FE2 SF4 D 501 1555 1555 2.24
LINK SG CYS E 151 FE2 SF4 E 502 1555 1555 2.31
LINK SG CYS E 188 FE4 SF4 E 502 1555 1555 2.38
LINK SG CYS E 189 FE1 SF4 E 502 1555 1555 2.27
LINK SG CYS E 193 FE3 SF4 E 502 1555 1555 2.31
LINK SG CYS E 193 FE SRM E 503 1555 1555 2.45
LINK SG CYS E 231 FE1 SF4 E 501 1555 1555 2.27
LINK SG CYS E 263 FE4 SF4 E 501 1555 1555 2.31
LINK SG CYS E 266 FE3 SF4 E 501 1555 1555 2.30
LINK SG CYS E 269 FE2 SF4 E 501 1555 1555 2.33
LINK FE SRM E 503 S SO3 E 504 1555 1555 2.31
CISPEP 1 MET A 132 HIS A 133 0 -5.43
CISPEP 2 ILE A 335 LEU A 336 0 -3.60
CISPEP 3 ASP A 353 PRO A 354 0 8.52
CISPEP 4 PRO B 315 PRO B 316 0 7.98
CISPEP 5 MET D 132 HIS D 133 0 -0.02
CISPEP 6 ILE D 335 LEU D 336 0 4.20
CISPEP 7 ASP D 353 PRO D 354 0 14.02
CISPEP 8 PRO E 315 PRO E 316 0 5.96
SITE 1 AC1 7 CYS A 284 CYS A 288 CYS A 303 THR A 304
SITE 2 AC1 7 CYS A 306 MET A 307 CYS A 309
SITE 1 AC2 8 CYS A 177 CYS A 183 TRP A 185 ALA A 186
SITE 2 AC2 8 GLY A 220 CYS A 221 ASN A 223 CYS A 225
SITE 1 AC3 43 CYS A 177 LEU A 178 ARG A 182 CYS A 183
SITE 2 AC3 43 GLU A 184 TRP A 185 ASN A 223 GLY A 224
SITE 3 AC3 43 CYS A 225 ASN A 262 ASN A 311 HOH A2122
SITE 4 AC3 43 HOH A2124 HOH A2150 HOH A2151 HOH A2180
SITE 5 AC3 43 HOH A2307 HOH A2308 HOH A2309 HOH A2310
SITE 6 AC3 43 HOH A2311 HOH A2313 HOH A2314 HOH A2315
SITE 7 AC3 43 HOH A2316 HIS B 44 ILE B 46 HIS B 54
SITE 8 AC3 43 ARG B 66 ARG B 94 THR B 96 THR B 97
SITE 9 AC3 43 ARG B 98 ASN B 100 THR B 135 GLY B 136
SITE 10 AC3 43 THR B 140 ARG B 183 LYS B 293 VAL B 294
SITE 11 AC3 43 SER B 295 ARG B 297 ARG B 341
SITE 1 AC4 7 CYS B 231 ILE B 236 CYS B 263 MET B 264
SITE 2 AC4 7 CYS B 266 GLY B 267 CYS B 269
SITE 1 AC5 10 THR B 145 GLN B 146 CYS B 151 THR B 153
SITE 2 AC5 10 PRO B 154 CYS B 188 CYS B 189 ASN B 191
SITE 3 AC5 10 CYS B 193 SRM B 503
SITE 1 AC6 36 ARG A 83 ARG A 101 GLY A 134 ALA A 135
SITE 2 AC6 36 THR A 136 GLY A 137 ASP A 138 TYR A 212
SITE 3 AC6 36 LYS A 213 LYS A 215 LYS A 217 ARG A 231
SITE 4 AC6 36 LYS A 332 ALA A 333 ILE A 335 ARG A 376
SITE 5 AC6 36 ARG A 378 HOH A2070 HOH A2080 HOH A2081
SITE 6 AC6 36 HOH A2097 ARG B 71 HIS B 144 THR B 145
SITE 7 AC6 36 GLN B 146 HIS B 150 CYS B 151 HIS B 152
SITE 8 AC6 36 ASN B 191 MET B 192 CYS B 193 GLY B 194
SITE 9 AC6 36 SF4 B 502 SO3 B 504 GLY C 103 CYS C 104
SITE 1 AC7 6 ARG A 101 ARG A 172 LYS A 213 LYS A 215
SITE 2 AC7 6 SRM B 503 CYS C 104
SITE 1 AC8 7 CYS D 284 CYS D 288 CYS D 303 THR D 304
SITE 2 AC8 7 CYS D 306 MET D 307 CYS D 309
SITE 1 AC9 6 CYS D 177 CYS D 183 TRP D 185 ALA D 186
SITE 2 AC9 6 CYS D 221 CYS D 225
SITE 1 BC1 42 CYS D 177 LEU D 178 ARG D 182 CYS D 183
SITE 2 BC1 42 GLU D 184 TRP D 185 ASN D 223 GLY D 224
SITE 3 BC1 42 CYS D 225 ASN D 262 ASN D 311 HOH D2120
SITE 4 BC1 42 HOH D2123 HOH D2156 HOH D2157 HOH D2274
SITE 5 BC1 42 HOH D2275 HOH D2276 HOH D2277 HOH D2278
SITE 6 BC1 42 HOH D2279 HOH D2280 HOH D2281 HIS E 44
SITE 7 BC1 42 LEU E 52 HIS E 54 ARG E 66 ARG E 94
SITE 8 BC1 42 THR E 96 THR E 97 ARG E 98 ASN E 100
SITE 9 BC1 42 GLY E 134 THR E 135 GLY E 136 THR E 140
SITE 10 BC1 42 ARG E 183 LYS E 293 VAL E 294 SER E 295
SITE 11 BC1 42 ARG E 297 ARG E 341
SITE 1 BC2 7 CYS E 231 ILE E 236 CYS E 263 MET E 264
SITE 2 BC2 7 CYS E 266 GLY E 267 CYS E 269
SITE 1 BC3 10 THR E 145 GLN E 146 CYS E 151 THR E 153
SITE 2 BC3 10 PRO E 154 CYS E 188 CYS E 189 ASN E 191
SITE 3 BC3 10 CYS E 193 SRM E 503
SITE 1 BC4 35 ARG D 83 ARG D 101 GLY D 134 ALA D 135
SITE 2 BC4 35 THR D 136 GLY D 137 ASP D 138 TYR D 212
SITE 3 BC4 35 LYS D 213 LYS D 215 LYS D 217 ARG D 231
SITE 4 BC4 35 LYS D 332 ALA D 333 ILE D 335 ARG D 376
SITE 5 BC4 35 ARG D 378 HOH D2066 HOH D2077 HOH D2078
SITE 6 BC4 35 HOH D2093 ARG E 71 HIS E 144 THR E 145
SITE 7 BC4 35 GLN E 146 HIS E 150 CYS E 151 HIS E 152
SITE 8 BC4 35 ASN E 191 MET E 192 CYS E 193 SF4 E 502
SITE 9 BC4 35 SO3 E 504 GLY F 103 CYS F 104
SITE 1 BC5 6 ARG D 101 ARG D 172 LYS D 213 LYS D 215
SITE 2 BC5 6 SRM E 503 CYS F 104
CRYST1 99.340 135.090 178.030 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 0.010066 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007402 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005617 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
