HEADER OXIDOREDUCTASE 28-APR-05 1ZJ9
TITLE STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS NIRA PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE FERREDOXIN-DEPENDENT NITRITE REDUCTASE NIRA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 3-555;
COMPND 5 SYNONYM: SULFITE REDUCTASE NIRA;
COMPND 6 EC: 1.7.7.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: NIRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS NIRA, SULFITE, NITRITE, REDUCTASE, SIROHEME, FE4-S4, CYS-TYR COVALENT
KEYWDS 2 BOND, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SCHNELL,T.SANDALOVA,U.HELLMAN,Y.LINDQVIST,G.SCHNEIDER
REVDAT 6 27-DEC-23 1ZJ9 1 COMPND FORMUL
REVDAT 5 25-OCT-23 1ZJ9 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1ZJ9 1 VERSN
REVDAT 3 24-FEB-09 1ZJ9 1 VERSN
REVDAT 2 02-AUG-05 1ZJ9 1 JRNL
REVDAT 1 31-MAY-05 1ZJ9 0
JRNL AUTH R.SCHNELL,T.SANDALOVA,U.HELLMAN,Y.LINDQVIST,G.SCHNEIDER
JRNL TITL SIROHEME- AND [FE4-S4]-DEPENDENT NIRA FROM MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS IS A SULFITE REDUCTASE WITH A COVALENT CYS-TYR
JRNL TITL 3 BOND IN THE ACTIVE SITE
JRNL REF J.BIOL.CHEM. V. 280 27319 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15917234
JRNL DOI 10.1074/JBC.M502560200
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 22013
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1659
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.4270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8632
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 144
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30000
REMARK 3 B22 (A**2) : -2.61000
REMARK 3 B33 (A**2) : 1.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.524
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.433
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.446
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8982 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12220 ; 1.592 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1090 ; 6.694 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 446 ;38.297 ;23.184
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1484 ;20.184 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;21.109 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1294 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6976 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4547 ; 0.244 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6028 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 332 ; 0.187 ; 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): 62 ; 0.255 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.195 ; 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): 5516 ; 0.495 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8668 ; 0.843 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4484 ; 0.981 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3525 ; 1.590 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 555 4
REMARK 3 1 B 10 B 555 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4316 ; 0.34 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4316 ; 0.65 ; 2.00
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZJ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032777.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-04
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 : ID14-1
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 QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23209
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33800
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: MOLREP
REMARK 200 STARTING MODEL: 2GET
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS-HCL, MAGNESIUM
REMARK 280 CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.65350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER IN A COMPLEX WITH
REMARK 300 SIROHEME AND FE4-S4 CLUSTER
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -10
REMARK 465 ASP A -9
REMARK 465 VAL A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 ARG A 5
REMARK 465 PRO A 6
REMARK 465 ALA A 7
REMARK 465 LYS A 8
REMARK 465 ALA A 9
REMARK 465 MET B -10
REMARK 465 ASP B -9
REMARK 465 VAL B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 ARG B 5
REMARK 465 PRO B 6
REMARK 465 ALA B 7
REMARK 465 LYS B 8
REMARK 465 ALA B 9
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 ND2 ASN A 132 O1B SRM A 569 1.99
REMARK 500 NH2 ARG A 206 O4D SRM A 569 2.15
REMARK 500 SG CYS B 417 FE4 SF4 B 1556 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 100 CB CYS A 100 SG -0.102
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 32 78.69 -103.56
REMARK 500 ILE A 45 -68.20 -104.54
REMARK 500 ASP A 55 137.70 -37.20
REMARK 500 ASP A 101 98.11 -55.68
REMARK 500 ARG A 166 -178.29 -62.41
REMARK 500 ALA A 219 50.75 36.92
REMARK 500 GLU A 221 -9.81 -58.63
REMARK 500 SER A 248 -96.71 -46.86
REMARK 500 ARG A 284 -63.68 -91.55
REMARK 500 ASN A 339 -37.31 -37.14
REMARK 500 ARG A 406 57.70 -119.19
REMARK 500 HIS A 409 -55.68 -23.91
REMARK 500 CYS A 417 -161.76 -77.86
REMARK 500 THR A 430 -52.44 -120.62
REMARK 500 SER A 466 38.98 71.74
REMARK 500 ARG A 469 66.49 60.22
REMARK 500 ARG A 512 -75.26 -50.77
REMARK 500 TRP B 15 -35.16 -34.10
REMARK 500 HIS B 19 69.23 -68.07
REMARK 500 LEU B 36 -8.31 -58.54
REMARK 500 ILE B 45 -67.85 -106.07
REMARK 500 LYS B 56 8.01 -59.61
REMARK 500 TRP B 65 -7.61 -54.47
REMARK 500 ASP B 123 16.17 58.22
REMARK 500 ASP B 129 9.05 -68.10
REMARK 500 GLN B 131 37.07 77.39
REMARK 500 GLU B 141 -59.33 -26.54
REMARK 500 LYS B 207 135.44 -25.84
REMARK 500 GLN B 216 59.51 -90.39
REMARK 500 SER B 248 -99.81 -53.36
REMARK 500 LYS B 288 44.46 -144.37
REMARK 500 GLN B 379 37.55 70.12
REMARK 500 ALA B 400 -18.06 -45.52
REMARK 500 PHE B 422 -21.28 -148.84
REMARK 500 THR B 430 -54.61 -120.47
REMARK 500 ARG B 469 70.66 59.41
REMARK 500 ARG B 512 -70.72 -62.84
REMARK 500 GLN B 513 51.97 -114.41
REMARK 500 LYS B 534 -71.36 -66.33
REMARK 500 ALA B 549 136.04 -36.09
REMARK 500 GLU B 551 -18.31 -45.78
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 556 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 417 SG
REMARK 620 2 SF4 A 556 S2 54.0
REMARK 620 3 SF4 A 556 S3 50.1 103.9
REMARK 620 4 SF4 A 556 S4 114.1 106.8 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 556 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 423 SG
REMARK 620 2 SF4 A 556 S1 60.1
REMARK 620 3 SF4 A 556 S3 120.1 101.7
REMARK 620 4 SF4 A 556 S4 46.2 106.1 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 556 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 463 SG
REMARK 620 2 SF4 A 556 S1 122.2
REMARK 620 3 SF4 A 556 S2 54.2 104.1
REMARK 620 4 SF4 A 556 S4 52.6 105.9 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 556 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 467 SG
REMARK 620 2 SF4 A 556 S1 54.0
REMARK 620 3 SF4 A 556 S2 120.9 105.0
REMARK 620 4 SF4 A 556 S3 50.3 103.8 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1556 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 417 SG
REMARK 620 2 SF4 B1556 S2 54.3
REMARK 620 3 SF4 B1556 S3 50.1 102.6
REMARK 620 4 SF4 B1556 S4 105.8 106.1 107.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1556 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 423 SG
REMARK 620 2 SF4 B1556 S1 62.0
REMARK 620 3 SF4 B1556 S3 125.6 105.0
REMARK 620 4 SF4 B1556 S4 43.0 104.1 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1556 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 463 SG
REMARK 620 2 SF4 B1556 S1 120.5
REMARK 620 3 SF4 B1556 S2 51.2 105.6
REMARK 620 4 SF4 B1556 S4 55.2 103.9 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1556 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 467 SG
REMARK 620 2 SF4 B1556 S1 61.8
REMARK 620 3 SF4 B1556 S2 113.3 105.4
REMARK 620 4 SF4 B1556 S3 44.7 106.4 103.6
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 CL A 570
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM A 569
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM B 1569
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZJ8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
DBREF 1ZJ9 A 3 555 UNP P71753 SIR_MYCTU 11 563
DBREF 1ZJ9 B 3 555 UNP P71753 SIR_MYCTU 11 563
SEQADV 1ZJ9 MET A -10 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 ASP A -9 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 VAL A -8 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 SER A -7 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS A -6 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS A -5 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS A -4 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS A -3 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS A -2 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS A -1 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 GLY A 0 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 MET A 1 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 ALA A 2 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 MET B -10 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 ASP B -9 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 VAL B -8 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 SER B -7 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS B -6 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS B -5 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS B -4 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS B -3 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS B -2 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 HIS B -1 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 GLY B 0 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 MET B 1 UNP P71753 EXPRESSION TAG
SEQADV 1ZJ9 ALA B 2 UNP P71753 EXPRESSION TAG
SEQRES 1 A 566 MET ASP VAL SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 566 THR ALA ARG PRO ALA LYS ALA ARG ASN GLU GLY GLN TRP
SEQRES 3 A 566 ALA LEU GLY HIS ARG GLU PRO LEU ASN ALA ASN GLU GLU
SEQRES 4 A 566 LEU LYS LYS ALA GLY ASN PRO LEU ASP VAL ARG GLU ARG
SEQRES 5 A 566 ILE GLU ASN ILE TYR ALA LYS GLN GLY PHE ASP SER ILE
SEQRES 6 A 566 ASP LYS THR ASP LEU ARG GLY ARG PHE ARG TRP TRP GLY
SEQRES 7 A 566 LEU TYR THR GLN ARG GLU GLN GLY TYR ASP GLY THR TRP
SEQRES 8 A 566 THR GLY ASP ASP ASN ILE ASP LYS LEU GLU ALA LYS TYR
SEQRES 9 A 566 PHE MET MET ARG VAL ARG CYS ASP GLY GLY ALA LEU SER
SEQRES 10 A 566 ALA ALA ALA LEU ARG THR LEU GLY GLN ILE SER THR GLU
SEQRES 11 A 566 PHE ALA ARG ASP THR ALA ASP ILE SER ASP ARG GLN ASN
SEQRES 12 A 566 VAL GLN TYR HIS TRP ILE GLU VAL GLU ASN VAL PRO GLU
SEQRES 13 A 566 ILE TRP ARG ARG LEU ASP ASP VAL GLY LEU GLN THR THR
SEQRES 14 A 566 GLU ALA CYS GLY ASP CYS PRO ARG VAL VAL LEU GLY SER
SEQRES 15 A 566 PRO LEU ALA GLY GLU SER LEU ASP GLU VAL LEU ASP PRO
SEQRES 16 A 566 THR TRP ALA ILE GLU GLU ILE VAL ARG ARG TYR ILE GLY
SEQRES 17 A 566 LYS PRO ASP PHE ALA ASP LEU PRO ARG LYS TYR LYS THR
SEQRES 18 A 566 ALA ILE SER GLY LEU GLN ASP VAL ALA HIS GLU ILE ASN
SEQRES 19 A 566 ASP VAL ALA PHE ILE GLY VAL ASN HIS PRO GLU HIS GLY
SEQRES 20 A 566 PRO GLY LEU ASP LEU TRP VAL GLY GLY GLY LEU SER THR
SEQRES 21 A 566 ASN PRO MET LEU ALA GLN ARG VAL GLY ALA TRP VAL PRO
SEQRES 22 A 566 LEU GLY GLU VAL PRO GLU VAL TRP ALA ALA VAL THR SER
SEQRES 23 A 566 VAL PHE ARG ASP TYR GLY TYR ARG ARG LEU ARG ALA LYS
SEQRES 24 A 566 ALA ARG LEU LYS PHE LEU ILE LYS ASP TRP GLY ILE ALA
SEQRES 25 A 566 LYS PHE ARG GLU VAL LEU GLU THR GLU TYR LEU LYS ARG
SEQRES 26 A 566 PRO LEU ILE ASP GLY PRO ALA PRO GLU PRO VAL LYS HIS
SEQRES 27 A 566 PRO ILE ASP HIS VAL GLY VAL GLN ARG LEU LYS ASN GLY
SEQRES 28 A 566 LEU ASN ALA VAL GLY VAL ALA PRO ILE ALA GLY ARG VAL
SEQRES 29 A 566 SER GLY THR ILE LEU THR ALA VAL ALA ASP LEU MET ALA
SEQRES 30 A 566 ARG ALA GLY SER ASP ARG ILE ARG PHE THR PRO TYR GLN
SEQRES 31 A 566 LYS LEU VAL ILE LEU ASP ILE PRO ASP ALA LEU LEU ASP
SEQRES 32 A 566 ASP LEU ILE ALA GLY LEU ASP ALA LEU GLY LEU GLN SER
SEQRES 33 A 566 ARG PRO SER HIS TRP ARG ARG ASN LEU MET ALA CYS SER
SEQRES 34 A 566 GLY ILE GLU PHE CYS LYS LEU SER PHE ALA GLU THR ARG
SEQRES 35 A 566 VAL ARG ALA GLN HIS LEU VAL PRO GLU LEU GLU ARG ARG
SEQRES 36 A 566 LEU GLU ASP ILE ASN SER GLN LEU ASP VAL PRO ILE THR
SEQRES 37 A 566 VAL ASN ILE ASN GLY CYS PRO ASN SER CYS ALA ARG ILE
SEQRES 38 A 566 GLN ILE ALA ASP ILE GLY PHE LYS GLY GLN MET ILE ASP
SEQRES 39 A 566 ASP GLY HIS GLY GLY SER VAL GLU GLY PHE GLN VAL HIS
SEQRES 40 A 566 LEU GLY GLY HIS LEU GLY LEU ASP ALA GLY PHE GLY ARG
SEQRES 41 A 566 LYS LEU ARG GLN HIS LYS VAL THR SER ASP GLU LEU GLY
SEQRES 42 A 566 ASP TYR ILE ASP ARG VAL VAL ARG ASN PHE VAL LYS HIS
SEQRES 43 A 566 ARG SER GLU GLY GLU ARG PHE ALA GLN TRP VAL ILE ARG
SEQRES 44 A 566 ALA GLU GLU ASP ASP LEU ARG
SEQRES 1 B 566 MET ASP VAL SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 B 566 THR ALA ARG PRO ALA LYS ALA ARG ASN GLU GLY GLN TRP
SEQRES 3 B 566 ALA LEU GLY HIS ARG GLU PRO LEU ASN ALA ASN GLU GLU
SEQRES 4 B 566 LEU LYS LYS ALA GLY ASN PRO LEU ASP VAL ARG GLU ARG
SEQRES 5 B 566 ILE GLU ASN ILE TYR ALA LYS GLN GLY PHE ASP SER ILE
SEQRES 6 B 566 ASP LYS THR ASP LEU ARG GLY ARG PHE ARG TRP TRP GLY
SEQRES 7 B 566 LEU TYR THR GLN ARG GLU GLN GLY TYR ASP GLY THR TRP
SEQRES 8 B 566 THR GLY ASP ASP ASN ILE ASP LYS LEU GLU ALA LYS TYR
SEQRES 9 B 566 PHE MET MET ARG VAL ARG CYS ASP GLY GLY ALA LEU SER
SEQRES 10 B 566 ALA ALA ALA LEU ARG THR LEU GLY GLN ILE SER THR GLU
SEQRES 11 B 566 PHE ALA ARG ASP THR ALA ASP ILE SER ASP ARG GLN ASN
SEQRES 12 B 566 VAL GLN TYR HIS TRP ILE GLU VAL GLU ASN VAL PRO GLU
SEQRES 13 B 566 ILE TRP ARG ARG LEU ASP ASP VAL GLY LEU GLN THR THR
SEQRES 14 B 566 GLU ALA CYS GLY ASP CYS PRO ARG VAL VAL LEU GLY SER
SEQRES 15 B 566 PRO LEU ALA GLY GLU SER LEU ASP GLU VAL LEU ASP PRO
SEQRES 16 B 566 THR TRP ALA ILE GLU GLU ILE VAL ARG ARG TYR ILE GLY
SEQRES 17 B 566 LYS PRO ASP PHE ALA ASP LEU PRO ARG LYS TYR LYS THR
SEQRES 18 B 566 ALA ILE SER GLY LEU GLN ASP VAL ALA HIS GLU ILE ASN
SEQRES 19 B 566 ASP VAL ALA PHE ILE GLY VAL ASN HIS PRO GLU HIS GLY
SEQRES 20 B 566 PRO GLY LEU ASP LEU TRP VAL GLY GLY GLY LEU SER THR
SEQRES 21 B 566 ASN PRO MET LEU ALA GLN ARG VAL GLY ALA TRP VAL PRO
SEQRES 22 B 566 LEU GLY GLU VAL PRO GLU VAL TRP ALA ALA VAL THR SER
SEQRES 23 B 566 VAL PHE ARG ASP TYR GLY TYR ARG ARG LEU ARG ALA LYS
SEQRES 24 B 566 ALA ARG LEU LYS PHE LEU ILE LYS ASP TRP GLY ILE ALA
SEQRES 25 B 566 LYS PHE ARG GLU VAL LEU GLU THR GLU TYR LEU LYS ARG
SEQRES 26 B 566 PRO LEU ILE ASP GLY PRO ALA PRO GLU PRO VAL LYS HIS
SEQRES 27 B 566 PRO ILE ASP HIS VAL GLY VAL GLN ARG LEU LYS ASN GLY
SEQRES 28 B 566 LEU ASN ALA VAL GLY VAL ALA PRO ILE ALA GLY ARG VAL
SEQRES 29 B 566 SER GLY THR ILE LEU THR ALA VAL ALA ASP LEU MET ALA
SEQRES 30 B 566 ARG ALA GLY SER ASP ARG ILE ARG PHE THR PRO TYR GLN
SEQRES 31 B 566 LYS LEU VAL ILE LEU ASP ILE PRO ASP ALA LEU LEU ASP
SEQRES 32 B 566 ASP LEU ILE ALA GLY LEU ASP ALA LEU GLY LEU GLN SER
SEQRES 33 B 566 ARG PRO SER HIS TRP ARG ARG ASN LEU MET ALA CYS SER
SEQRES 34 B 566 GLY ILE GLU PHE CYS LYS LEU SER PHE ALA GLU THR ARG
SEQRES 35 B 566 VAL ARG ALA GLN HIS LEU VAL PRO GLU LEU GLU ARG ARG
SEQRES 36 B 566 LEU GLU ASP ILE ASN SER GLN LEU ASP VAL PRO ILE THR
SEQRES 37 B 566 VAL ASN ILE ASN GLY CYS PRO ASN SER CYS ALA ARG ILE
SEQRES 38 B 566 GLN ILE ALA ASP ILE GLY PHE LYS GLY GLN MET ILE ASP
SEQRES 39 B 566 ASP GLY HIS GLY GLY SER VAL GLU GLY PHE GLN VAL HIS
SEQRES 40 B 566 LEU GLY GLY HIS LEU GLY LEU ASP ALA GLY PHE GLY ARG
SEQRES 41 B 566 LYS LEU ARG GLN HIS LYS VAL THR SER ASP GLU LEU GLY
SEQRES 42 B 566 ASP TYR ILE ASP ARG VAL VAL ARG ASN PHE VAL LYS HIS
SEQRES 43 B 566 ARG SER GLU GLY GLU ARG PHE ALA GLN TRP VAL ILE ARG
SEQRES 44 B 566 ALA GLU GLU ASP ASP LEU ARG
HET CL A 570 1
HET SF4 A 556 8
HET SRM A 569 63
HET CL B1570 1
HET SF4 B1556 8
HET SRM B1569 63
HETNAM CL CHLORIDE ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM SRM SIROHEME
FORMUL 3 CL 2(CL 1-)
FORMUL 4 SF4 2(FE4 S4)
FORMUL 5 SRM 2(C42 H44 FE N4 O16)
FORMUL 9 HOH *16(H2 O)
HELIX 1 1 GLN A 14 GLY A 18 5 5
HELIX 2 2 ASN A 24 LYS A 31 1 8
HELIX 3 3 ASN A 34 LEU A 36 5 3
HELIX 4 4 ASP A 37 ILE A 45 1 9
HELIX 5 5 ILE A 45 GLY A 50 1 6
HELIX 6 6 PHE A 51 ILE A 54 5 4
HELIX 7 7 ASP A 55 GLY A 61 1 7
HELIX 8 8 ARG A 62 TRP A 66 5 5
HELIX 9 9 ASP A 77 THR A 81 5 5
HELIX 10 10 GLY A 82 ASP A 84 5 3
HELIX 11 11 ASN A 85 LEU A 89 1 5
HELIX 12 12 SER A 106 ALA A 121 1 16
HELIX 13 13 GLU A 139 GLU A 141 5 3
HELIX 14 14 ASN A 142 ASP A 152 1 11
HELIX 15 15 PRO A 184 ILE A 196 1 13
HELIX 16 16 LYS A 198 ALA A 202 5 5
HELIX 17 17 ALA A 219 ASN A 223 5 5
HELIX 18 18 PRO A 262 GLY A 264 5 3
HELIX 19 19 GLU A 265 GLY A 281 1 17
HELIX 20 20 LEU A 285 ALA A 289 5 5
HELIX 21 21 ARG A 290 GLY A 299 1 10
HELIX 22 22 GLY A 299 TYR A 311 1 13
HELIX 23 23 GLY A 355 GLY A 369 1 15
HELIX 24 24 PRO A 387 LEU A 390 5 4
HELIX 25 25 LEU A 391 ALA A 400 1 10
HELIX 26 26 SER A 408 ASN A 413 1 6
HELIX 27 27 SER A 418 PHE A 422 5 5
HELIX 28 28 THR A 430 GLU A 446 1 17
HELIX 29 29 ILE A 448 LEU A 452 5 5
HELIX 30 30 ARG A 469 ALA A 473 5 5
HELIX 31 31 GLU A 520 ARG A 536 1 17
HELIX 32 32 ARG A 541 ALA A 549 1 9
HELIX 33 33 GLU A 550 ARG A 555 5 6
HELIX 34 34 GLN B 14 GLY B 18 5 5
HELIX 35 35 ASN B 24 ALA B 32 1 9
HELIX 36 36 ASN B 34 LEU B 36 5 3
HELIX 37 37 ASP B 37 ILE B 45 1 9
HELIX 38 38 ILE B 45 GLY B 50 1 6
HELIX 39 39 GLY B 61 TRP B 66 5 6
HELIX 40 40 ASP B 77 THR B 81 5 5
HELIX 41 41 ASN B 85 LEU B 89 1 5
HELIX 42 42 CYS B 100 GLY B 102 5 3
HELIX 43 43 SER B 106 ALA B 121 1 16
HELIX 44 44 GLU B 139 GLU B 141 5 3
HELIX 45 45 ASN B 142 ASP B 152 1 11
HELIX 46 46 PRO B 184 ILE B 196 1 13
HELIX 47 47 LYS B 198 ALA B 202 5 5
HELIX 48 48 ALA B 219 ASN B 223 5 5
HELIX 49 49 PRO B 262 GLY B 264 5 3
HELIX 50 50 GLU B 265 GLY B 281 1 17
HELIX 51 51 ARG B 290 TYR B 311 1 22
HELIX 52 52 GLY B 355 ALA B 368 1 14
HELIX 53 53 PRO B 387 LEU B 401 1 15
HELIX 54 54 SER B 408 ASN B 413 1 6
HELIX 55 55 SER B 418 PHE B 422 5 5
HELIX 56 56 THR B 430 LEU B 445 1 16
HELIX 57 57 GLU B 446 LEU B 452 5 7
HELIX 58 58 ASP B 519 HIS B 535 1 17
HELIX 59 59 ARG B 541 ALA B 549 1 9
HELIX 60 60 GLU B 550 ARG B 555 5 6
SHEET 1 A 5 LEU A 68 ARG A 72 0
SHEET 2 A 5 GLU A 90 VAL A 98 -1 O MET A 95 N TYR A 69
SHEET 3 A 5 VAL A 133 ILE A 138 -1 O TYR A 135 N MET A 96
SHEET 4 A 5 THR A 124 ILE A 127 -1 N ASP A 126 O GLN A 134
SHEET 5 A 5 ARG A 352 SER A 354 -1 O VAL A 353 N ALA A 125
SHEET 1 B 5 ALA A 104 LEU A 105 0
SHEET 2 B 5 ILE A 373 PHE A 375 -1 O ILE A 373 N LEU A 105
SHEET 3 B 5 LEU A 381 ILE A 386 -1 O VAL A 382 N ARG A 374
SHEET 4 B 5 ASN A 342 VAL A 346 -1 N ASN A 342 O ILE A 386
SHEET 5 B 5 GLY A 333 ARG A 336 -1 N GLY A 333 O GLY A 345
SHEET 1 C 5 PRO A 165 LEU A 169 0
SHEET 2 C 5 TYR A 208 SER A 213 1 O THR A 210 N LEU A 169
SHEET 3 C 5 VAL A 225 HIS A 232 1 O PHE A 227 N ALA A 211
SHEET 4 C 5 GLY A 236 VAL A 243 -1 O ASP A 240 N ILE A 228
SHEET 5 C 5 GLN A 255 VAL A 261 -1 O VAL A 261 N LEU A 239
SHEET 1 D 5 LEU A 414 ALA A 416 0
SHEET 2 D 5 VAL A 458 ASN A 461 1 O ILE A 460 N MET A 415
SHEET 3 D 5 ILE A 475 ASP A 483 1 O PHE A 477 N ASN A 459
SHEET 4 D 5 SER A 489 LEU A 497 -1 O VAL A 490 N ILE A 482
SHEET 5 D 5 ARG A 509 LYS A 510 -1 O ARG A 509 N LEU A 497
SHEET 1 E 5 LEU A 414 ALA A 416 0
SHEET 2 E 5 VAL A 458 ASN A 461 1 O ILE A 460 N MET A 415
SHEET 3 E 5 ILE A 475 ASP A 483 1 O PHE A 477 N ASN A 459
SHEET 4 E 5 SER A 489 LEU A 497 -1 O VAL A 490 N ILE A 482
SHEET 5 E 5 VAL A 516 THR A 517 -1 O VAL A 516 N PHE A 493
SHEET 1 F 5 LEU B 68 ARG B 72 0
SHEET 2 F 5 GLU B 90 VAL B 98 -1 O TYR B 93 N GLN B 71
SHEET 3 F 5 ASN B 132 ILE B 138 -1 O TYR B 135 N MET B 96
SHEET 4 F 5 THR B 124 SER B 128 -1 N SER B 128 O ASN B 132
SHEET 5 F 5 ARG B 352 SER B 354 -1 O VAL B 353 N ALA B 125
SHEET 1 G 5 ALA B 104 LEU B 105 0
SHEET 2 G 5 ILE B 373 PHE B 375 -1 O ILE B 373 N LEU B 105
SHEET 3 G 5 LEU B 381 ILE B 386 -1 O VAL B 382 N ARG B 374
SHEET 4 G 5 ASN B 342 VAL B 346 -1 N VAL B 346 O LEU B 381
SHEET 5 G 5 GLY B 333 ARG B 336 -1 N GLY B 333 O GLY B 345
SHEET 1 H 5 PRO B 165 LEU B 169 0
SHEET 2 H 5 TYR B 208 SER B 213 1 O ILE B 212 N LEU B 169
SHEET 3 H 5 VAL B 225 HIS B 232 1 O PHE B 227 N SER B 213
SHEET 4 H 5 GLY B 236 VAL B 243 -1 O ASP B 240 N ILE B 228
SHEET 5 H 5 GLN B 255 VAL B 261 -1 O VAL B 261 N LEU B 239
SHEET 1 I 5 LEU B 414 ALA B 416 0
SHEET 2 I 5 VAL B 458 ASN B 461 1 O ILE B 460 N MET B 415
SHEET 3 I 5 ILE B 475 ASP B 483 1 O PHE B 477 N ASN B 459
SHEET 4 I 5 SER B 489 LEU B 497 -1 O VAL B 490 N ILE B 482
SHEET 5 I 5 ARG B 509 THR B 517 -1 O VAL B 516 N PHE B 493
LINK CE1 TYR A 69 SG CYS A 161 1555 1555 1.76
LINK CE1 TYR B 69 SG CYS B 161 1555 1555 1.88
LINK SG CYS A 417 FE1 SF4 A 556 1555 1555 4.90
LINK SG CYS A 423 FE2 SF4 A 556 1555 1555 4.64
LINK SG CYS A 463 FE3 SF4 A 556 1555 1555 4.62
LINK SG CYS A 467 FE4 SF4 A 556 1555 1555 4.59
LINK SG CYS B 417 FE1 SF4 B1556 1555 1555 4.93
LINK SG CYS B 423 FE2 SF4 B1556 1555 1555 4.48
LINK SG CYS B 463 FE3 SF4 B1556 1555 1555 4.59
LINK SG CYS B 467 FE4 SF4 B1556 1555 1555 4.77
SITE 1 AC1 4 ARG A 97 ARG A 166 LYS A 207 SRM A 569
SITE 1 AC2 4 ARG B 97 ARG B 166 LYS B 207 SRM B1569
SITE 1 AC3 9 CYS A 417 SER A 418 CYS A 423 SER A 426
SITE 2 AC3 9 GLY A 462 CYS A 463 ASN A 465 CYS A 467
SITE 3 AC3 9 SRM A 569
SITE 1 AC4 30 TYR A 69 ARG A 97 SER A 128 ASP A 129
SITE 2 AC4 30 ARG A 130 ASN A 132 GLN A 134 HIS A 136
SITE 3 AC4 30 ARG A 206 LYS A 207 LYS A 209 ILE A 222
SITE 4 AC4 30 GLY A 246 LEU A 247 SER A 248 ARG A 290
SITE 5 AC4 30 GLN A 379 ALA A 416 CYS A 417 SER A 418
SITE 6 AC4 30 PHE A 422 CYS A 423 LEU A 425 ARG A 431
SITE 7 AC4 30 ASN A 465 SER A 466 CYS A 467 ARG A 469
SITE 8 AC4 30 SF4 A 556 CL A 570
SITE 1 AC5 8 CYS B 417 SER B 418 GLY B 419 CYS B 423
SITE 2 AC5 8 SER B 426 GLY B 462 CYS B 463 CYS B 467
SITE 1 AC6 30 TYR B 69 MET B 95 ARG B 97 SER B 128
SITE 2 AC6 30 ASP B 129 ARG B 130 ASN B 132 GLN B 134
SITE 3 AC6 30 HIS B 136 VAL B 167 ARG B 206 LYS B 207
SITE 4 AC6 30 LYS B 209 ILE B 222 GLY B 246 LEU B 247
SITE 5 AC6 30 SER B 248 ARG B 290 GLN B 379 ALA B 416
SITE 6 AC6 30 CYS B 417 SER B 418 PHE B 422 CYS B 423
SITE 7 AC6 30 ARG B 431 ASN B 465 SER B 466 CYS B 467
SITE 8 AC6 30 ARG B 469 CL B1570
CRYST1 59.983 83.307 108.801 90.00 102.22 90.00 P 1 21 1 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 0.016671 0.000000 0.003612 0.00000
SCALE2 0.000000 0.012004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
