HEADER ELECTRON TRANSPORT 08-SEP-12 4H0K
TITLE MUTANT M58H OF NOSTOC SP CYTOCHROME C6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOCHROME C-553, CYTOCHROME C553, SOLUBLE CYTOCHROME F;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120;
SOURCE 5 GENE: PETJ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ELECTRON TRANSPORT, HEME BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR N.S.PANNU,P.SKUBAK,D.CAVAZZINI,G.L.ROSSI,M.UBBINK
REVDAT 4 08-NOV-23 4H0K 1 SEQADV LINK
REVDAT 3 02-OCT-19 4H0K 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL LINK ATOM
REVDAT 2 25-JAN-17 4H0K 1 JRNL
REVDAT 1 11-SEP-13 4H0K 0
JRNL AUTH I.DIAZ-MORENO,R.HULSKER,P.SKUBAK,J.M.FOERSTER,D.CAVAZZINI,
JRNL AUTH 2 M.G.FINIGUERRA,A.DIAZ-QUINTANA,B.MORENO-BELTRAN,G.L.ROSSI,
JRNL AUTH 3 G.M.ULLMANN,N.S.PANNU,M.A.DE LA ROSA,M.UBBINK
JRNL TITL THE DYNAMIC COMPLEX OF CYTOCHROME C6 AND CYTOCHROME F
JRNL TITL 2 STUDIED WITH PARAMAGNETIC NMR SPECTROSCOPY
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1837 1305 2014
JRNL REFN ISSN 0006-3002
JRNL PMID 24685428
JRNL DOI 10.1016/J.BBABIO.2014.03.009
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0027
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 14317
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 767
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1277
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 65
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -0.65000
REMARK 3 B12 (A**2) : 0.22000
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): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.915
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1397 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1327 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1907 ; 1.964 ; 2.035
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3047 ; 1.318 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 169 ; 6.759 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 54 ;38.987 ;26.296
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 230 ;18.290 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;23.234 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 193 ; 0.131 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1625 ; 0.015 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 321 ; 0.014 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 85 B 2 85 4143 0.18 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5670 -25.5980 -10.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1890 T22: 0.2258
REMARK 3 T33: 0.1215 T12: 0.0410
REMARK 3 T13: 0.0498 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 3.2371 L22: 2.9231
REMARK 3 L33: 6.3266 L12: -0.9426
REMARK 3 L13: -2.0152 L23: 1.5094
REMARK 3 S TENSOR
REMARK 3 S11: 0.2558 S12: 0.1143 S13: 0.3370
REMARK 3 S21: -0.2124 S22: 0.0268 S23: -0.4125
REMARK 3 S31: -0.2892 S32: 0.2821 S33: -0.2827
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3410 -45.8170 2.2850
REMARK 3 T TENSOR
REMARK 3 T11: 0.9583 T22: 0.2962
REMARK 3 T33: 0.1269 T12: 0.2206
REMARK 3 T13: 0.2355 T23: 0.0951
REMARK 3 L TENSOR
REMARK 3 L11: 4.8512 L22: 8.0763
REMARK 3 L33: 6.2689 L12: -2.8957
REMARK 3 L13: -2.6061 L23: 1.6483
REMARK 3 S TENSOR
REMARK 3 S11: -0.9772 S12: -0.3931 S13: -0.5192
REMARK 3 S21: 1.7946 S22: 0.1421 S23: 0.2849
REMARK 3 S31: 1.4634 S32: 0.3603 S33: 0.8351
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: RESIDUAL ONLY
REMARK 4
REMARK 4 4H0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95371
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14317
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 35.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4GYD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 2.5M AMMONIUM SULPHATE,
REMARK 280 0.1M LITHIUM SULPHATE, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.58000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.79000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.79000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 63.58000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 ALA B 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 CE1 HIS A 58 FE HEC A 200 2.02
REMARK 500 OE1 GLN B 26 OE1 GLN B 28 2.15
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 SER A 3 -49.63 -26.76
REMARK 500 LYS A 22 -160.80 -100.06
REMARK 500 LYS A 29 71.76 -116.68
REMARK 500 SER B 3 173.01 123.83
REMARK 500 VAL B 4 -47.18 100.73
REMARK 500 ASN B 56 56.47 72.02
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 HEC A 200 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 200 NA 91.6
REMARK 620 3 HEC A 200 NB 89.9 91.6
REMARK 620 4 HEC A 200 NC 87.8 178.9 87.6
REMARK 620 5 HEC A 200 ND 89.5 88.2 179.3 92.7
REMARK 620 6 HIS A 58 NE2 158.7 100.7 72.6 79.7 108.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 200 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEC B 200 NA 89.8
REMARK 620 3 HEC B 200 NB 92.9 91.0
REMARK 620 4 HEC B 200 NC 90.8 179.0 88.2
REMARK 620 5 HEC B 200 ND 87.8 89.5 179.2 91.3
REMARK 620 6 HIS B 58 NE2 179.0 91.2 86.9 88.2 92.5
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 HEM A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GYD RELATED DB: PDB
REMARK 900 RELATED ID: 4H0J RELATED DB: PDB
DBREF 4H0K A 1 86 UNP P0A3X7 CYC6_NOSS1 26 111
DBREF 4H0K B 1 86 UNP P0A3X7 CYC6_NOSS1 26 111
SEQADV 4H0K HIS A 58 UNP P0A3X7 MET 83 ENGINEERED MUTATION
SEQADV 4H0K HIS B 58 UNP P0A3X7 MET 83 ENGINEERED MUTATION
SEQRES 1 A 86 ALA ASP SER VAL ASN GLY ALA LYS ILE PHE SER ALA ASN
SEQRES 2 A 86 CYS ALA SER CYS HIS ALA GLY GLY LYS ASN LEU VAL GLN
SEQRES 3 A 86 ALA GLN LYS THR LEU LYS LYS ALA ASP LEU GLU LYS TYR
SEQRES 4 A 86 GLY MET TYR SER ALA GLU ALA ILE ILE ALA GLN VAL THR
SEQRES 5 A 86 ASN GLY LYS ASN ALA HIS PRO ALA PHE LYS GLY ARG LEU
SEQRES 6 A 86 LYS PRO GLU GLN ILE GLU ASP VAL ALA ALA TYR VAL LEU
SEQRES 7 A 86 GLY LYS ALA ASP ALA ASP TRP LYS
SEQRES 1 B 86 ALA ASP SER VAL ASN GLY ALA LYS ILE PHE SER ALA ASN
SEQRES 2 B 86 CYS ALA SER CYS HIS ALA GLY GLY LYS ASN LEU VAL GLN
SEQRES 3 B 86 ALA GLN LYS THR LEU LYS LYS ALA ASP LEU GLU LYS TYR
SEQRES 4 B 86 GLY MET TYR SER ALA GLU ALA ILE ILE ALA GLN VAL THR
SEQRES 5 B 86 ASN GLY LYS ASN ALA HIS PRO ALA PHE LYS GLY ARG LEU
SEQRES 6 B 86 LYS PRO GLU GLN ILE GLU ASP VAL ALA ALA TYR VAL LEU
SEQRES 7 B 86 GLY LYS ALA ASP ALA ASP TRP LYS
HET HEC A 200 43
HET HEC B 200 43
HETNAM HEC HEME C
FORMUL 3 HEC 2(C34 H34 FE N4 O4)
FORMUL 5 HOH *65(H2 O)
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 CYS A 14 ALA A 19 1 6
HELIX 3 3 GLY A 20 LYS A 22 5 3
HELIX 4 4 LYS A 32 TYR A 39 1 8
HELIX 5 5 SER A 43 GLY A 54 1 12
HELIX 6 6 LYS A 66 ALA A 83 1 18
HELIX 7 7 VAL B 4 CYS B 14 1 11
HELIX 8 8 CYS B 14 ALA B 19 1 6
HELIX 9 9 GLY B 20 LYS B 22 5 3
HELIX 10 10 LYS B 32 TYR B 39 1 8
HELIX 11 11 SER B 43 GLY B 54 1 12
HELIX 12 12 LYS B 66 ALA B 83 1 18
LINK SG CYS A 14 CAB HEC A 200 1555 1555 1.93
LINK SG CYS A 17 CAC HEC A 200 1555 1555 2.28
LINK SG CYS B 14 CAB HEC B 200 1555 1555 2.05
LINK SG CYS B 17 CAC HEC B 200 1555 1555 2.23
LINK NE2 HIS A 18 FE HEC A 200 1555 1555 1.96
LINK NE2 HIS A 58 FE HEC A 200 1555 1555 2.95
LINK NE2 HIS B 18 FE HEC B 200 1555 1555 1.94
LINK NE2 HIS B 58 FE HEC B 200 1555 1555 1.97
SITE 1 AC1 18 ASN A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 18 ASN A 23 GLN A 26 LYS A 29 THR A 30
SITE 3 AC1 18 LEU A 31 ASP A 35 TYR A 39 GLN A 50
SITE 4 AC1 18 VAL A 51 ASN A 56 HIS A 58 PRO A 59
SITE 5 AC1 18 HOH A 336 HOH A 337
SITE 1 AC2 17 ALA A 19 ASN B 13 CYS B 14 CYS B 17
SITE 2 AC2 17 HIS B 18 ASN B 23 VAL B 25 LYS B 29
SITE 3 AC2 17 THR B 30 TYR B 39 MET B 41 GLN B 50
SITE 4 AC2 17 VAL B 51 ASN B 56 HIS B 58 PRO B 59
SITE 5 AC2 17 HOH B 307
CRYST1 60.370 60.370 95.370 90.00 90.00 120.00 P 32 2 1 12
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 0.016565 0.009564 0.000000 0.00000
SCALE2 0.000000 0.019127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010485 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
