HEADER ELECTRON TRANSPORT 04-JUN-10 3NBT
TITLE CRYSTAL STRUCTURE OF TRIMERIC CYTOCHROME C FROM HORSE HEART
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A, B, C, D, E, F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: DOMESTIC HORSE,EQUINE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 ORGAN: HEART
KEYWDS CYTOCHROME C, POLYMERIZATION, DOMAIN SWAPPING, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TAKETA,H.KOMORI,S.HIROTA,Y.HIGUCHI
REVDAT 5 02-OCT-19 3NBT 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 HETSYN FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 08-NOV-17 3NBT 1 REMARK
REVDAT 3 28-JUL-10 3NBT 1 JRNL
REVDAT 2 21-JUL-10 3NBT 1 JRNL
REVDAT 1 14-JUL-10 3NBT 0
JRNL AUTH S.HIROTA,Y.HATTORI,S.NAGAO,M.TAKETA,H.KOMORI,H.KAMIKUBO,
JRNL AUTH 2 Z.WANG,I.TAKAHASHI,S.NEGI,Y.SUGIURA,M.KATAOKA,Y.HIGUCHI
JRNL TITL CYTOCHROME C POLYMERIZATION BY SUCCESSIVE DOMAIN SWAPPING AT
JRNL TITL 2 THE C-TERMINAL HELIX
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 12854 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20615990
JRNL DOI 10.1073/PNAS.1001839107
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 77168.570
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 40288
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 SET) : 0.211
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4052
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5766
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 646
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 384
REMARK 3 SOLVENT ATOMS : 345
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.98000
REMARK 3 B22 (A**2) : -4.59000
REMARK 3 B33 (A**2) : 6.57000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 2.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 48.75
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PARAM19X_MOD.H
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : PEG.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TOPH19.HEM
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : PEG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3NBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059632.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-09
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 : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : SI DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43002
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.590
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: PDB ENTRY 1CRC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 200, 0.1M TRIS-HCL, 0.2M
REMARK 280 AMMONIUM PHOSPHATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 28.60200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.46750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.83050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.46750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.60200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.83050
REMARK 290 SMTRY3 4 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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D
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 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 SG CYS F 17 CBC HEC F 105 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 27 -134.88 -130.91
REMARK 500 ASN A 70 89.78 -162.46
REMARK 500 PHE A 82 125.55 -36.24
REMARK 500 LYS B 27 -138.00 -131.96
REMARK 500 ASN B 70 87.80 -161.33
REMARK 500 LYS C 27 -139.29 -129.23
REMARK 500 ASN C 70 88.11 -160.00
REMARK 500 LYS D 27 -129.83 -127.83
REMARK 500 ASN D 70 88.25 -166.84
REMARK 500 LYS E 27 -132.12 -124.38
REMARK 500 ASN E 70 87.67 -163.05
REMARK 500 PHE E 82 123.12 -36.72
REMARK 500 LYS F 27 -134.97 -131.82
REMARK 500 ASN F 70 92.01 -164.43
REMARK 500 PHE F 82 119.66 -38.65
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 E 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 18 NE2
REMARK 620 2 HEC E 105 NA 95.2
REMARK 620 3 HEC E 105 NB 94.5 91.8
REMARK 620 4 HEC E 105 NC 87.4 177.1 89.4
REMARK 620 5 HEC E 105 ND 85.1 89.4 178.8 89.5
REMARK 620 6 HOH E 205 O 175.1 88.3 88.8 89.0 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 105 NA 89.9
REMARK 620 3 HEC A 105 NB 95.7 91.7
REMARK 620 4 HEC A 105 NC 93.0 175.5 91.3
REMARK 620 5 HEC A 105 ND 84.7 87.8 179.4 89.1
REMARK 620 6 HOH A 201 O 171.2 87.6 92.8 89.0 86.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC F 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 18 NE2
REMARK 620 2 HEC F 105 NA 93.7
REMARK 620 3 HEC F 105 NB 88.8 90.1
REMARK 620 4 HEC F 105 NC 88.4 177.9 89.7
REMARK 620 5 HEC F 105 ND 86.9 88.2 175.2 92.2
REMARK 620 6 HOH F 206 O 169.1 95.8 96.5 82.1 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC C 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 18 NE2
REMARK 620 2 HEC C 105 NA 95.0
REMARK 620 3 HEC C 105 NB 89.1 91.4
REMARK 620 4 HEC C 105 NC 87.3 177.7 88.3
REMARK 620 5 HEC C 105 ND 87.8 89.2 176.9 91.2
REMARK 620 6 HOH C 203 O 176.0 88.8 89.7 88.9 93.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 18 NE2
REMARK 620 2 HEC D 105 NA 89.9
REMARK 620 3 HEC D 105 NB 89.0 90.9
REMARK 620 4 HEC D 105 NC 90.4 179.7 89.2
REMARK 620 5 HEC D 105 ND 91.2 88.3 179.2 91.6
REMARK 620 6 HOH D 204 O 176.5 90.6 94.5 89.1 85.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEC B 105 NA 95.8
REMARK 620 3 HEC B 105 NB 91.2 91.4
REMARK 620 4 HEC B 105 NC 87.7 176.1 90.1
REMARK 620 5 HEC B 105 ND 87.1 90.1 177.9 88.5
REMARK 620 6 HOH B 202 O 176.7 87.3 87.6 89.3 94.1
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 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE D 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 E 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 F 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE F 1012
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NBS RELATED DB: PDB
REMARK 900 DIMERIC STRUCTURE
DBREF 3NBT A 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3NBT B 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3NBT C 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3NBT D 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3NBT E 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 3NBT F 1 104 UNP P00004 CYC_HORSE 2 105
SEQRES 1 A 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 A 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 A 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 A 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 A 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 A 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 A 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 A 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
SEQRES 1 B 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 B 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 B 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 B 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 B 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 B 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 B 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 B 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
SEQRES 1 C 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 C 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 C 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 C 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 C 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 C 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 C 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 C 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
SEQRES 1 D 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 D 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 D 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 D 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 D 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 D 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 D 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 D 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
SEQRES 1 E 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 E 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 E 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 E 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 E 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 E 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 E 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 E 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
SEQRES 1 F 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 F 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 F 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 F 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 F 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 F 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 F 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 F 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
HET HEC A 105 43
HET PG4 A1001 13
HET PEG A1007 7
HET HEC B 105 43
HET PG4 B1004 13
HET PEG B1008 7
HET HEC C 105 43
HET PG4 C1005 13
HET PEG C1009 7
HET HEC D 105 43
HET PG4 D1006 13
HET PGE D1010 10
HET HEC E 105 43
HET PG4 E1002 13
HET PEG E1011 7
HET HEC F 105 43
HET PG4 F1003 13
HET PGE F1012 10
HETNAM HEC HEME C
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 7 HEC 6(C34 H34 FE N4 O4)
FORMUL 8 PG4 6(C8 H18 O5)
FORMUL 9 PEG 4(C4 H10 O3)
FORMUL 18 PGE 2(C6 H14 O4)
FORMUL 25 HOH *345(H2 O)
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 THR A 49 LYS A 55 1 7
HELIX 3 3 LYS A 60 LEU A 68 1 9
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 THR A 102 1 16
HELIX 6 6 ASP B 2 CYS B 14 1 13
HELIX 7 7 THR B 49 LYS B 55 1 7
HELIX 8 8 LYS B 60 ASN B 70 1 11
HELIX 9 9 ASN B 70 ILE B 75 1 6
HELIX 10 10 LYS B 87 THR B 102 1 16
HELIX 11 11 ASP C 2 CYS C 14 1 13
HELIX 12 12 THR C 49 ASN C 54 1 6
HELIX 13 13 LYS C 60 ASN C 70 1 11
HELIX 14 14 ASN C 70 ILE C 75 1 6
HELIX 15 15 LYS C 87 THR C 102 1 16
HELIX 16 16 ASP D 2 CYS D 14 1 13
HELIX 17 17 THR D 49 ASN D 54 1 6
HELIX 18 18 LYS D 60 ASN D 70 1 11
HELIX 19 19 ASN D 70 ILE D 75 1 6
HELIX 20 20 LYS D 87 THR D 102 1 16
HELIX 21 21 ASP E 2 CYS E 14 1 13
HELIX 22 22 THR E 49 LYS E 55 1 7
HELIX 23 23 LYS E 60 ASN E 70 1 11
HELIX 24 24 ASN E 70 ILE E 75 1 6
HELIX 25 25 LYS E 87 THR E 102 1 16
HELIX 26 26 ASP F 2 CYS F 14 1 13
HELIX 27 27 THR F 49 ASN F 54 1 6
HELIX 28 28 LYS F 60 ASN F 70 1 11
HELIX 29 29 ASN F 70 ILE F 75 1 6
HELIX 30 30 LYS F 87 THR F 102 1 16
LINK NE2 HIS E 18 FE HEC E 105 1555 1555 1.96
LINK NE2 HIS A 18 FE HEC A 105 1555 1555 1.96
LINK NE2 HIS F 18 FE HEC F 105 1555 1555 1.98
LINK NE2 HIS C 18 FE HEC C 105 1555 1555 1.99
LINK NE2 HIS D 18 FE HEC D 105 1555 1555 1.99
LINK NE2 HIS B 18 FE HEC B 105 1555 1555 2.00
LINK SG CYS A 14 CAB HEC A 105 1555 1555 1.85
LINK SG CYS A 17 CAC HEC A 105 1555 1555 1.85
LINK SG CYS B 14 CAB HEC B 105 1555 1555 1.85
LINK SG CYS B 17 CAC HEC B 105 1555 1555 1.84
LINK SG CYS C 14 CAB HEC C 105 1555 1555 1.85
LINK SG CYS C 17 CAC HEC C 105 1555 1555 1.86
LINK SG CYS D 14 CAB HEC D 105 1555 1555 1.85
LINK SG CYS D 17 CAC HEC D 105 1555 1555 1.84
LINK SG CYS E 14 CAB HEC E 105 1555 1555 1.85
LINK SG CYS E 17 CAC HEC E 105 1555 1555 1.86
LINK SG CYS F 14 CAB HEC F 105 1555 1555 1.84
LINK SG CYS F 17 CAC HEC F 105 1555 1555 1.83
LINK FE HEC C 105 O HOH C 203 1555 1555 2.09
LINK FE HEC D 105 O HOH D 204 1555 1555 2.11
LINK FE HEC F 105 O HOH F 206 1555 1555 2.11
LINK FE HEC A 105 O HOH A 201 1555 1555 2.11
LINK FE HEC E 105 O HOH E 205 1555 1555 2.11
LINK FE HEC B 105 O HOH B 202 1555 1555 2.12
SITE 1 AC1 24 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 24 THR A 28 GLY A 29 PRO A 30 THR A 40
SITE 3 AC1 24 GLY A 41 TYR A 48 THR A 49 ASN A 52
SITE 4 AC1 24 TRP A 59 TYR A 67 LEU A 68 THR A 78
SITE 5 AC1 24 LYS A 79 MET A 80 HOH A 201 HOH A 243
SITE 6 AC1 24 HOH A 437 PEG A1007 PHE E 82 LEU E 94
SITE 1 AC2 7 LYS A 55 ILE A 57 GLU A 66 LYS A 73
SITE 2 AC2 7 TYR A 74 PRO A 76 HOH A 305
SITE 1 AC3 7 THR A 28 THR A 47 LYS A 79 GLY A 84
SITE 2 AC3 7 HEC A 105 HOH A 238 HOH A 496
SITE 1 AC4 21 LYS B 13 CYS B 14 CYS B 17 HIS B 18
SITE 2 AC4 21 THR B 28 GLY B 29 ARG B 38 THR B 40
SITE 3 AC4 21 GLY B 41 TYR B 48 THR B 49 ASN B 52
SITE 4 AC4 21 TRP B 59 TYR B 67 THR B 78 LYS B 79
SITE 5 AC4 21 MET B 80 HOH B 202 HOH B 495 PEG B1008
SITE 6 AC4 21 PHE C 82
SITE 1 AC5 6 LYS B 55 ILE B 57 GLU B 66 LYS B 73
SITE 2 AC5 6 TYR B 74 ASP E 50
SITE 1 AC6 8 THR B 47 TYR B 48 THR B 49 LYS B 79
SITE 2 AC6 8 ILE B 81 GLY B 84 HEC B 105 HOH B 407
SITE 1 AC7 23 LYS C 13 CYS C 14 CYS C 17 HIS C 18
SITE 2 AC7 23 THR C 28 GLY C 29 PRO C 30 THR C 40
SITE 3 AC7 23 GLY C 41 TYR C 48 THR C 49 ASN C 52
SITE 4 AC7 23 TRP C 59 TYR C 67 LEU C 68 THR C 78
SITE 5 AC7 23 LYS C 79 MET C 80 HOH C 203 HOH C 227
SITE 6 AC7 23 HOH C 265 PHE D 82 LEU D 94
SITE 1 AC8 7 ASP A 50 LYS C 55 ILE C 57 LYS C 73
SITE 2 AC8 7 TYR C 74 PRO C 76 HOH C 545
SITE 1 AC9 7 THR C 28 THR C 47 THR C 49 ILE C 81
SITE 2 AC9 7 GLY C 84 HOH C 419 HOH C 433
SITE 1 BC1 21 PHE B 82 LEU B 94 LYS D 13 CYS D 14
SITE 2 BC1 21 CYS D 17 HIS D 18 THR D 28 GLY D 29
SITE 3 BC1 21 THR D 40 GLY D 41 TYR D 48 THR D 49
SITE 4 BC1 21 ASN D 52 TRP D 59 TYR D 67 THR D 78
SITE 5 BC1 21 LYS D 79 MET D 80 HOH D 204 HOH D 247
SITE 6 BC1 21 PGE D1010
SITE 1 BC2 6 LYS D 55 GLU D 66 LYS D 73 TYR D 74
SITE 2 BC2 6 PRO D 76 HOH F 411
SITE 1 BC3 11 THR D 28 THR D 47 TYR D 48 THR D 49
SITE 2 BC3 11 LYS D 79 ILE D 81 PHE D 82 GLY D 84
SITE 3 BC3 11 HEC D 105 HOH D 234 HOH D 516
SITE 1 BC4 21 LYS E 13 CYS E 14 CYS E 17 HIS E 18
SITE 2 BC4 21 THR E 28 GLY E 29 THR E 40 GLY E 41
SITE 3 BC4 21 TYR E 48 THR E 49 ASN E 52 TRP E 59
SITE 4 BC4 21 LEU E 64 TYR E 67 THR E 78 LYS E 79
SITE 5 BC4 21 MET E 80 HOH E 205 PEG E1011 PHE F 82
SITE 6 BC4 21 LEU F 94
SITE 1 BC5 7 ASP B 50 LYS E 55 GLU E 66 LYS E 73
SITE 2 BC5 7 TYR E 74 PRO E 76 HOH E 279
SITE 1 BC6 7 THR E 28 THR E 47 THR E 49 LYS E 79
SITE 2 BC6 7 ILE E 81 HEC E 105 HOH E 288
SITE 1 BC7 21 PHE A 82 LEU A 94 LYS F 13 CYS F 14
SITE 2 BC7 21 CYS F 17 HIS F 18 THR F 28 GLY F 29
SITE 3 BC7 21 THR F 40 GLY F 41 TYR F 48 THR F 49
SITE 4 BC7 21 ASN F 52 TRP F 59 TYR F 67 THR F 78
SITE 5 BC7 21 LYS F 79 MET F 80 HOH F 206 HOH F 289
SITE 6 BC7 21 PGE F1012
SITE 1 BC8 5 HOH D 325 LYS F 55 LYS F 73 TYR F 74
SITE 2 BC8 5 PRO F 76
SITE 1 BC9 9 THR F 47 THR F 49 ILE F 81 PHE F 82
SITE 2 BC9 9 GLY F 84 HEC F 105 HOH F 253 HOH F 374
SITE 3 BC9 9 HOH F 392
CRYST1 57.204 95.661 130.935 90.00 90.00 90.00 P 21 21 21 24
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 0.017481 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010454 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007637 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
