HEADER ELECTRON TRANSPORT 12-NOV-14 4RSZ
TITLE THE X-RAY STRUCTURE OF THE PRIMARY ADDUCT FORMED IN THE REACTION
TITLE 2 BETWEEN CISPLATIN AND CYTOCHROME C
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
KEYWDS ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MERLINO
REVDAT 2 25-FEB-15 4RSZ 1 JRNL
REVDAT 1 14-JAN-15 4RSZ 0
JRNL AUTH G.FERRARO,L.MESSORI,A.MERLINO
JRNL TITL THE X-RAY STRUCTURE OF THE PRIMARY ADDUCTS FORMED IN THE
JRNL TITL 2 REACTION BETWEEN CISPLATIN AND CYTOCHROME C.
JRNL REF CHEM.COMMUN.(CAMB.) V. 51 2559 2015
JRNL REFN ISSN 1359-7345
JRNL PMID 25567806
JRNL DOI 10.1039/C4CC09056J
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 104.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 28987
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1544
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2124
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3300
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 : 347
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 2.59000
REMARK 3 B12 (A**2) : -0.40000
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): 0.446
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.272
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.245
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.786
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5450 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5241 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7317 ; 1.845 ; 2.054
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12126 ; 1.431 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 622 ; 5.865 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;34.760 ;25.340
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1029 ;17.446 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;28.912 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 718 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6050 ; 0.017 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1189 ; 0.024 ; 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): 2500 ; 1.629 ; 1.947
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2499 ; 1.629 ; 1.948
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3118 ; 2.688 ; 2.911
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3119 ; 2.687 ; 2.910
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2950 ; 2.276 ; 2.106
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2903 ; 2.227 ; 2.085
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4152 ; 3.102 ; 2.985
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6874 ; 5.884 ;15.505
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6848 ; 5.848 ;15.448
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 : 15
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 104 B 1 104 6285 0.11 0.05
REMARK 3 2 A 1 104 C 1 104 6325 0.11 0.05
REMARK 3 3 A 1 104 D 1 104 6209 0.11 0.05
REMARK 3 4 A 1 104 E 1 104 6222 0.10 0.05
REMARK 3 5 A 1 104 F 1 104 6294 0.11 0.05
REMARK 3 6 B 1 104 C 1 104 6268 0.10 0.05
REMARK 3 7 B 1 104 D 1 104 6243 0.09 0.05
REMARK 3 8 B 1 104 E 1 104 6167 0.10 0.05
REMARK 3 9 B 1 104 F 1 104 6281 0.09 0.05
REMARK 3 10 C 1 104 D 1 104 6260 0.10 0.05
REMARK 3 11 C 1 104 E 1 104 6234 0.09 0.05
REMARK 3 12 C 1 104 F 1 104 6331 0.10 0.05
REMARK 3 13 D 1 104 E 1 104 6242 0.10 0.05
REMARK 3 14 D 1 104 F 1 104 6343 0.08 0.05
REMARK 3 15 E 1 104 F 1 104 6248 0.09 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 201
REMARK 3 ORIGIN FOR THE GROUP (A): -90.9794 -0.3117 18.3381
REMARK 3 T TENSOR
REMARK 3 T11: 0.2665 T22: 0.1786
REMARK 3 T33: 0.2037 T12: 0.0338
REMARK 3 T13: -0.0527 T23: -0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 1.7688 L22: 1.4210
REMARK 3 L33: 0.3832 L12: 0.0159
REMARK 3 L13: 0.0191 L23: 0.6297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0585 S12: -0.0358 S13: -0.2311
REMARK 3 S21: -0.1775 S22: -0.0949 S23: 0.1336
REMARK 3 S31: -0.2033 S32: -0.0296 S33: 0.1534
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 1 B 201
REMARK 3 ORIGIN FOR THE GROUP (A): -73.1461 18.1040 20.0515
REMARK 3 T TENSOR
REMARK 3 T11: 0.4296 T22: 0.1043
REMARK 3 T33: 0.2751 T12: -0.0454
REMARK 3 T13: 0.0293 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 3.6454 L22: 1.5331
REMARK 3 L33: 0.3965 L12: 0.9320
REMARK 3 L13: 1.0414 L23: 0.4425
REMARK 3 S TENSOR
REMARK 3 S11: -0.4309 S12: -0.2249 S13: 0.2145
REMARK 3 S21: -0.6802 S22: 0.2465 S23: -0.1584
REMARK 3 S31: -0.2353 S32: -0.0114 S33: 0.1844
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 201
REMARK 3 ORIGIN FOR THE GROUP (A): -66.0765 -6.3671 15.9623
REMARK 3 T TENSOR
REMARK 3 T11: 0.2787 T22: 0.1683
REMARK 3 T33: 0.4756 T12: -0.0147
REMARK 3 T13: 0.2814 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 0.6244 L22: 1.7783
REMARK 3 L33: 0.4601 L12: 0.0397
REMARK 3 L13: -0.4866 L23: 0.2049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0345 S12: -0.0498 S13: -0.2128
REMARK 3 S21: -0.5747 S22: 0.0442 S23: -0.7270
REMARK 3 S31: -0.1030 S32: -0.0334 S33: -0.0097
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 201
REMARK 3 ORIGIN FOR THE GROUP (A):-104.6333 -16.3125 34.8594
REMARK 3 T TENSOR
REMARK 3 T11: 0.1308 T22: 0.3379
REMARK 3 T33: 0.1908 T12: -0.1286
REMARK 3 T13: 0.0595 T23: -0.1635
REMARK 3 L TENSOR
REMARK 3 L11: 3.0940 L22: 2.2049
REMARK 3 L33: 0.2286 L12: 0.5242
REMARK 3 L13: 0.6655 L23: 0.4337
REMARK 3 S TENSOR
REMARK 3 S11: 0.3172 S12: -0.4243 S13: 0.3914
REMARK 3 S21: 0.1662 S22: -0.4033 S23: 0.1807
REMARK 3 S31: 0.1383 S32: -0.1470 S33: 0.0861
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 201
REMARK 3 ORIGIN FOR THE GROUP (A): -90.2994 31.4375 35.6297
REMARK 3 T TENSOR
REMARK 3 T11: 0.3034 T22: 0.6550
REMARK 3 T33: 0.2698 T12: 0.1639
REMARK 3 T13: -0.1803 T23: -0.3436
REMARK 3 L TENSOR
REMARK 3 L11: 6.4221 L22: 1.6841
REMARK 3 L33: 0.2523 L12: -3.2503
REMARK 3 L13: -1.2684 L23: 0.6343
REMARK 3 S TENSOR
REMARK 3 S11: -0.7533 S12: -1.6493 S13: 0.9217
REMARK 3 S21: 0.3260 S22: 0.9238 S23: -0.4829
REMARK 3 S31: 0.1664 S32: 0.3131 S33: -0.1705
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 201
REMARK 3 ORIGIN FOR THE GROUP (A): -84.8421 -32.0314 31.2018
REMARK 3 T TENSOR
REMARK 3 T11: 0.2912 T22: 0.2131
REMARK 3 T33: 0.5851 T12: 0.0112
REMARK 3 T13: 0.0725 T23: 0.2808
REMARK 3 L TENSOR
REMARK 3 L11: 4.0217 L22: 0.7142
REMARK 3 L33: 1.4049 L12: 0.7520
REMARK 3 L13: 0.3244 L23: -0.6546
REMARK 3 S TENSOR
REMARK 3 S11: 0.3096 S12: -0.6375 S13: -0.8887
REMARK 3 S21: -0.0021 S22: -0.1852 S23: -0.3824
REMARK 3 S31: -0.2096 S32: -0.1561 S33: -0.1244
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
REMARK 4
REMARK 4 4RSZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-14.
REMARK 100 THE RCSB ID CODE IS RCSB087757.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR571
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30538
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 104.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.400
REMARK 200 R MERGE (I) : 0.10900
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHASER
REMARK 200 STARTING MODEL: PDB CODE 1HRC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: A NEW CRYSTAL FORM OF HORSE HEART
REMARK 280 CYTOCHROME C THAT CO-CRYSTALLIZED WITH NITRATE AND SULPHATE IONS
REMARK 280 HAS BEEN OBTAINED. CRYSTALLIZATION WAS PREPARED BY USING THE
REMARK 280 HANGING-DROP VAPOUR DIFFUSION METHOD IN LINBRO PLATES AND A
REMARK 280 RESERVOIR CONTAINED 3.5 M AMMONIUM SULPHATE, 0.6 M SODIUM
REMARK 280 NITRATE. THE DROPLETS CONSISTED OF 1 MICROLITER PROTEIN (30 MG/ML
REMARK 280 IN WATER) AND 1 MICROLITER OF RESERVOIR. THEY WERE EQUILIBRATED
REMARK 280 AGAINST A 500 MICROLITERS RESERVOIR SOLUTION AT 20 C. THESE
REMARK 280 CONDITIONS PRODUCED WELL SHAPED RED CRYSTALS AFTER 1 MONTH. THESE
REMARK 280 CRYSTALS HAVE BEEN SOAKED FOR 24 H IN A SOLUTION CONSISTING OF
REMARK 280 0.005 M CISPLATIN IN 2.0 M AMMONIUM SULPHATE AND 0.4 M SODIUM
REMARK 280 NITRATE. TO PREPARE THIS SOLUTION, CISPLATIN WAS FIRST DISSOLVED
REMARK 280 IN 5 MM SODIUM ACETATE BUFFER AT PH 5.0. , VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -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 0.00000
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -232.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 -0.500000 0.866025 0.000000 -180.51600
REMARK 350 BIOMT2 1 -0.866025 -0.500000 0.000000 -104.22096
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -36.67300
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -36.67300
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 E 14 CBB HEM E 201 1.92
REMARK 500 OE1 GLU B 61 N1 CPT B 203 2.13
REMARK 500 OG1 THR F 40 O HOH F 310 2.14
REMARK 500 OE1 GLU A 104 O HOH A 302 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 GLU E 92 CG GLU E 92 CD 0.175
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 GLU E 92 OE1 - CD - OE2 ANGL. DEV. = -9.6 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 LYS A 27 -142.95 -105.27
REMARK 500 ASN A 70 84.66 -166.03
REMARK 500 LYS B 27 -141.75 -105.90
REMARK 500 ASN B 70 82.46 -164.95
REMARK 500 LYS C 27 -143.67 -103.74
REMARK 500 ASN C 70 83.52 -165.70
REMARK 500 LYS D 27 -158.30 -123.48
REMARK 500 ASN D 70 83.82 -165.35
REMARK 500 LYS E 27 -144.34 -104.13
REMARK 500 ASN E 70 83.04 -165.86
REMARK 500 LYS F 22 25.51 -63.27
REMARK 500 LYS F 27 -151.71 -112.24
REMARK 500 ASN F 70 83.81 -166.29
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 CPT F 203 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 61 OE2
REMARK 620 2 CPT F 203 N1 175.7
REMARK 620 3 CPT F 203 CL1 89.1 89.2
REMARK 620 4 MET F 65 SD 117.9 63.3 152.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CPT A 202 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 61 OE2
REMARK 620 2 CPT A 202 N1 158.0
REMARK 620 3 CPT A 202 N2 92.2 95.9
REMARK 620 4 MET A 65 SD 98.9 67.2 157.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 18 NE2
REMARK 620 2 HEM F 201 NA 90.3
REMARK 620 3 HEM F 201 NB 86.1 90.9
REMARK 620 4 HEM F 201 NC 89.2 179.5 88.8
REMARK 620 5 HEM F 201 ND 93.5 90.1 178.9 90.2
REMARK 620 6 MET F 80 SD 177.2 87.8 96.0 92.6 84.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEM B 201 NA 90.7
REMARK 620 3 HEM B 201 NB 88.1 92.0
REMARK 620 4 HEM B 201 NC 88.3 178.5 86.8
REMARK 620 5 HEM B 201 ND 91.4 89.0 178.9 92.2
REMARK 620 6 MET B 80 SD 171.2 85.0 99.7 96.1 80.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 18 NE2
REMARK 620 2 HEM D 201 NA 87.4
REMARK 620 3 HEM D 201 NB 86.3 89.9
REMARK 620 4 HEM D 201 NC 91.8 178.7 89.1
REMARK 620 5 HEM D 201 ND 93.3 90.9 179.2 90.2
REMARK 620 6 MET D 80 SD 171.5 84.3 95.3 96.5 85.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 18 NE2
REMARK 620 2 HEM C 201 NA 85.3
REMARK 620 3 HEM C 201 NB 88.2 88.9
REMARK 620 4 HEM C 201 NC 94.2 178.7 90.0
REMARK 620 5 HEM C 201 ND 91.3 91.4 179.4 89.7
REMARK 620 6 MET C 80 SD 170.1 86.1 96.5 94.6 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 18 NE2
REMARK 620 2 HEM E 201 NA 89.4
REMARK 620 3 HEM E 201 NB 84.0 91.1
REMARK 620 4 HEM E 201 NC 89.8 179.0 88.2
REMARK 620 5 HEM E 201 ND 95.3 89.5 179.1 91.2
REMARK 620 6 MET E 80 SD 175.5 86.1 95.9 94.6 84.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEM A 201 NA 88.7
REMARK 620 3 HEM A 201 NB 85.9 91.3
REMARK 620 4 HEM A 201 NC 90.0 178.7 88.3
REMARK 620 5 HEM A 201 ND 93.8 89.4 179.3 91.1
REMARK 620 6 MET A 80 SD 174.7 86.7 96.9 94.6 83.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CPT D 202 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET D 65 SD
REMARK 620 2 CPT D 202 N1 177.2
REMARK 620 3 CPT D 202 N2 105.5 77.2
REMARK 620 4 CPT D 202 CL1 73.3 103.9 178.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CPT B 203 PT1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 65 SD
REMARK 620 2 CPT B 203 N1 177.5
REMARK 620 3 CPT B 203 N2 70.0 107.5
REMARK 620 4 CPT B 203 CL1 111.3 71.1 178.6
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 HEM A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPT F 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 205
DBREF 4RSZ A 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 4RSZ B 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 4RSZ C 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 4RSZ D 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 4RSZ E 1 104 UNP P00004 CYC_HORSE 2 105
DBREF 4RSZ 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 HEM A 201 43
HET CPT A 202 3
HET NO3 A 203 4
HET NO3 A 204 4
HET HEM B 201 43
HET SO4 B 202 5
HET CPT B 203 4
HET NO3 B 204 4
HET NO3 B 205 4
HET NO3 B 206 4
HET HEM C 201 43
HET NO3 C 202 4
HET NO3 C 203 4
HET NO3 C 204 4
HET NO3 C 205 4
HET HEM D 201 43
HET CPT D 202 4
HET NO3 D 203 4
HET NO3 D 204 4
HET HEM E 201 43
HET CPT E 202 1
HET NO3 E 203 4
HET NO3 E 204 4
HET NO3 E 205 4
HET HEM F 201 43
HET SO4 F 202 5
HET CPT F 203 3
HET NO3 F 204 4
HET NO3 F 205 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CPT CISPLATIN
HETNAM NO3 NITRATE ION
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
HETSYN CPT DIAMMINE(DICHLORO)PLATINUM
FORMUL 7 HEM 6(C34 H32 FE N4 O4)
FORMUL 8 CPT 5(CL2 H6 N2 PT)
FORMUL 9 NO3 16(N O3 1-)
FORMUL 12 SO4 2(O4 S 2-)
FORMUL 36 HOH *127(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 ASN A 70 1 11
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 LYS C 55 1 7
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 LYS D 55 1 7
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 LYS F 55 1 7
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 OE2 GLU F 61 PT1 CPT F 203 1555 1555 1.83
LINK OE2 GLU A 61 PT1 CPT A 202 1555 1555 1.83
LINK NE2 HIS F 18 FE HEM F 201 1555 1555 1.90
LINK NE2 HIS B 18 FE HEM B 201 1555 1555 1.90
LINK NE2 HIS D 18 FE HEM D 201 1555 1555 1.91
LINK NE2 HIS C 18 FE HEM C 201 1555 1555 1.93
LINK NE2 HIS E 18 FE HEM E 201 1555 1555 1.94
LINK NE2 HIS A 18 FE HEM A 201 1555 1555 1.95
LINK SD MET D 65 PT1 CPT D 202 1555 1555 2.23
LINK SD MET A 65 PT1 CPT A 202 1555 1555 2.26
LINK SD MET E 80 FE HEM E 201 1555 1555 2.28
LINK SD MET A 80 FE HEM A 201 1555 1555 2.28
LINK SD MET F 65 PT1 CPT F 203 1555 1555 2.28
LINK SD MET E 65 PT1 CPT E 202 1555 1555 2.29
LINK SD MET F 80 FE HEM F 201 1555 1555 2.31
LINK SD MET D 80 FE HEM D 201 1555 1555 2.31
LINK SD MET B 80 FE HEM B 201 1555 1555 2.31
LINK SD MET B 65 PT1 CPT B 203 1555 1555 2.33
LINK SD MET C 80 FE HEM C 201 1555 1555 2.35
LINK SG CYS A 14 CAB HEM A 201 1555 1555 1.77
LINK SG CYS B 14 CAB HEM B 201 1555 1555 1.65
LINK SG CYS C 14 CAB HEM C 201 1555 1555 1.73
LINK SG CYS D 14 CAB HEM D 201 1555 1555 1.74
LINK SG CYS E 14 CAB HEM E 201 1555 1555 1.68
LINK SG CYS F 14 CAB HEM F 201 1555 1555 1.76
LINK SG CYS A 17 CAC HEM A 201 1555 1555 1.82
LINK SG CYS B 17 CAC HEM B 201 1555 1555 1.79
LINK SG CYS C 17 CAC HEM C 201 1555 1555 1.83
LINK SG CYS D 17 CAC HEM D 201 1555 1555 1.75
LINK SG CYS E 17 CAC HEM E 201 1555 1555 1.72
LINK SG CYS F 17 CAC HEM F 201 1555 1555 1.81
SITE 1 AC1 22 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 22 THR A 28 PRO A 30 ARG A 38 THR A 40
SITE 3 AC1 22 GLY A 41 TYR A 48 THR A 49 ASN A 52
SITE 4 AC1 22 TRP A 59 TYR A 67 LEU A 68 THR A 78
SITE 5 AC1 22 LYS A 79 MET A 80 ILE A 81 PHE A 82
SITE 6 AC1 22 LEU A 94 HOH A 305
SITE 1 AC2 3 GLU A 61 MET A 65 GLU A 92
SITE 1 AC3 8 PHE A 10 THR A 19 VAL A 20 GLU A 21
SITE 2 AC3 8 HOH A 310 THR C 28 ILE C 81 HOH C 302
SITE 1 AC4 6 PHE A 82 ALA A 83 GLY A 84 LYS B 8
SITE 2 AC4 6 VAL B 11 GLN B 12
SITE 1 AC5 21 LYS B 13 CYS B 14 GLN B 16 CYS B 17
SITE 2 AC5 21 HIS B 18 THR B 28 GLY B 29 PRO B 30
SITE 3 AC5 21 THR B 40 GLY B 41 TYR B 48 THR B 49
SITE 4 AC5 21 ASN B 52 TRP B 59 TYR B 67 LEU B 68
SITE 5 AC5 21 THR B 78 LYS B 79 MET B 80 LEU B 94
SITE 6 AC5 21 HOH B 307
SITE 1 AC6 4 LYS A 72 LYS B 100 GLU B 104 GLY E 23
SITE 1 AC7 5 GLU B 61 GLU B 62 MET B 65 GLU B 92
SITE 2 AC7 5 GLU E 62
SITE 1 AC8 8 THR A 28 ILE A 81 PHE B 10 THR B 19
SITE 2 AC8 8 VAL B 20 GLU B 21 HOH B 306 HOH B 318
SITE 1 AC9 6 PHE B 82 ALA B 83 GLY B 84 LYS C 8
SITE 2 AC9 6 VAL C 11 GLN C 12
SITE 1 BC1 4 GLY B 41 PHE B 46 THR B 47 TYR B 48
SITE 1 BC2 22 LYS C 13 CYS C 14 GLN C 16 CYS C 17
SITE 2 BC2 22 HIS C 18 THR C 28 PRO C 30 ARG C 38
SITE 3 BC2 22 THR C 40 GLY C 41 TYR C 48 THR C 49
SITE 4 BC2 22 ASN C 52 TRP C 59 TYR C 67 LEU C 68
SITE 5 BC2 22 THR C 78 LYS C 79 MET C 80 ILE C 81
SITE 6 BC2 22 LEU C 94 HOH C 308
SITE 1 BC3 8 THR B 28 ILE B 81 PHE C 10 THR C 19
SITE 2 BC3 8 VAL C 20 GLU C 21 HOH C 304 HOH C 305
SITE 1 BC4 6 LYS A 8 VAL A 11 GLN A 12 PHE C 82
SITE 2 BC4 6 ALA C 83 GLY C 84
SITE 1 BC5 3 ALA B 83 GLU C 4 LYS C 7
SITE 1 BC6 3 PHE C 36 LYS C 99 LYS F 22
SITE 1 BC7 21 LYS D 13 CYS D 14 GLN D 16 CYS D 17
SITE 2 BC7 21 HIS D 18 THR D 28 GLY D 29 PRO D 30
SITE 3 BC7 21 ARG D 38 GLY D 41 TYR D 48 THR D 49
SITE 4 BC7 21 ASN D 52 TRP D 59 TYR D 67 LEU D 68
SITE 5 BC7 21 THR D 78 LYS D 79 MET D 80 LEU D 94
SITE 6 BC7 21 HOH D 301
SITE 1 BC8 5 GLU A 61 GLU D 61 GLU D 62 MET D 65
SITE 2 BC8 5 GLU D 92
SITE 1 BC9 8 PHE D 10 THR D 19 VAL D 20 GLU D 21
SITE 2 BC9 8 HOH D 310 HOH D 318 THR F 28 ILE F 81
SITE 1 CC1 6 PHE D 82 ALA D 83 GLY D 84 LYS E 8
SITE 2 CC1 6 VAL E 11 GLN E 12
SITE 1 CC2 20 LYS E 13 CYS E 14 CYS E 17 HIS E 18
SITE 2 CC2 20 THR E 28 GLY E 29 ARG E 38 THR E 40
SITE 3 CC2 20 GLY E 41 TYR E 48 THR E 49 ASN E 52
SITE 4 CC2 20 TRP E 59 TYR E 67 LEU E 68 THR E 78
SITE 5 CC2 20 LYS E 79 MET E 80 LEU E 94 HOH E 301
SITE 1 CC3 1 MET E 65
SITE 1 CC4 7 HIS E 26 PRO E 30 ASN E 31 ALA E 43
SITE 2 CC4 7 PRO E 44 GLY E 45 PHE E 46
SITE 1 CC5 6 PHE E 82 ALA E 83 GLY E 84 LYS F 8
SITE 2 CC5 6 VAL F 11 GLN F 12
SITE 1 CC6 7 THR D 28 ILE D 81 PHE E 10 THR E 19
SITE 2 CC6 7 VAL E 20 GLU E 21 HOH E 309
SITE 1 CC7 22 LYS F 13 CYS F 14 GLN F 16 CYS F 17
SITE 2 CC7 22 HIS F 18 THR F 28 GLY F 29 PRO F 30
SITE 3 CC7 22 ARG F 38 THR F 40 GLY F 41 TYR F 48
SITE 4 CC7 22 THR F 49 ASN F 52 TRP F 59 TYR F 67
SITE 5 CC7 22 THR F 78 LYS F 79 MET F 80 ILE F 81
SITE 6 CC7 22 LEU F 94 HOH F 311
SITE 1 CC8 10 LYS D 25 LYS D 27 LYS E 25 LYS E 27
SITE 2 CC8 10 GLN F 16 LYS F 25 LYS F 27 HOH F 303
SITE 3 CC8 10 HOH F 304 HOH F 308
SITE 1 CC9 3 GLU F 61 MET F 65 GLU F 92
SITE 1 DC1 7 THR E 28 ILE E 81 HOH E 312 THR F 19
SITE 2 DC1 7 VAL F 20 GLU F 21 HOH F 313
SITE 1 DC2 6 LYS D 8 VAL D 11 GLN D 12 PHE F 82
SITE 2 DC2 6 ALA F 83 GLY F 84
CRYST1 120.344 120.344 36.673 90.00 90.00 120.00 P 3 18
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 0.008310 0.004797 0.000000 0.00000
SCALE2 0.000000 0.009595 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027268 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
