HEADER OXIDOREDUCTASE 02-AUG-04 1U75
TITLE ELECTRON TRANSFER COMPLEX BETWEEN HORSE HEART CYTOCHROME C AND ZINC-
TITLE 2 PORPHYRIN SUBSTITUTED CYTOCHROME C PEROXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE;
COMPND 3 CHAIN: A, C;
COMPND 4 EC: 1.11.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CYTOCHROME C;
COMPND 8 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YEAST;
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: PT7CCP;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 13 ORGANISM_COMMON: HORSE;
SOURCE 14 ORGANISM_TAXID: 9796;
SOURCE 15 OTHER_DETAILS: HORSE HEART
KEYWDS PROTEIN-PROTEIN COMPLEX, HEME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.CRANE,S.A.KANG
REVDAT 3 13-JUL-11 1U75 1 VERSN
REVDAT 2 24-FEB-09 1U75 1 VERSN
REVDAT 1 28-SEP-04 1U75 0
JRNL AUTH S.A.KANG,P.J.MARJAVAARA,B.R.CRANE
JRNL TITL ELECTRON TRANSFER BETWEEN CYTOCHROME C AND CYTOCHOME C
JRNL TITL 2 PEROXIDASE IN SINGLE CRYSTALS.
JRNL REF J.AM.CHEM.SOC. V. 126 10836 2004
JRNL REFN ISSN 0002-7863
JRNL PMID 15339156
JRNL DOI 10.1021/JA049230U
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.9999
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 32279
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) : 0.273
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1685
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2305
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3770
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.4340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5573
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 139
REMARK 3 SOLVENT ATOMS : 320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.85000
REMARK 3 B22 (A**2) : -0.85000
REMARK 3 B33 (A**2) : 1.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.605
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.343
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.326
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.815
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.908
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5890 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7996 ; 2.217 ; 2.006
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 689 ; 1.545 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 290 ;43.118 ;24.966
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 971 ;22.602 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;25.815 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 785 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4594 ; 0.018 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2317 ; 0.212 ; 0.200
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): 157 ; 0.184 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.050 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 42 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 1.021 ; 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): 3544 ; 1.586 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5520 ; 2.528 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2775 ; 4.563 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2470 ; 5.905 ; 4.500
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 C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 294 5
REMARK 3 1 C 1 C 294 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 72 ; 1.60 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 60 ; 2.93 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 72 ; 3.20 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 60 ; 4.44 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 104
REMARK 3 RESIDUE RANGE : B 1101 B 1101
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2263 52.5677 59.6992
REMARK 3 T TENSOR
REMARK 3 T11: 0.6466 T22: 0.6340
REMARK 3 T33: 0.9773 T12: 0.0102
REMARK 3 T13: 0.3319 T23: -0.3610
REMARK 3 L TENSOR
REMARK 3 L11: 5.3473 L22: 5.9370
REMARK 3 L33: 11.3178 L12: 0.4514
REMARK 3 L13: -3.8025 L23: 4.1218
REMARK 3 S TENSOR
REMARK 3 S11: 0.5952 S12: -1.2781 S13: 1.4903
REMARK 3 S21: 0.5576 S22: 0.8028 S23: -1.1242
REMARK 3 S31: -1.7368 S32: 1.0713 S33: -1.3980
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 294
REMARK 3 RESIDUE RANGE : A 1001 A 1001
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9207 27.5789 40.3568
REMARK 3 T TENSOR
REMARK 3 T11: -0.1988 T22: -0.1703
REMARK 3 T33: -0.2260 T12: 0.0541
REMARK 3 T13: -0.0029 T23: 0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 2.7245 L22: 2.9650
REMARK 3 L33: 1.9683 L12: 0.0267
REMARK 3 L13: -0.5743 L23: -0.6638
REMARK 3 S TENSOR
REMARK 3 S11: -0.1318 S12: -0.1019 S13: -0.0080
REMARK 3 S21: -0.1421 S22: 0.1907 S23: 0.2260
REMARK 3 S31: 0.1061 S32: 0.0031 S33: -0.0590
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 294
REMARK 3 RESIDUE RANGE : C 1201 C 1201
REMARK 3 ORIGIN FOR THE GROUP (A): 70.1101 1.0437 33.9368
REMARK 3 T TENSOR
REMARK 3 T11: -0.1070 T22: -0.1935
REMARK 3 T33: -0.1417 T12: 0.0215
REMARK 3 T13: 0.1071 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 1.6021 L22: 4.1773
REMARK 3 L33: 2.1900 L12: 0.2908
REMARK 3 L13: -0.4126 L23: -1.3190
REMARK 3 S TENSOR
REMARK 3 S11: -0.1421 S12: -0.0123 S13: -0.1859
REMARK 3 S21: -0.2388 S22: 0.0875 S23: -0.1065
REMARK 3 S31: -0.0778 S32: -0.0491 S33: 0.0546
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB023329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 78
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9363
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34216
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
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 : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2PCB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PH 7.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.44200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.23250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.23250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 140.16300
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.23250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.23250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.72100
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.23250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.23250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 140.16300
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.23250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.23250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.72100
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.44200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER CONTAINING TWO
REMARK 300 MOLECULES OF CYTOCHROME C PEROXIDASE AND ONE MOLECULE OF CYTOCHROME
REMARK 300 C
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 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B1982 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -1
REMARK 465 ILE A 0
REMARK 465 MET C -1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1886 O HOH A 1994 0.25
REMARK 500 O ILE B 85 NH1 ARG B 91 1.51
REMARK 500 O1 PO4 C 2202 NA ZNH C 1201 1.81
REMARK 500 O1 PO4 C 2202 ND ZNH C 1201 1.84
REMARK 500 CD1 TRP A 51 O2 PO4 A 2201 1.92
REMARK 500 N VAL A 7 O HOH A 2002 2.01
REMARK 500 OE1 GLU A 135 O HOH A 2012 2.05
REMARK 500 O3 PO4 C 2202 NA ZNH C 1201 2.10
REMARK 500 SG CYS B 14 CBB HEM B 1101 2.15
REMARK 500 N SER C 66 O HOH C 1998 2.16
REMARK 500 O1 PO4 A 2201 NA ZNH A 1001 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2017 O HOH C 1999 8565 0.59
REMARK 500 O HOH A 2015 O HOH C 1401 8565 0.60
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 THR A 1 C THR A 1 O 0.116
REMARK 500 THR A 2 C PRO A 3 N 0.146
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 PRO A 3 C - N - CA ANGL. DEV. = 31.6 DEGREES
REMARK 500 PRO A 3 C - N - CD ANGL. DEV. = -26.2 DEGREES
REMARK 500 LEU B 64 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 PHE C 77 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 2 -176.58 44.66
REMARK 500 PRO A 3 78.56 -117.80
REMARK 500 GLU A 11 108.79 -54.91
REMARK 500 LYS A 12 108.57 -16.65
REMARK 500 SER A 15 -165.33 -105.86
REMARK 500 ASP A 33 43.83 -90.03
REMARK 500 THR A 70 5.90 -67.23
REMARK 500 GLU A 135 -34.13 -35.12
REMARK 500 ASN A 184 -64.32 -101.94
REMARK 500 ALA A 194 76.88 -102.35
REMARK 500 PRO A 277 -169.97 -69.62
REMARK 500 ASP A 279 48.22 -80.05
REMARK 500 LYS B 27 -122.11 -104.59
REMARK 500 ALA B 43 110.42 -39.22
REMARK 500 ALA B 51 -40.85 175.94
REMARK 500 LEU B 64 0.23 147.06
REMARK 500 LYS B 100 -70.85 -86.45
REMARK 500 ASN B 103 -55.93 -145.47
REMARK 500 THR C 1 122.36 -170.50
REMARK 500 LYS C 12 99.79 -48.40
REMARK 500 ASP C 33 47.54 -94.26
REMARK 500 ASP C 34 0.50 -68.04
REMARK 500 MET C 119 31.52 -92.67
REMARK 500 LYS C 149 -151.99 -108.10
REMARK 500 ASN C 196 20.49 -141.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 67 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR B 63 10.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU A 4 24.9 L L OUTSIDE RANGE
REMARK 500 LYS A 12 23.9 L L OUTSIDE RANGE
REMARK 500 LYS A 74 24.4 L L OUTSIDE RANGE
REMARK 500 ASN A 195 23.9 L L OUTSIDE RANGE
REMARK 500 GLN B 42 24.1 L L OUTSIDE RANGE
REMARK 500 ASN B 52 23.6 L L OUTSIDE RANGE
REMARK 500 GLU B 62 23.7 L L OUTSIDE RANGE
REMARK 500 GLU C 35 24.0 L L OUTSIDE RANGE
REMARK 500 TYR C 39 23.7 L L OUTSIDE RANGE
REMARK 500 ILE C 239 24.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1496 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A1584 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A1596 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A1658 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A1747 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A1808 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH A1831 DISTANCE = 8.20 ANGSTROMS
REMARK 525 HOH A1835 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH A1867 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH A1877 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH A1880 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A1883 DISTANCE = 9.50 ANGSTROMS
REMARK 525 HOH A1884 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH A1892 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH A1893 DISTANCE = 9.50 ANGSTROMS
REMARK 525 HOH A1894 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A1895 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH A1896 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A1898 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1900 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH A1904 DISTANCE = 8.36 ANGSTROMS
REMARK 525 HOH A1907 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A1908 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH A1925 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A1932 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A1981 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH B1667 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH B1670 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH B1683 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH B1748 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH B1849 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B1850 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH B1913 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH B1914 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH B1915 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH B1919 DISTANCE = 9.03 ANGSTROMS
REMARK 525 HOH B1920 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH B1939 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH B1983 DISTANCE = 11.69 ANGSTROMS
REMARK 525 HOH B1984 DISTANCE = 8.84 ANGSTROMS
REMARK 525 HOH C1556 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C1709 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH C1778 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH C1787 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH C1853 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH C1905 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH C1936 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH C1938 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH C1940 DISTANCE = 12.12 ANGSTROMS
REMARK 525 HOH C1941 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH C1946 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH C1947 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH C1948 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH C1951 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C1955 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH C1957 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH C1959 DISTANCE = 8.30 ANGSTROMS
REMARK 525 HOH C1960 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH C1961 DISTANCE = 12.62 ANGSTROMS
REMARK 525 HOH C1964 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH C1968 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH C1969 DISTANCE = 8.61 ANGSTROMS
REMARK 525 HOH C1970 DISTANCE = 10.42 ANGSTROMS
REMARK 525 HOH C1971 DISTANCE = 10.72 ANGSTROMS
REMARK 525 HOH C1972 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH C2001 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH C2019 DISTANCE = 5.50 ANGSTROMS
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 HEM B1101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEM B1101 NA 89.6
REMARK 620 3 HEM B1101 NB 94.3 87.2
REMARK 620 4 HEM B1101 NC 105.1 165.3 92.8
REMARK 620 5 HEM B1101 ND 92.0 90.4 173.2 87.9
REMARK 620 6 MET B 80 SD 161.0 71.4 84.1 93.9 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZNH A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 A2201 O1
REMARK 620 2 ZNH A1001 NA 73.4
REMARK 620 3 ZNH A1001 NB 42.4 88.4
REMARK 620 4 ZNH A1001 NC 82.8 148.4 87.7
REMARK 620 5 ZNH A1001 ND 113.4 87.2 155.4 83.5
REMARK 620 6 HIS A 175 NE2 140.2 110.8 97.8 100.7 106.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZNH C1201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 C2202 O1
REMARK 620 2 ZNH C1201 NA 58.7
REMARK 620 3 ZNH C1201 NB 96.7 85.2
REMARK 620 4 ZNH C1201 NC 98.0 154.6 88.3
REMARK 620 5 ZNH C1201 ND 63.0 86.8 159.3 90.8
REMARK 620 6 HIS C 175 NE2 158.2 112.8 102.6 92.5 98.0
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 PO4 A 2201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 2202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZNH A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZNH C 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U74 RELATED DB: PDB
REMARK 900 ELECTRON TRANSFER COMPLEX BETWEEN YEAST CYTOCHROME C AND
REMARK 900 ZINE-PORPHYRIN SUBSTITUTED CYTOCHROME C PEROXIDASE
DBREF 1U75 A 1 294 GB 171177 AAA88709 69 362
DBREF 1U75 C 1 294 GB 171177 AAA88709 69 362
DBREF 1U75 B 1 104 UNP P00004 CYC_HORSE 1 104
SEQADV 1U75 MET A -1 GB 171177 CLONING ARTIFACT
SEQADV 1U75 ILE A 0 GB 171177 CLONING ARTIFACT
SEQADV 1U75 MET C -1 GB 171177 CLONING ARTIFACT
SEQADV 1U75 ILE C 0 GB 171177 CLONING ARTIFACT
SEQRES 1 A 296 MET ILE THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU
SEQRES 2 A 296 LYS GLY ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN
SEQRES 3 A 296 ALA ILE ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP
SEQRES 4 A 296 ASN TYR ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA
SEQRES 5 A 296 TRP HIS ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR
SEQRES 6 A 296 GLY GLY SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU
SEQRES 7 A 296 PHE ASN ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE
SEQRES 8 A 296 LYS PHE LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE
SEQRES 9 A 296 SER SER GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA
SEQRES 10 A 296 VAL GLN GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS
SEQRES 11 A 296 GLY ARG VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN
SEQRES 12 A 296 GLY ARG LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL
SEQRES 13 A 296 ARG THR PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU
SEQRES 14 A 296 VAL VAL ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR
SEQRES 15 A 296 HIS LEU LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA
SEQRES 16 A 296 ALA ASN ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU
SEQRES 17 A 296 LEU ASN GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN
SEQRES 18 A 296 ASN GLU GLN TRP ASP SER LYS SER GLY TYR MET MET LEU
SEQRES 19 A 296 PRO THR ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU
SEQRES 20 A 296 SER ILE VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE
SEQRES 21 A 296 PHE LYS ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU
SEQRES 22 A 296 ASN GLY ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE
SEQRES 23 A 296 ILE PHE LYS THR LEU GLU GLU GLN GLY LEU
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 296 MET ILE THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU
SEQRES 2 C 296 LYS GLY ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN
SEQRES 3 C 296 ALA ILE ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP
SEQRES 4 C 296 ASN TYR ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA
SEQRES 5 C 296 TRP HIS ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR
SEQRES 6 C 296 GLY GLY SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU
SEQRES 7 C 296 PHE ASN ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE
SEQRES 8 C 296 LYS PHE LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE
SEQRES 9 C 296 SER SER GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA
SEQRES 10 C 296 VAL GLN GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS
SEQRES 11 C 296 GLY ARG VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN
SEQRES 12 C 296 GLY ARG LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL
SEQRES 13 C 296 ARG THR PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU
SEQRES 14 C 296 VAL VAL ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR
SEQRES 15 C 296 HIS LEU LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA
SEQRES 16 C 296 ALA ASN ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU
SEQRES 17 C 296 LEU ASN GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN
SEQRES 18 C 296 ASN GLU GLN TRP ASP SER LYS SER GLY TYR MET MET LEU
SEQRES 19 C 296 PRO THR ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU
SEQRES 20 C 296 SER ILE VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE
SEQRES 21 C 296 PHE LYS ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU
SEQRES 22 C 296 ASN GLY ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE
SEQRES 23 C 296 ILE PHE LYS THR LEU GLU GLU GLN GLY LEU
HET PO4 A2201 5
HET PO4 C2202 5
HET ZNH A1001 43
HET HEM B1101 43
HET ZNH C1201 43
HETNAM PO4 PHOSPHATE ION
HETNAM ZNH PROTOPORPHYRIN IX CONTAINING ZN
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 6 ZNH 2(C34 H32 N4 O4 ZN)
FORMUL 7 HEM C34 H32 FE N4 O4
FORMUL 9 HOH *320(H2 O)
HELIX 1 1 SER A 15 ASP A 33 1 19
HELIX 2 2 GLU A 35 ILE A 40 1 6
HELIX 3 3 TYR A 42 GLY A 55 1 14
HELIX 4 4 GLY A 69 ARG A 72 5 4
HELIX 5 5 PHE A 73 ASN A 78 1 6
HELIX 6 6 ASP A 79 GLY A 84 5 6
HELIX 7 7 LEU A 85 PHE A 99 1 15
HELIX 8 8 SER A 103 MET A 119 1 17
HELIX 9 9 PRO A 134 THR A 138 5 5
HELIX 10 10 ASP A 150 ARG A 160 1 11
HELIX 11 11 ASN A 164 MET A 172 1 9
HELIX 12 12 GLY A 173 LEU A 177 5 5
HELIX 13 13 HIS A 181 GLY A 186 1 6
HELIX 14 14 ASN A 200 GLU A 209 1 10
HELIX 15 15 LEU A 232 ASP A 241 1 10
HELIX 16 16 ASP A 241 ASP A 254 1 14
HELIX 17 17 ASP A 254 ASN A 272 1 19
HELIX 18 18 THR A 288 GLY A 293 5 6
HELIX 19 19 LYS B 5 CYS B 14 1 10
HELIX 20 20 ASN B 52 GLY B 56 5 5
HELIX 21 21 LYS B 87 THR B 102 1 16
HELIX 22 22 SER C 15 ASP C 33 1 19
HELIX 23 23 GLU C 35 ILE C 40 1 6
HELIX 24 24 TYR C 42 GLY C 55 1 14
HELIX 25 25 GLY C 69 ARG C 72 5 4
HELIX 26 26 PHE C 73 ASN C 78 1 6
HELIX 27 27 ASP C 79 ALA C 83 5 5
HELIX 28 28 LEU C 85 PHE C 99 1 15
HELIX 29 29 SER C 103 MET C 119 1 17
HELIX 30 30 PRO C 134 THR C 138 5 5
HELIX 31 31 ASP C 150 ARG C 160 1 11
HELIX 32 32 ASN C 164 MET C 172 1 9
HELIX 33 33 GLY C 173 LEU C 177 5 5
HELIX 34 34 HIS C 181 GLY C 186 1 6
HELIX 35 35 ASN C 200 GLU C 209 1 10
HELIX 36 36 LEU C 232 SER C 237 1 6
HELIX 37 37 ASP C 241 ASP C 254 1 14
HELIX 38 38 ASP C 254 ASN C 272 1 19
SHEET 1 A 2 HIS A 6 VAL A 7 0
SHEET 2 A 2 ILE A 274 THR A 275 1 O THR A 275 N HIS A 6
SHEET 1 B 2 LYS A 179 THR A 180 0
SHEET 2 B 2 GLY A 189 PRO A 190 -1 O GLY A 189 N THR A 180
SHEET 1 C 3 LYS A 212 LYS A 215 0
SHEET 2 C 3 GLU A 221 ASP A 224 -1 O ASP A 224 N LYS A 212
SHEET 3 C 3 MET A 230 MET A 231 -1 O MET A 231 N TRP A 223
SHEET 1 D 2 LYS C 179 THR C 180 0
SHEET 2 D 2 GLY C 189 PRO C 190 -1 O GLY C 189 N THR C 180
SHEET 1 E 3 TRP C 211 LYS C 215 0
SHEET 2 E 3 GLU C 221 SER C 225 -1 O ASP C 224 N LYS C 212
SHEET 3 E 3 MET C 230 MET C 231 -1 O MET C 231 N TRP C 223
LINK FE HEM B1101 NE2 HIS B 18 1555 1555 2.04
LINK NE1 TRP A 51 O2 PO4 A2201 1555 1555 1.39
LINK NB ZNH A1001 O1 PO4 A2201 1555 1555 1.36
LINK ZN ZNH A1001 O1 PO4 A2201 1555 1555 1.57
LINK ZN ZNH A1001 NE2 HIS A 175 1555 1555 1.95
LINK SG CYS B 14 CAB HEM B1101 1555 1555 1.71
LINK FE HEM B1101 SD MET B 80 1555 1555 2.70
LINK ZN ZNH C1201 O1 PO4 C2202 1555 1555 1.19
LINK ZN ZNH C1201 NE2 HIS C 175 1555 1555 2.10
CISPEP 1 THR A 2 PRO A 3 0 -2.55
SITE 1 AC1 6 ARG A 48 TRP A 51 HIS A 52 HIS A 175
SITE 2 AC1 6 ZNH A1001 HOH A2004
SITE 1 AC2 5 ARG C 48 TRP C 51 HIS C 52 HIS C 175
SITE 2 AC2 5 ZNH C1201
SITE 1 AC3 20 PRO A 44 ARG A 48 TRP A 51 LEU A 171
SITE 2 AC3 20 MET A 172 ALA A 174 HIS A 175 LEU A 177
SITE 3 AC3 20 GLY A 178 LYS A 179 THR A 180 HIS A 181
SITE 4 AC3 20 ASN A 184 SER A 185 TRP A 191 LEU A 232
SITE 5 AC3 20 THR A 234 PHE A 266 HOH A2004 PO4 A2201
SITE 1 AC4 17 LYS B 13 CYS B 14 CYS B 17 HIS B 18
SITE 2 AC4 17 THR B 28 THR B 40 GLY B 41 GLN B 42
SITE 3 AC4 17 TYR B 48 THR B 49 ASN B 52 TRP B 59
SITE 4 AC4 17 TYR B 67 THR B 78 LYS B 79 MET B 80
SITE 5 AC4 17 PHE B 82
SITE 1 AC5 17 PRO C 44 ARG C 48 TRP C 51 PRO C 145
SITE 2 AC5 17 ASP C 146 LEU C 171 ALA C 174 HIS C 175
SITE 3 AC5 17 GLY C 178 LYS C 179 HIS C 181 ASN C 184
SITE 4 AC5 17 SER C 185 TRP C 191 HOH C1422 HOH C1534
SITE 5 AC5 17 PO4 C2202
CRYST1 104.465 104.465 186.884 90.00 90.00 90.00 P 43 21 2 16
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 0.009573 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009573 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
