HEADER OXIDOREDUCTASE 17-MAY-11 3S33
TITLE STRUCTURE OF THERMUS THERMOPHILUS CYTOCHROME BA3 OXIDASE 10S AFTER XE
TITLE 2 DEPRESSURIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME C BA(3) SUBUNIT I, CYTOCHROME C OXIDASE
COMPND 5 POLYPEPTIDE I, CYTOCHROME CBA3 SUBUNIT 1;
COMPND 6 EC: 1.9.3.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: CYTOCHROME C BA(3) SUBUNIT II, CYTOCHROME C OXIDASE
COMPND 12 POLYPEPTIDE II, CYTOCHROME CBA3 SUBUNIT 2;
COMPND 13 EC: 1.9.3.1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE 2A;
COMPND 17 CHAIN: C;
COMPND 18 SYNONYM: CYTOCHROME C BA(3) SUBUNIT IIA, CYTOCHROME C OXIDASE
COMPND 19 POLYPEPTIDE IIA, CYTOCHROME CBA3 SUBUNIT 2A;
COMPND 20 EC: 1.9.3.1;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: CBAA, TTHA1135;
SOURCE 6 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 300852;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMK18;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 13 ORGANISM_TAXID: 300852;
SOURCE 14 STRAIN: HB8;
SOURCE 15 GENE: CBAB, CBAC, CTAC, TTHA1134;
SOURCE 16 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 300852;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PMK18;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 23 ORGANISM_TAXID: 300852;
SOURCE 24 STRAIN: HB8;
SOURCE 25 GENE: CBAD, TTHA1133;
SOURCE 26 EXPRESSION_SYSTEM: THERMUS THERMOPHILUS;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 300852;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: HB8;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PMK18
KEYWDS OXIDOREDUCTASE, XENON
EXPDTA X-RAY DIFFRACTION
AUTHOR V.M.LUNA,J.A.FEE,A.A.DENIZ,C.D.STOUT
REVDAT 4 13-SEP-23 3S33 1 REMARK SEQADV LINK
REVDAT 3 12-SEP-12 3S33 1 JRNL
REVDAT 2 30-MAY-12 3S33 1 JRNL
REVDAT 1 23-MAY-12 3S33 0
JRNL AUTH V.M.LUNA,J.A.FEE,A.A.DENIZ,C.D.STOUT
JRNL TITL MOBILITY OF XE ATOMS WITHIN THE OXYGEN DIFFUSION CHANNEL OF
JRNL TITL 2 CYTOCHROME BA(3) OXIDASE.
JRNL REF BIOCHEMISTRY V. 51 4669 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22607023
JRNL DOI 10.1021/BI3003988
REMARK 2
REMARK 2 RESOLUTION. 4.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 6323
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) : 0.307
REMARK 3 R VALUE (WORKING SET) : 0.305
REMARK 3 FREE R VALUE : 0.350
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 294
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) : 4.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 435
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 18
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5964
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 130.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : -0.49000
REMARK 3 B33 (A**2) : 0.97000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 1.593
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.412
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 110.263
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.826
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.791
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6287 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8641 ; 1.267 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 753 ; 4.729 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;34.941 ;22.265
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 910 ;15.956 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.590 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 965 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4777 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3S33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.127
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6368
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.450
REMARK 200 RESOLUTION RANGE LOW (A) : 90.115
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 23.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.19300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.10
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : 0.51000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: 1XME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-17% PEG 2000, 0-200MM KCL, 15-60MM
REMARK 280 BIS-TRIS PH 7.0, 6.5MM NONYL-B-D-GLUCOPYRANOSIDE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 297K
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 81.32000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.12500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.12500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 121.98000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.12500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.12500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.66000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.12500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.12500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 121.98000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.12500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.12500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.66000
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 81.32000
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: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 13940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL
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 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 -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
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 SER A 9 CA GLY B 143 3444 1.03
REMARK 500 C GLU A 7 CA GLU B 144 3444 1.17
REMARK 500 C SER A 9 N GLY B 143 3444 1.17
REMARK 500 O SER A 9 N GLY B 143 3444 1.19
REMARK 500 N ILE A 8 CA GLU B 144 3444 1.30
REMARK 500 N ILE A 8 C GLU B 144 3444 1.32
REMARK 500 N ARG A 10 N GLY B 143 3444 1.36
REMARK 500 C GLU A 7 C GLU B 144 3444 1.45
REMARK 500 CA GLU A 7 CA GLU B 144 3444 1.49
REMARK 500 NH1 ARG A 10 CB PHE B 139 3444 1.51
REMARK 500 C SER A 9 C PRO B 142 3444 1.58
REMARK 500 C SER A 9 CA GLY B 143 3444 1.64
REMARK 500 N VAL A 11 C PRO B 142 3444 1.67
REMARK 500 O GLU A 7 N TYR B 145 3444 1.75
REMARK 500 CA ARG A 10 N GLY B 143 3444 1.76
REMARK 500 N ARG A 10 C PRO B 142 3444 1.78
REMARK 500 C GLU A 7 N TYR B 145 3444 1.78
REMARK 500 N VAL A 11 CB PRO B 142 3444 1.85
REMARK 500 O SER A 9 C PRO B 142 3444 1.86
REMARK 500 N ILE A 8 N GLU B 144 3444 1.92
REMARK 500 OE1 GLU A 13 N VAL B 166 3444 1.96
REMARK 500 N VAL A 11 CA PRO B 142 3444 1.96
REMARK 500 C GLU A 7 N GLU B 144 3444 1.98
REMARK 500 NH1 ARG A 10 CG PHE B 139 3444 2.01
REMARK 500 N ILE A 8 N TYR B 145 3444 2.01
REMARK 500 C ARG A 10 N GLY B 143 3444 2.02
REMARK 500 C SER A 9 O PRO B 142 3444 2.08
REMARK 500 O GLU A 7 O GLY B 143 3444 2.09
REMARK 500 CA GLU A 7 CB GLU B 144 3444 2.11
REMARK 500 OE2 GLU A 13 O GLY B 143 3444 2.13
REMARK 500 CA ARG A 10 CA PRO B 142 3444 2.13
REMARK 500 O SER A 9 O PRO B 142 3444 2.13
REMARK 500 CB ARG A 10 CA PRO B 142 3444 2.17
REMARK 500 CD GLU A 7 CG GLU B 144 3444 2.17
REMARK 500 C ARG A 10 C PRO B 142 3444 2.18
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 A 7 CB GLU A 7 CG 0.129
REMARK 500 GLY B 143 N GLY B 143 CA 0.117
REMARK 500 GLU B 144 N GLU B 144 CA 0.143
REMARK 500 GLU B 144 CA GLU B 144 C 0.164
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 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 GLU B 144 N - CA - C ANGL. DEV. = 16.8 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 ARG A 10 -37.78 -21.09
REMARK 500 VAL A 90 -43.68 -133.07
REMARK 500 ASN A 102 95.92 -47.33
REMARK 500 ALA A 129 49.59 -144.63
REMARK 500 LEU A 132 176.49 62.20
REMARK 500 PHE A 135 54.12 35.30
REMARK 500 PHE A 207 -74.19 -118.85
REMARK 500 PRO A 278 47.89 -82.06
REMARK 500 VAL A 279 11.32 -141.22
REMARK 500 ARG A 330 -111.09 -98.32
REMARK 500 SER A 368 45.38 -90.12
REMARK 500 PHE A 369 -94.25 44.56
REMARK 500 GLN A 388 -72.57 -92.54
REMARK 500 SER A 391 -82.27 -107.09
REMARK 500 ALA A 463 30.47 -87.37
REMARK 500 PRO A 507 60.00 -60.56
REMARK 500 ARG A 518 -64.00 -28.79
REMARK 500 GLU B 4 -57.76 64.71
REMARK 500 ALA B 87 86.34 -53.70
REMARK 500 PHE B 88 53.10 77.31
REMARK 500 ASP B 111 -86.02 -123.44
REMARK 500 GLU B 144 43.56 -81.70
REMARK 500 GLU C 3 -152.78 -156.51
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 HEM A 800 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 72 NE2
REMARK 620 2 HEM A 800 NA 96.2
REMARK 620 3 HEM A 800 NB 92.0 88.2
REMARK 620 4 HEM A 800 NC 77.2 173.3 90.8
REMARK 620 5 HEM A 800 ND 85.6 89.2 176.3 91.4
REMARK 620 6 HIS A 386 NE2 174.7 82.8 93.2 103.9 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 803 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 233 ND1
REMARK 620 2 HIS A 282 NE2 103.0
REMARK 620 3 HIS A 283 NE2 144.1 84.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HAS A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 384 NE2
REMARK 620 2 HAS A 801 NA 88.0
REMARK 620 3 HAS A 801 NB 91.1 178.5
REMARK 620 4 HAS A 801 NC 89.8 92.8 88.4
REMARK 620 5 HAS A 801 ND 89.2 91.4 87.3 175.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA B 802 CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 114 ND1
REMARK 620 2 CUA B 802 CU1 158.3
REMARK 620 3 CYS B 149 SG 130.5 40.7
REMARK 620 4 MET B 160 SD 95.5 103.9 91.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA B 802 CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 151 O
REMARK 620 2 CUA B 802 CU2 96.4
REMARK 620 3 CYS B 153 SG 88.3 40.5
REMARK 620 4 HIS B 157 ND1 86.3 157.5 117.6
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 CU A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAS A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A 563
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A 567
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S38 RELATED DB: PDB
REMARK 900 RELATED ID: 3S39 RELATED DB: PDB
REMARK 900 RELATED ID: 3S3A RELATED DB: PDB
REMARK 900 RELATED ID: 3S3B RELATED DB: PDB
REMARK 900 RELATED ID: 3S3C RELATED DB: PDB
REMARK 900 RELATED ID: 3S3D RELATED DB: PDB
DBREF 3S33 A 2 562 UNP Q5SJ79 COX1_THET8 2 562
DBREF 3S33 B 3 168 UNP Q5SJ80 COX2_THET8 3 168
DBREF 3S33 C 2 34 UNP P82543 COXA_THET8 2 34
SEQADV 3S33 MET A -5 UNP Q5SJ79 EXPRESSION TAG
SEQADV 3S33 HIS A -4 UNP Q5SJ79 EXPRESSION TAG
SEQADV 3S33 HIS A -3 UNP Q5SJ79 EXPRESSION TAG
SEQADV 3S33 HIS A -2 UNP Q5SJ79 EXPRESSION TAG
SEQADV 3S33 HIS A -1 UNP Q5SJ79 EXPRESSION TAG
SEQADV 3S33 HIS A 0 UNP Q5SJ79 EXPRESSION TAG
SEQADV 3S33 HIS A 1 UNP Q5SJ79 EXPRESSION TAG
SEQRES 1 A 568 MET HIS HIS HIS HIS HIS HIS ALA VAL ARG ALA SER GLU
SEQRES 2 A 568 ILE SER ARG VAL TYR GLU ALA TYR PRO GLU LYS LYS ALA
SEQRES 3 A 568 THR LEU TYR PHE LEU VAL LEU GLY PHE LEU ALA LEU ILE
SEQRES 4 A 568 VAL GLY SER LEU PHE GLY PRO PHE GLN ALA LEU ASN TYR
SEQRES 5 A 568 GLY ASN VAL ASP ALA TYR PRO LEU LEU LYS ARG LEU LEU
SEQRES 6 A 568 PRO PHE VAL GLN SER TYR TYR GLN GLY LEU THR LEU HIS
SEQRES 7 A 568 GLY VAL LEU ASN ALA ILE VAL PHE THR GLN LEU PHE ALA
SEQRES 8 A 568 GLN ALA ILE MET VAL TYR LEU PRO ALA ARG GLU LEU ASN
SEQRES 9 A 568 MET ARG PRO ASN MET GLY LEU MET TRP LEU SER TRP TRP
SEQRES 10 A 568 MET ALA PHE ILE GLY LEU VAL VAL ALA ALA LEU PRO LEU
SEQRES 11 A 568 LEU ALA ASN GLU ALA THR VAL LEU TYR THR PHE TYR PRO
SEQRES 12 A 568 PRO LEU LYS GLY HIS TRP ALA PHE TYR LEU GLY ALA SER
SEQRES 13 A 568 VAL PHE VAL LEU SER THR TRP VAL SER ILE TYR ILE VAL
SEQRES 14 A 568 LEU ASP LEU TRP ARG ARG TRP LYS ALA ALA ASN PRO GLY
SEQRES 15 A 568 LYS VAL THR PRO LEU VAL THR TYR MET ALA VAL VAL PHE
SEQRES 16 A 568 TRP LEU MET TRP PHE LEU ALA SER LEU GLY LEU VAL LEU
SEQRES 17 A 568 GLU ALA VAL LEU PHE LEU LEU PRO TRP SER PHE GLY LEU
SEQRES 18 A 568 VAL GLU GLY VAL ASP PRO LEU VAL ALA ARG THR LEU PHE
SEQRES 19 A 568 TRP TRP THR GLY HIS PRO ILE VAL TYR PHE TRP LEU LEU
SEQRES 20 A 568 PRO ALA TYR ALA ILE ILE TYR THR ILE LEU PRO LYS GLN
SEQRES 21 A 568 ALA GLY GLY LYS LEU VAL SER ASP PRO MET ALA ARG LEU
SEQRES 22 A 568 ALA PHE LEU LEU PHE LEU LEU LEU SER THR PRO VAL GLY
SEQRES 23 A 568 PHE HIS HIS GLN PHE ALA ASP PRO GLY ILE ASP PRO THR
SEQRES 24 A 568 TRP LYS MET ILE HIS SER VAL LEU THR LEU PHE VAL ALA
SEQRES 25 A 568 VAL PRO SER LEU MET THR ALA PHE THR VAL ALA ALA SER
SEQRES 26 A 568 LEU GLU PHE ALA GLY ARG LEU ARG GLY GLY ARG GLY LEU
SEQRES 27 A 568 PHE GLY TRP ILE ARG ALA LEU PRO TRP ASP ASN PRO ALA
SEQRES 28 A 568 PHE VAL ALA PRO VAL LEU GLY LEU LEU GLY PHE ILE PRO
SEQRES 29 A 568 GLY GLY ALA GLY GLY ILE VAL ASN ALA SER PHE THR LEU
SEQRES 30 A 568 ASP TYR VAL VAL HIS ASN THR ALA TRP VAL PRO GLY HIS
SEQRES 31 A 568 PHE HIS LEU GLN VAL ALA SER LEU VAL THR LEU THR ALA
SEQRES 32 A 568 MET GLY SER LEU TYR TRP LEU LEU PRO ASN LEU THR GLY
SEQRES 33 A 568 LYS PRO ILE SER ASP ALA GLN ARG ARG LEU GLY LEU ALA
SEQRES 34 A 568 VAL VAL TRP LEU TRP PHE LEU GLY MET MET ILE MET ALA
SEQRES 35 A 568 VAL GLY LEU HIS TRP ALA GLY LEU LEU ASN VAL PRO ARG
SEQRES 36 A 568 ARG ALA TYR ILE ALA GLN VAL PRO ASP ALA TYR PRO HIS
SEQRES 37 A 568 ALA ALA VAL PRO MET VAL PHE ASN VAL LEU ALA GLY ILE
SEQRES 38 A 568 VAL LEU LEU VAL ALA LEU LEU LEU PHE ILE TYR GLY LEU
SEQRES 39 A 568 PHE SER VAL LEU LEU SER ARG GLU ARG LYS PRO GLU LEU
SEQRES 40 A 568 ALA GLU ALA PRO LEU PRO PHE ALA GLU VAL ILE SER GLY
SEQRES 41 A 568 PRO GLU ASP ARG ARG LEU VAL LEU ALA MET ASP ARG ILE
SEQRES 42 A 568 GLY PHE TRP PHE ALA VAL ALA ALA ILE LEU VAL VAL LEU
SEQRES 43 A 568 ALA TYR GLY PRO THR LEU VAL GLN LEU PHE GLY HIS LEU
SEQRES 44 A 568 ASN PRO VAL PRO GLY TRP ARG LEU TRP
SEQRES 1 B 166 ASP GLU HIS LYS ALA HIS LYS ALA ILE LEU ALA TYR GLU
SEQRES 2 B 166 LYS GLY TRP LEU ALA PHE SER LEU ALA MET LEU PHE VAL
SEQRES 3 B 166 PHE ILE ALA LEU ILE ALA TYR THR LEU ALA THR HIS THR
SEQRES 4 B 166 ALA GLY VAL ILE PRO ALA GLY LYS LEU GLU ARG VAL ASP
SEQRES 5 B 166 PRO THR THR VAL ARG GLN GLU GLY PRO TRP ALA ASP PRO
SEQRES 6 B 166 ALA GLN ALA VAL VAL GLN THR GLY PRO ASN GLN TYR THR
SEQRES 7 B 166 VAL TYR VAL LEU ALA PHE ALA PHE GLY TYR GLN PRO ASN
SEQRES 8 B 166 PRO ILE GLU VAL PRO GLN GLY ALA GLU ILE VAL PHE LYS
SEQRES 9 B 166 ILE THR SER PRO ASP VAL ILE HIS GLY PHE HIS VAL GLU
SEQRES 10 B 166 GLY THR ASN ILE ASN VAL GLU VAL LEU PRO GLY GLU VAL
SEQRES 11 B 166 SER THR VAL ARG TYR THR PHE LYS ARG PRO GLY GLU TYR
SEQRES 12 B 166 ARG ILE ILE CYS ASN GLN TYR CYS GLY LEU GLY HIS GLN
SEQRES 13 B 166 ASN MET PHE GLY THR ILE VAL VAL LYS GLU
SEQRES 1 C 33 GLU GLU LYS PRO LYS GLY ALA LEU ALA VAL ILE LEU VAL
SEQRES 2 C 33 LEU THR LEU THR ILE LEU VAL PHE TRP LEU GLY VAL TYR
SEQRES 3 C 33 ALA VAL PHE PHE ALA ARG GLY
HET CU A 803 1
HET HEM A 800 43
HET HAS A 801 65
HET XE A 563 1
HET XE A 564 1
HET XE A 565 1
HET XE A 566 1
HET XE A 567 1
HET CUA B 802 2
HETNAM CU COPPER (II) ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM HAS HEME-AS
HETNAM XE XENON
HETNAM CUA DINUCLEAR COPPER ION
HETSYN HEM HEME
FORMUL 4 CU CU 2+
FORMUL 5 HEM C34 H32 FE N4 O4
FORMUL 6 HAS C54 H64 FE N4 O6
FORMUL 7 XE 5(XE)
FORMUL 12 CUA CU2
HELIX 1 1 ARG A 10 TYR A 15 1 6
HELIX 2 2 PRO A 16 LEU A 37 1 22
HELIX 3 3 LEU A 37 TYR A 46 1 10
HELIX 4 4 ALA A 51 LEU A 59 1 9
HELIX 5 5 SER A 64 ILE A 78 1 15
HELIX 6 6 ILE A 78 ASN A 98 1 21
HELIX 7 7 ASN A 102 ALA A 126 1 25
HELIX 8 8 HIS A 142 ASN A 174 1 33
HELIX 9 9 PRO A 180 PHE A 207 1 28
HELIX 10 10 PHE A 207 GLY A 214 1 8
HELIX 11 11 ASP A 220 HIS A 233 1 14
HELIX 12 12 HIS A 233 ILE A 250 1 18
HELIX 13 13 ILE A 250 GLY A 256 1 7
HELIX 14 14 SER A 261 SER A 276 1 16
HELIX 15 15 VAL A 279 GLN A 284 5 6
HELIX 16 16 ASP A 291 VAL A 305 1 15
HELIX 17 17 VAL A 305 ARG A 327 1 23
HELIX 18 18 PHE A 333 LEU A 339 1 7
HELIX 19 19 ASN A 343 ALA A 367 1 25
HELIX 20 20 SER A 368 THR A 370 5 3
HELIX 21 21 LEU A 371 HIS A 376 1 6
HELIX 22 22 ALA A 379 LEU A 387 1 9
HELIX 23 23 SER A 391 GLY A 410 1 20
HELIX 24 24 SER A 414 LEU A 445 1 32
HELIX 25 25 TYR A 452 ALA A 464 5 13
HELIX 26 26 VAL A 465 LEU A 493 1 29
HELIX 27 27 GLU A 516 ASP A 525 1 10
HELIX 28 28 ARG A 526 GLY A 551 1 26
HELIX 29 29 GLU B 4 THR B 39 1 36
HELIX 30 30 HIS B 40 ILE B 45 5 6
HELIX 31 31 ASP B 66 GLN B 69 5 4
HELIX 32 32 GLY B 156 ASN B 159 5 4
HELIX 33 33 PRO C 5 ARG C 33 1 29
SHEET 1 A 2 GLY A 218 VAL A 219 0
SHEET 2 A 2 VAL A 556 PRO A 557 -1 O VAL A 556 N VAL A 219
SHEET 1 B 3 VAL B 71 GLN B 73 0
SHEET 2 B 3 GLN B 78 PHE B 86 -1 O THR B 80 N VAL B 72
SHEET 3 B 3 GLY B 89 GLN B 91 -1 O GLN B 91 N LEU B 84
SHEET 1 C 4 VAL B 71 GLN B 73 0
SHEET 2 C 4 GLN B 78 PHE B 86 -1 O THR B 80 N VAL B 72
SHEET 3 C 4 GLU B 102 THR B 108 1 O VAL B 104 N TYR B 79
SHEET 4 C 4 SER B 133 TYR B 137 -1 O SER B 133 N ILE B 107
SHEET 1 D 5 ILE B 95 PRO B 98 0
SHEET 2 D 5 PHE B 161 LYS B 167 1 O VAL B 165 N ILE B 95
SHEET 3 D 5 GLY B 143 ILE B 148 -1 N TYR B 145 O ILE B 164
SHEET 4 D 5 HIS B 114 VAL B 118 -1 N HIS B 117 O ILE B 148
SHEET 5 D 5 ASN B 124 VAL B 127 -1 O VAL B 127 N HIS B 114
LINK NE2 HIS A 72 FE HEM A 800 1555 1555 2.14
LINK ND1 HIS A 233 CU CU A 803 1555 1555 1.73
LINK NE2 HIS A 282 CU CU A 803 1555 1555 2.20
LINK NE2 HIS A 283 CU CU A 803 1555 1555 1.96
LINK NE2 HIS A 384 FE HAS A 801 1555 1555 2.48
LINK NE2 HIS A 386 FE HEM A 800 1555 1555 2.02
LINK ND1 HIS B 114 CU2 CUA B 802 1555 1555 1.80
LINK SG CYS B 149 CU2 CUA B 802 1555 1555 2.38
LINK O GLN B 151 CU1 CUA B 802 1555 1555 2.48
LINK SG CYS B 153 CU1 CUA B 802 1555 1555 2.36
LINK ND1 HIS B 157 CU1 CUA B 802 1555 1555 1.96
LINK SD MET B 160 CU2 CUA B 802 1555 1555 2.39
CISPEP 1 PRO A 137 PRO A 138 0 1.97
CISPEP 2 GLN B 91 PRO B 92 0 0.00
CISPEP 3 ASN B 93 PRO B 94 0 -7.27
SITE 1 AC1 3 HIS A 233 HIS A 282 HIS A 283
SITE 1 AC2 24 SER A 36 GLY A 39 PRO A 40 GLN A 42
SITE 2 AC2 24 ALA A 43 TYR A 46 TYR A 65 LEU A 69
SITE 3 AC2 24 HIS A 72 ASN A 76 ALA A 77 LEU A 132
SITE 4 AC2 24 TYR A 133 PHE A 385 HIS A 386 VAL A 389
SITE 5 AC2 24 ALA A 390 THR A 394 TRP A 428 MET A 432
SITE 6 AC2 24 ARG A 449 ARG A 450 ALA A 451 LEU A 477
SITE 1 AC3 27 TYR A 133 TRP A 229 VAL A 236 TYR A 237
SITE 2 AC3 27 TRP A 239 HIS A 282 HIS A 283 SER A 309
SITE 3 AC3 27 ALA A 313 ALA A 317 TRP A 335 VAL A 350
SITE 4 AC3 27 LEU A 353 LEU A 354 PHE A 356 GLY A 360
SITE 5 AC3 27 GLY A 363 ASN A 366 ALA A 367 ASP A 372
SITE 6 AC3 27 HIS A 376 VAL A 381 HIS A 384 PHE A 385
SITE 7 AC3 27 GLN A 388 VAL A 389 ARG A 449
SITE 1 AC4 6 HIS B 114 CYS B 149 GLN B 151 CYS B 153
SITE 2 AC4 6 HIS B 157 MET B 160
SITE 1 AC5 1 GLY A 232
SITE 1 AC6 1 PHE A 228
CRYST1 108.250 108.250 162.640 90.00 90.00 90.00 P 43 21 2 8
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 0.009238 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006149 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
