HEADER OXIDOREDUCTASE 15-SEP-11 3TTV
TITLE STRUCTURE OF THE F413E VARIANT OF E. COLI KATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE HPII;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CATALASE KATE, HYDROXYPEROXIDASE II;
COMPND 5 EC: 1.11.1.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: B1732, JW1721, KATE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: UM255;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKS
KEYWDS HEME ORIENTATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.LOEWEN,V.JHA
REVDAT 4 06-DEC-23 3TTV 1 REMARK
REVDAT 3 13-SEP-23 3TTV 1 REMARK SEQADV LINK
REVDAT 2 27-FEB-13 3TTV 1 JRNL
REVDAT 1 12-OCT-11 3TTV 0
JRNL AUTH V.JHA,L.J.DONALD,P.C.LOEWEN
JRNL TITL MUTATION OF PHE413 TO TYR IN CATALASE KATE FROM ESCHERICHIA
JRNL TITL 2 COLI LEADS TO SIDE CHAIN DAMAGE AND MAIN CHAIN CLEAVAGE.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 525 207 2012
JRNL REFN ISSN 0003-9861
JRNL PMID 22172685
JRNL DOI 10.1016/J.ABB.2011.11.022
REMARK 2
REMARK 2 RESOLUTION. 1.45 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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 482857
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 24236
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 31866
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 1560
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22960
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 3326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : 0.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.059
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.062
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.906
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23851 ; 0.027 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32516 ; 2.663 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2920 ; 6.479 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1179 ;36.439 ;23.859
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3763 ;13.139 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 176 ;14.226 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3422 ; 0.196 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18832 ; 0.017 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 28 A 753 4
REMARK 3 1 B 28 B 753 4
REMARK 3 1 C 28 C 753 4
REMARK 3 1 D 28 D 753 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5733 ; 0.330 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 5733 ; 0.350 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 5733 ; 0.340 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 5733 ; 0.360 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5733 ; 2.750 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 5733 ; 2.650 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 5733 ; 2.340 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 5733 ; 2.110 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 28 A 753
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5219 -9.2131 31.8003
REMARK 3 T TENSOR
REMARK 3 T11: 0.0033 T22: 0.0081
REMARK 3 T33: 0.0254 T12: 0.0040
REMARK 3 T13: 0.0066 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.0668 L22: 0.0483
REMARK 3 L33: 0.0538 L12: -0.0002
REMARK 3 L13: 0.0116 L23: -0.0154
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: -0.0176 S13: -0.0285
REMARK 3 S21: 0.0084 S22: 0.0123 S23: 0.0242
REMARK 3 S31: -0.0006 S32: -0.0028 S33: -0.0062
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 28 B 753
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4534 11.8351 -18.9592
REMARK 3 T TENSOR
REMARK 3 T11: 0.0255 T22: 0.0072
REMARK 3 T33: 0.0221 T12: -0.0030
REMARK 3 T13: -0.0158 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.0541 L22: 0.0862
REMARK 3 L33: 0.0520 L12: -0.0337
REMARK 3 L13: -0.0255 L23: -0.0171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0113 S12: 0.0171 S13: 0.0177
REMARK 3 S21: -0.0378 S22: -0.0021 S23: 0.0146
REMARK 3 S31: -0.0039 S32: -0.0083 S33: -0.0092
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 28 C 753
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1975 -11.7457 -19.5604
REMARK 3 T TENSOR
REMARK 3 T11: 0.0322 T22: 0.0082
REMARK 3 T33: 0.0106 T12: -0.0010
REMARK 3 T13: 0.0087 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.0602 L22: 0.0655
REMARK 3 L33: 0.0601 L12: -0.0109
REMARK 3 L13: 0.0074 L23: -0.0090
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.0155 S13: -0.0196
REMARK 3 S21: -0.0417 S22: -0.0012 S23: -0.0041
REMARK 3 S31: 0.0178 S32: 0.0120 S33: 0.0029
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 28 D 753
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6918 9.0843 31.2335
REMARK 3 T TENSOR
REMARK 3 T11: 0.0078 T22: 0.0136
REMARK 3 T33: 0.0108 T12: -0.0027
REMARK 3 T13: -0.0028 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.0797 L22: 0.0488
REMARK 3 L33: 0.0406 L12: 0.0480
REMARK 3 L13: -0.0268 L23: -0.0025
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0206 S13: 0.0127
REMARK 3 S21: 0.0093 S22: -0.0072 S23: -0.0033
REMARK 3 S31: -0.0094 S32: 0.0205 S33: -0.0046
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:
REMARK 3 HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3TTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067912.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 482858
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 32.163
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : 0.49200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1GGE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 1.6 M LITHIUM CHLORIDE,
REMARK 280 0.1 M TRIS, PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 66.52500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 58630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 78970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -284.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 4
REMARK 465 ASN A 5
REMARK 465 GLU A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 PRO A 9
REMARK 465 HIS A 10
REMARK 465 GLN A 11
REMARK 465 HIS A 12
REMARK 465 GLN A 13
REMARK 465 SER A 14
REMARK 465 PRO A 15
REMARK 465 LEU A 16
REMARK 465 HIS A 17
REMARK 465 ASP A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 GLU A 21
REMARK 465 ALA A 22
REMARK 465 LYS A 23
REMARK 465 PRO A 24
REMARK 465 GLY A 25
REMARK 465 MET A 26
REMARK 465 ASP A 27
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 HIS B 4
REMARK 465 ASN B 5
REMARK 465 GLU B 6
REMARK 465 LYS B 7
REMARK 465 ASN B 8
REMARK 465 PRO B 9
REMARK 465 HIS B 10
REMARK 465 GLN B 11
REMARK 465 HIS B 12
REMARK 465 GLN B 13
REMARK 465 SER B 14
REMARK 465 PRO B 15
REMARK 465 LEU B 16
REMARK 465 HIS B 17
REMARK 465 ASP B 18
REMARK 465 SER B 19
REMARK 465 SER B 20
REMARK 465 GLU B 21
REMARK 465 ALA B 22
REMARK 465 LYS B 23
REMARK 465 PRO B 24
REMARK 465 GLY B 25
REMARK 465 MET B 26
REMARK 465 ASP B 27
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 HIS C 4
REMARK 465 ASN C 5
REMARK 465 GLU C 6
REMARK 465 LYS C 7
REMARK 465 ASN C 8
REMARK 465 PRO C 9
REMARK 465 HIS C 10
REMARK 465 GLN C 11
REMARK 465 HIS C 12
REMARK 465 GLN C 13
REMARK 465 SER C 14
REMARK 465 PRO C 15
REMARK 465 LEU C 16
REMARK 465 HIS C 17
REMARK 465 ASP C 18
REMARK 465 SER C 19
REMARK 465 SER C 20
REMARK 465 GLU C 21
REMARK 465 ALA C 22
REMARK 465 LYS C 23
REMARK 465 PRO C 24
REMARK 465 GLY C 25
REMARK 465 MET C 26
REMARK 465 ASP C 27
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 3
REMARK 465 HIS D 4
REMARK 465 ASN D 5
REMARK 465 GLU D 6
REMARK 465 LYS D 7
REMARK 465 ASN D 8
REMARK 465 PRO D 9
REMARK 465 HIS D 10
REMARK 465 GLN D 11
REMARK 465 HIS D 12
REMARK 465 GLN D 13
REMARK 465 SER D 14
REMARK 465 PRO D 15
REMARK 465 LEU D 16
REMARK 465 HIS D 17
REMARK 465 ASP D 18
REMARK 465 SER D 19
REMARK 465 SER D 20
REMARK 465 GLU D 21
REMARK 465 ALA D 22
REMARK 465 LYS D 23
REMARK 465 PRO D 24
REMARK 465 GLY D 25
REMARK 465 MET D 26
REMARK 465 ASP D 27
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 ND1 HIS D 392 CB TYR D 415 1.56
REMARK 500 ND1 HIS C 392 CB TYR C 415 1.57
REMARK 500 ND1 HIS B 392 CB TYR B 415 1.59
REMARK 500 ND1 HIS A 392 CB TYR A 415 1.59
REMARK 500 NE ARG D 488 O HOH D 2698 1.63
REMARK 500 NE2 HIS D 449 O HOH D 2501 1.65
REMARK 500 O HOH A 2238 O HOH A 2416 1.72
REMARK 500 O HOH A 2402 O HOH A 2868 1.78
REMARK 500 NH2 ARG A 479 O HOH A 2607 1.89
REMARK 500 O HOH D 1939 O HOH D 2903 1.93
REMARK 500 O HOH C 2497 O HOH D 1832 1.93
REMARK 500 O HOH A 3519 O HOH D 2485 1.94
REMARK 500 OE1 GLU C 283 O HOH C 2292 1.95
REMARK 500 O HOH B 1874 O HOH B 2016 1.95
REMARK 500 O HOH A 1067 O HOH A 3349 2.00
REMARK 500 O HOH D 2042 O HOH D 2245 2.01
REMARK 500 O HOH B 2741 O HOH B 3372 2.02
REMARK 500 O HOH A 1738 O HOH A 3512 2.03
REMARK 500 O HOH D 851 O HOH D 2659 2.03
REMARK 500 O HOH D 1772 O HOH D 3439 2.04
REMARK 500 O HOH A 2247 O HOH A 2575 2.07
REMARK 500 O HOH A 1162 O HOH A 2545 2.08
REMARK 500 O HOH D 763 O HOH D 3518 2.09
REMARK 500 O HOH D 2393 O HOH D 2703 2.09
REMARK 500 OE2 GLU D 731 O HOH D 3028 2.09
REMARK 500 OE1 GLU D 283 O HOH D 2496 2.12
REMARK 500 CG GLN A 546 O HOH A 3434 2.12
REMARK 500 O HOH B 2685 O HOH B 3359 2.13
REMARK 500 O HOH B 853 O HOH B 1874 2.13
REMARK 500 O HOH A 1111 O HOH A 3255 2.13
REMARK 500 O HOH D 2923 O HOH D 3380 2.13
REMARK 500 O HOH C 1185 O HOH C 1695 2.13
REMARK 500 O HOH B 1261 O HOH C 3165 2.14
REMARK 500 CE LYS B 533 O HOH C 2623 2.14
REMARK 500 O HOH C 787 O HOH C 2382 2.14
REMARK 500 O HOH D 2270 O HOH D 2713 2.16
REMARK 500 O HOH C 2041 O HOH C 2576 2.16
REMARK 500 O HOH B 2197 O HOH C 3168 2.17
REMARK 500 NH1 ARG C 636 O HOH C 2717 2.17
REMARK 500 OG SER A 743 O HOH A 1686 2.18
REMARK 500 O HOH B 2271 O HOH C 3063 2.18
REMARK 500 O HOH C 2497 O HOH D 767 2.18
REMARK 500 O HOH C 2207 O HOH C 2380 2.19
REMARK 500 CD ARG B 521 O HOH B 3047 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 2805 O HOH D 2468 1455 1.97
REMARK 500 OD1 ASP A 59 NH2 ARG B 369 2545 1.97
REMARK 500 OD1 ASP A 59 NH1 ARG B 369 2545 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 HIS A 36 CG HIS A 36 CD2 0.057
REMARK 500 ARG A 87 CZ ARG A 87 NH1 -0.078
REMARK 500 GLU A 321 CD GLU A 321 OE1 0.117
REMARK 500 GLU A 344 CD GLU A 344 OE1 0.075
REMARK 500 ARG A 377 CZ ARG A 377 NH1 0.079
REMARK 500 TYR A 440 CE1 TYR A 440 CZ 0.113
REMARK 500 TRP A 469 CE2 TRP A 469 CD2 0.074
REMARK 500 HIS A 549 CG HIS A 549 CD2 0.055
REMARK 500 GLU A 716 CD GLU A 716 OE1 0.083
REMARK 500 HIS B 36 CG HIS B 36 CD2 0.069
REMARK 500 HIS B 219 CG HIS B 219 CD2 0.077
REMARK 500 HIS B 226 CG HIS B 226 CD2 0.068
REMARK 500 HIS B 251 CG HIS B 251 CD2 0.063
REMARK 500 GLU B 333 CD GLU B 333 OE1 -0.070
REMARK 500 ASP B 568 CB ASP B 568 CG 0.137
REMARK 500 HIS B 739 CG HIS B 739 CD2 0.077
REMARK 500 ASP C 59 CB ASP C 59 CG 0.175
REMARK 500 HIS C 128 CG HIS C 128 CD2 0.056
REMARK 500 ARG C 377 CZ ARG C 377 NH1 0.081
REMARK 500 PHE C 391 CG PHE C 391 CD1 0.095
REMARK 500 HIS C 395 CG HIS C 395 CD2 0.058
REMARK 500 TYR C 440 CE1 TYR C 440 CZ 0.096
REMARK 500 HIS C 522 CG HIS C 522 CD2 0.066
REMARK 500 HIS C 739 CG HIS C 739 CD2 0.071
REMARK 500 TRP C 742 CE2 TRP C 742 CD2 0.074
REMARK 500 ARG D 37 CZ ARG D 37 NH1 0.082
REMARK 500 HIS D 219 CG HIS D 219 CD2 0.080
REMARK 500 HIS D 275 CG HIS D 275 CD2 0.058
REMARK 500 GLU D 321 CD GLU D 321 OE1 0.106
REMARK 500 GLU D 344 CD GLU D 344 OE2 0.078
REMARK 500 GLN D 368 CD GLN D 368 OE1 0.135
REMARK 500 ARG D 377 CZ ARG D 377 NH1 0.088
REMARK 500 TYR D 440 CE1 TYR D 440 CZ 0.105
REMARK 500 HIS D 507 CG HIS D 507 CD2 0.058
REMARK 500 HIS D 629 NE2 HIS D 629 CD2 -0.071
REMARK 500 HIS D 739 CG HIS D 739 CD2 0.063
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 37 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 118 CB - CG - OD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG A 165 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 PHE A 166 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP A 177 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 GLU A 248 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP A 259 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 260 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 278 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LYS A 309 CD - CE - NZ ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG A 313 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LYS A 372 CD - CE - NZ ANGL. DEV. = -15.7 DEGREES
REMARK 500 ARG A 377 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 411 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 411 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 450 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 450 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 471 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TYR A 485 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 488 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 488 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 PHE A 501 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 PHE A 501 CB - CG - CD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 509 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 PHE A 518 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ASP A 525 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 LEU A 552 CB - CG - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG A 636 NE - CZ - NH2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 663 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 722 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 740 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 740 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ASP B 70 CB - CG - OD1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP B 90 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 118 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG B 130 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 130 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LYS B 142 CD - CE - NZ ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG B 165 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 180 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP B 197 CB - CG - OD1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 LEU B 198 CB - CG - CD1 ANGL. DEV. = 15.7 DEGREES
REMARK 500 ASP B 241 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 259 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 259 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 278 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 118 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 75 -41.35 -165.31
REMARK 500 THR A 178 40.65 -98.69
REMARK 500 ILE A 274 -65.06 75.27
REMARK 500 ASP A 314 89.82 -157.76
REMARK 500 ASP A 446 -148.19 67.51
REMARK 500 ASP A 595 28.22 -156.61
REMARK 500 ASP A 725 -158.93 -118.25
REMARK 500 HIS A 739 -61.52 77.70
REMARK 500 SER B 75 -35.16 -164.30
REMARK 500 THR B 178 39.88 -94.90
REMARK 500 ILE B 274 -61.43 67.63
REMARK 500 ASP B 314 86.90 -156.52
REMARK 500 ASN B 442 -169.53 -163.29
REMARK 500 ASP B 446 -150.53 64.58
REMARK 500 HIS B 449 35.99 70.21
REMARK 500 ASP B 595 28.82 -142.53
REMARK 500 ARG B 612 97.98 -59.12
REMARK 500 ASP B 725 179.36 -34.10
REMARK 500 HIS B 739 -65.86 77.04
REMARK 500 SER C 75 -38.94 -169.70
REMARK 500 THR C 178 39.73 -94.25
REMARK 500 ILE C 274 -63.38 66.73
REMARK 500 ASP C 314 87.17 -154.35
REMARK 500 ASN C 442 -168.85 -160.72
REMARK 500 ASP C 446 -149.59 64.43
REMARK 500 HIS C 449 61.92 38.36
REMARK 500 LYS C 584 166.69 175.69
REMARK 500 ASP C 595 34.37 -142.49
REMARK 500 ALA C 724 47.47 -81.32
REMARK 500 ASP C 725 -134.46 -161.44
REMARK 500 HIS C 739 -64.99 69.12
REMARK 500 SER D 75 -38.17 -161.57
REMARK 500 THR D 178 40.85 -95.42
REMARK 500 ILE D 274 -65.35 72.87
REMARK 500 ASP D 314 88.46 -154.04
REMARK 500 ASP D 446 -150.01 64.72
REMARK 500 ASP D 595 35.41 -140.18
REMARK 500 HIS D 739 -69.15 79.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA C 724 ASP C 725 142.52
REMARK 500 ASP C 725 GLY C 726 -138.82
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 ARG B 121 0.07 SIDE CHAIN
REMARK 500 ARG C 121 0.07 SIDE CHAIN
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 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415 OH
REMARK 620 2 HEM A 760 NA 96.4
REMARK 620 3 HEM A 760 NB 94.7 88.7
REMARK 620 4 HEM A 760 NC 99.6 164.1 90.7
REMARK 620 5 HEM A 760 ND 100.0 88.7 165.3 87.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415 OH
REMARK 620 2 HEM B 760 NA 97.2
REMARK 620 3 HEM B 760 NB 92.8 90.6
REMARK 620 4 HEM B 760 NC 98.4 164.4 87.5
REMARK 620 5 HEM B 760 ND 100.5 89.8 166.5 88.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415 OH
REMARK 620 2 HEM C 760 NA 95.3
REMARK 620 3 HEM C 760 NB 92.8 89.7
REMARK 620 4 HEM C 760 NC 99.4 165.3 90.1
REMARK 620 5 HEM C 760 ND 101.9 88.6 165.3 87.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 415 OH
REMARK 620 2 HEM D 760 NA 97.0
REMARK 620 3 HEM D 760 NB 92.9 89.9
REMARK 620 4 HEM D 760 NC 98.9 164.1 88.7
REMARK 620 5 HEM D 760 ND 101.4 88.9 165.7 88.5
REMARK 620 N 1 2 3 4
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 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 760
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TTT RELATED DB: PDB
REMARK 900 RELATED ID: 3TTU RELATED DB: PDB
REMARK 900 RELATED ID: 3TTW RELATED DB: PDB
REMARK 900 RELATED ID: 3TTX RELATED DB: PDB
DBREF 3TTV A 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 3TTV B 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 3TTV C 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 3TTV D 1 753 UNP P21179 CATE_ECOLI 1 753
SEQADV 3TTV ALA A 115 UNP P21179 THR 115 ENGINEERED MUTATION
SEQADV 3TTV TYR A 413 UNP P21179 PHE 413 ENGINEERED MUTATION
SEQADV 3TTV ALA B 115 UNP P21179 THR 115 ENGINEERED MUTATION
SEQADV 3TTV TYR B 413 UNP P21179 PHE 413 ENGINEERED MUTATION
SEQADV 3TTV ALA C 115 UNP P21179 THR 115 ENGINEERED MUTATION
SEQADV 3TTV TYR C 413 UNP P21179 PHE 413 ENGINEERED MUTATION
SEQADV 3TTV ALA D 115 UNP P21179 THR 115 ENGINEERED MUTATION
SEQADV 3TTV TYR D 413 UNP P21179 PHE 413 ENGINEERED MUTATION
SEQRES 1 A 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 A 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 A 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 A 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 A 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 A 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 A 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 A 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 A 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE ALA HIS PHE
SEQRES 10 A 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 A 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 A 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 A 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 A 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 A 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 A 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 A 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 A 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 A 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 A 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 A 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 A 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 A 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 A 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 A 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 A 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 A 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 A 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 A 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 A 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 A 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 A 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR THR
SEQRES 33 A 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 A 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 A 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 A 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 A 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 A 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 A 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 A 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 A 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 A 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 A 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 A 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 A 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 A 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 A 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 A 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 A 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 A 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 A 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 A 753 ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 A 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 A 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 A 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 A 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 A 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 A 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 B 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 B 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 B 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 B 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 B 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 B 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 B 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 B 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 B 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE ALA HIS PHE
SEQRES 10 B 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 B 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 B 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 B 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 B 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 B 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 B 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 B 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 B 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 B 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 B 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 B 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 B 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 B 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 B 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 B 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 B 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 B 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 B 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 B 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 B 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 B 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 B 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR THR
SEQRES 33 B 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 B 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 B 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 B 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 B 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 B 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 B 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 B 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 B 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 B 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 B 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 B 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 B 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 B 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 B 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 B 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 B 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 B 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 B 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 B 753 ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 B 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 B 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 B 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 B 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 B 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 B 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 C 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 C 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 C 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 C 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 C 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 C 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 C 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 C 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 C 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE ALA HIS PHE
SEQRES 10 C 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 C 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 C 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 C 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 C 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 C 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 C 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 C 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 C 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 C 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 C 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 C 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 C 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 C 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 C 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 C 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 C 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 C 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 C 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 C 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 C 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 C 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 C 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR THR
SEQRES 33 C 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 C 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 C 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 C 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 C 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 C 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 C 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 C 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 C 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 C 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 C 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 C 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 C 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 C 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 C 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 C 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 C 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 C 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 C 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 C 753 ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 C 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 C 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 C 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 C 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 C 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 C 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 D 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 D 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 D 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 D 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 D 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 D 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 D 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 D 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 D 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE ALA HIS PHE
SEQRES 10 D 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 D 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 D 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 D 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 D 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 D 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 D 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 D 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 D 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 D 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 D 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 D 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 D 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 D 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 D 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 D 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 D 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 D 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 D 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 D 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 D 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 D 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 D 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR THR
SEQRES 33 D 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 D 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 D 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 D 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 D 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 D 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 D 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 D 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 D 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 D 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 D 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 D 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 D 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 D 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 D 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 D 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 D 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 D 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 D 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 D 753 ALA VAL ILE VAL PRO OCS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 D 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 D 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 D 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 D 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 D 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 D 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
MODRES 3TTV OCS A 669 CYS CYSTEINESULFONIC ACID
MODRES 3TTV OCS B 669 CYS CYSTEINESULFONIC ACID
MODRES 3TTV OCS C 669 CYS CYSTEINESULFONIC ACID
MODRES 3TTV OCS D 669 CYS CYSTEINESULFONIC ACID
HET OCS A 669 9
HET OCS B 669 9
HET OCS C 669 9
HET OCS D 669 9
HET HEM A 760 43
HET HEM B 760 43
HET HEM C 760 43
HET HEM D 760 43
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 1 OCS 4(C3 H7 N O5 S)
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 HOH *3326(H2 O)
HELIX 1 1 PRO A 52 ALA A 57 1 6
HELIX 2 2 ASN A 62 LEU A 68 1 7
HELIX 3 3 ASP A 107 HIS A 119 1 13
HELIX 4 4 ALA A 150 SER A 154 5 5
HELIX 5 5 ASP A 210 HIS A 212 5 3
HELIX 6 6 LYS A 213 LYS A 222 1 10
HELIX 7 7 HIS A 236 GLN A 246 1 11
HELIX 8 8 THR A 249 SER A 258 1 10
HELIX 9 9 ASP A 259 ILE A 262 5 4
HELIX 10 10 SER A 265 MET A 269 5 5
HELIX 11 11 VAL A 303 ASP A 314 1 12
HELIX 12 12 ASP A 316 GLY A 329 1 14
HELIX 13 13 GLU A 344 GLU A 346 5 3
HELIX 14 14 ASN A 381 ASN A 386 1 6
HELIX 15 15 ASP A 405 GLY A 424 1 20
HELIX 16 16 ASN A 427 ARG A 435 5 9
HELIX 17 17 SER A 498 GLY A 502 5 5
HELIX 18 18 TYR A 505 GLN A 515 1 11
HELIX 19 19 THR A 516 LYS A 533 1 18
HELIX 20 20 ARG A 536 HIS A 549 1 14
HELIX 21 21 ASP A 551 LEU A 562 1 12
HELIX 22 22 THR A 567 ASN A 572 1 6
HELIX 23 23 ASP A 585 SER A 589 5 5
HELIX 24 24 ARG A 612 LYS A 626 1 15
HELIX 25 25 PRO A 658 VAL A 662 5 5
HELIX 26 26 ASN A 671 ILE A 675 5 5
HELIX 27 27 ASN A 678 HIS A 691 1 14
HELIX 28 28 ASP A 700 LYS A 709 5 10
HELIX 29 29 ASP A 725 ALA A 738 1 14
HELIX 30 30 VAL A 741 SER A 743 5 3
HELIX 31 31 ARG A 744 ASP A 749 1 6
HELIX 32 32 PRO B 52 ALA B 57 1 6
HELIX 33 33 ASN B 62 LEU B 68 1 7
HELIX 34 34 ASP B 107 HIS B 119 1 13
HELIX 35 35 ALA B 150 SER B 154 5 5
HELIX 36 36 ASP B 210 HIS B 212 5 3
HELIX 37 37 LYS B 213 LYS B 222 1 10
HELIX 38 38 HIS B 236 GLN B 246 1 11
HELIX 39 39 THR B 249 SER B 258 1 10
HELIX 40 40 ASP B 259 ILE B 262 5 4
HELIX 41 41 SER B 265 MET B 269 5 5
HELIX 42 42 VAL B 303 ASP B 314 1 12
HELIX 43 43 ASP B 316 GLY B 329 1 14
HELIX 44 44 GLU B 344 GLU B 346 5 3
HELIX 45 45 ASN B 381 ASN B 386 1 6
HELIX 46 46 ASP B 405 GLY B 424 1 20
HELIX 47 47 ASN B 427 ARG B 435 5 9
HELIX 48 48 SER B 498 GLY B 502 5 5
HELIX 49 49 TYR B 505 SER B 514 1 10
HELIX 50 50 THR B 516 LYS B 533 1 18
HELIX 51 51 ARG B 536 HIS B 549 1 14
HELIX 52 52 ASP B 551 LEU B 562 1 12
HELIX 53 53 THR B 567 ASN B 572 1 6
HELIX 54 54 ASP B 585 SER B 589 5 5
HELIX 55 55 ARG B 612 LYS B 626 1 15
HELIX 56 56 PRO B 658 VAL B 662 5 5
HELIX 57 57 ASN B 671 ILE B 675 5 5
HELIX 58 58 ASN B 678 HIS B 691 1 14
HELIX 59 59 ASP B 700 THR B 707 5 8
HELIX 60 60 ASP B 725 ALA B 738 1 14
HELIX 61 61 VAL B 741 SER B 743 5 3
HELIX 62 62 ARG B 744 ASP B 749 1 6
HELIX 63 63 PRO C 52 ALA C 57 1 6
HELIX 64 64 ASN C 62 LEU C 68 1 7
HELIX 65 65 ASP C 107 HIS C 119 1 13
HELIX 66 66 ALA C 150 SER C 154 5 5
HELIX 67 67 ASP C 210 HIS C 212 5 3
HELIX 68 68 LYS C 213 LYS C 222 1 10
HELIX 69 69 HIS C 236 GLN C 246 1 11
HELIX 70 70 THR C 249 SER C 258 1 10
HELIX 71 71 ASP C 259 ILE C 262 5 4
HELIX 72 72 SER C 265 MET C 269 5 5
HELIX 73 73 VAL C 303 ASP C 314 1 12
HELIX 74 74 ASP C 316 GLY C 329 1 14
HELIX 75 75 GLU C 344 GLU C 346 5 3
HELIX 76 76 ASN C 381 ASN C 386 1 6
HELIX 77 77 ASP C 405 GLY C 424 1 20
HELIX 78 78 ASN C 427 ARG C 435 5 9
HELIX 79 79 SER C 498 GLY C 502 5 5
HELIX 80 80 TYR C 505 SER C 514 1 10
HELIX 81 81 THR C 516 LYS C 533 1 18
HELIX 82 82 ARG C 536 HIS C 549 1 14
HELIX 83 83 ASP C 551 LEU C 562 1 12
HELIX 84 84 THR C 567 ASN C 572 1 6
HELIX 85 85 ASP C 585 SER C 589 5 5
HELIX 86 86 ARG C 612 LYS C 626 1 15
HELIX 87 87 PRO C 658 VAL C 662 5 5
HELIX 88 88 ILE C 672 ASP C 677 1 6
HELIX 89 89 ASN C 678 HIS C 691 1 14
HELIX 90 90 ASP C 700 LYS C 709 5 10
HELIX 91 91 SER C 727 ALA C 738 1 12
HELIX 92 92 VAL C 741 SER C 743 5 3
HELIX 93 93 ARG C 744 ASP C 749 1 6
HELIX 94 94 PRO D 52 ALA D 57 1 6
HELIX 95 95 ASN D 62 LEU D 68 1 7
HELIX 96 96 ASP D 107 HIS D 119 1 13
HELIX 97 97 ALA D 150 SER D 154 5 5
HELIX 98 98 ASP D 210 HIS D 212 5 3
HELIX 99 99 LYS D 213 LYS D 222 1 10
HELIX 100 100 HIS D 236 GLN D 246 1 11
HELIX 101 101 THR D 249 SER D 258 1 10
HELIX 102 102 ASP D 259 ILE D 262 5 4
HELIX 103 103 SER D 265 MET D 269 5 5
HELIX 104 104 VAL D 303 ASP D 314 1 12
HELIX 105 105 ASP D 316 GLY D 329 1 14
HELIX 106 106 GLU D 344 GLU D 346 5 3
HELIX 107 107 ASN D 381 ASN D 386 1 6
HELIX 108 108 ASP D 405 GLY D 424 1 20
HELIX 109 109 ASN D 427 ARG D 435 5 9
HELIX 110 110 SER D 498 GLY D 502 5 5
HELIX 111 111 TYR D 505 SER D 514 1 10
HELIX 112 112 THR D 516 LYS D 533 1 18
HELIX 113 113 ARG D 536 HIS D 549 1 14
HELIX 114 114 ASP D 551 LEU D 562 1 12
HELIX 115 115 THR D 567 ASN D 572 1 6
HELIX 116 116 ASP D 585 SER D 589 5 5
HELIX 117 117 ARG D 612 LYS D 626 1 15
HELIX 118 118 PRO D 658 VAL D 662 5 5
HELIX 119 119 ASN D 671 ILE D 675 5 5
HELIX 120 120 ASN D 678 HIS D 691 1 14
HELIX 121 121 ASP D 700 LYS D 709 5 10
HELIX 122 122 SER D 727 ALA D 738 1 12
HELIX 123 123 VAL D 741 SER D 743 5 3
HELIX 124 124 ARG D 744 ASP D 749 1 6
SHEET 1 A 2 ARG A 72 LYS A 73 0
SHEET 2 A 2 ILE C 453 ASP C 454 1 O ILE C 453 N LYS A 73
SHEET 1 B 4 LEU A 95 ALA A 97 0
SHEET 2 B 4 ARG D 488 ARG D 495 -1 O VAL D 494 N ARG A 96
SHEET 3 B 4 ARG C 488 ARG C 495 -1 N GLY C 491 O VAL D 489
SHEET 4 B 4 LEU B 95 ALA B 97 -1 N ARG B 96 O VAL C 494
SHEET 1 C11 LEU A 400 ASP A 401 0
SHEET 2 C11 PHE A 277 ILE A 280 -1 N ARG A 278 O ASP A 401
SHEET 3 C11 ALA A 286 PRO A 295 -1 O VAL A 289 N PHE A 277
SHEET 4 C11 GLU A 333 PRO A 342 -1 O GLN A 339 N ARG A 290
SHEET 5 C11 GLN A 368 ARG A 377 -1 O GLN A 368 N PHE A 338
SHEET 6 C11 GLY A 131 PRO A 140 -1 N HIS A 135 O ARG A 377
SHEET 7 C11 THR A 160 SER A 167 -1 O PHE A 166 N SER A 132
SHEET 8 C11 GLY A 184 THR A 191 -1 O LYS A 188 N PHE A 163
SHEET 9 C11 GLY A 194 ASN A 201 -1 O PHE A 196 N PHE A 189
SHEET 10 C11 GLY A 271 PHE A 272 -1 O PHE A 272 N ASN A 201
SHEET 11 C11 ALA A 286 PRO A 295 -1 O TRP A 293 N GLY A 271
SHEET 1 D 2 ILE A 453 ASP A 454 0
SHEET 2 D 2 ARG C 72 LYS C 73 1 O LYS C 73 N ILE A 453
SHEET 1 E 4 LEU C 95 ALA C 97 0
SHEET 2 E 4 ARG B 488 ARG B 495 -1 N VAL B 494 O ARG C 96
SHEET 3 E 4 ARG A 488 ARG A 495 -1 N GLY A 491 O VAL B 489
SHEET 4 E 4 LEU D 95 ALA D 97 -1 O ARG D 96 N VAL A 494
SHEET 1 F 6 ALA A 652 THR A 653 0
SHEET 2 F 6 HIS A 629 TYR A 634 1 N TYR A 634 O ALA A 652
SHEET 3 F 6 VAL A 602 LEU A 606 1 N ILE A 605 O LYS A 631
SHEET 4 F 6 ALA A 664 VAL A 667 1 O ILE A 666 N ALA A 604
SHEET 5 F 6 ILE A 695 ALA A 698 1 O ALA A 696 N VAL A 667
SHEET 6 F 6 ILE A 718 ALA A 721 1 O VAL A 719 N LEU A 697
SHEET 1 G 2 GLU A 639 THR A 641 0
SHEET 2 G 2 VAL A 647 PRO A 649 -1 O LEU A 648 N VAL A 640
SHEET 1 H 2 ARG B 72 LYS B 73 0
SHEET 2 H 2 ILE D 453 ASP D 454 1 O ILE D 453 N LYS B 73
SHEET 1 I11 LEU B 400 ASP B 401 0
SHEET 2 I11 PHE B 277 ILE B 280 -1 N ARG B 278 O ASP B 401
SHEET 3 I11 ALA B 286 PRO B 295 -1 O THR B 287 N LEU B 279
SHEET 4 I11 GLU B 333 PRO B 342 -1 O GLY B 337 N HIS B 292
SHEET 5 I11 VAL B 367 ARG B 377 -1 O GLN B 368 N PHE B 338
SHEET 6 I11 GLY B 131 PRO B 140 -1 N HIS B 135 O ARG B 377
SHEET 7 I11 THR B 160 SER B 167 -1 O PHE B 166 N SER B 132
SHEET 8 I11 GLY B 184 THR B 191 -1 O LYS B 188 N PHE B 163
SHEET 9 I11 GLY B 194 ASN B 201 -1 O PHE B 196 N PHE B 189
SHEET 10 I11 GLY B 271 PHE B 272 -1 O PHE B 272 N ASN B 201
SHEET 11 I11 ALA B 286 PRO B 295 -1 O TRP B 293 N GLY B 271
SHEET 1 J 2 ILE B 453 ASP B 454 0
SHEET 2 J 2 ARG D 72 LYS D 73 1 O LYS D 73 N ILE B 453
SHEET 1 K 6 ALA B 652 THR B 653 0
SHEET 2 K 6 HIS B 629 TYR B 634 1 N TYR B 634 O ALA B 652
SHEET 3 K 6 VAL B 602 LEU B 606 1 N ILE B 605 O LEU B 633
SHEET 4 K 6 ALA B 664 VAL B 667 1 O ILE B 666 N ALA B 604
SHEET 5 K 6 ILE B 695 ALA B 698 1 O ALA B 696 N VAL B 667
SHEET 6 K 6 ILE B 718 ALA B 721 1 O VAL B 719 N LEU B 697
SHEET 1 L 2 GLU B 639 THR B 641 0
SHEET 2 L 2 VAL B 647 PRO B 649 -1 O LEU B 648 N VAL B 640
SHEET 1 M11 LEU C 400 ASP C 401 0
SHEET 2 M11 PHE C 277 ILE C 280 -1 N ARG C 278 O ASP C 401
SHEET 3 M11 ALA C 286 PRO C 295 -1 O VAL C 289 N PHE C 277
SHEET 4 M11 GLU C 333 PRO C 342 -1 O GLY C 337 N HIS C 292
SHEET 5 M11 VAL C 367 ARG C 377 -1 O GLN C 368 N PHE C 338
SHEET 6 M11 GLY C 131 PRO C 140 -1 N HIS C 135 O ARG C 377
SHEET 7 M11 THR C 160 SER C 167 -1 O PHE C 166 N SER C 132
SHEET 8 M11 GLY C 184 THR C 191 -1 O LYS C 188 N PHE C 163
SHEET 9 M11 GLY C 194 ASN C 201 -1 O GLY C 200 N PHE C 185
SHEET 10 M11 GLY C 271 PHE C 272 -1 O PHE C 272 N ASN C 201
SHEET 11 M11 ALA C 286 PRO C 295 -1 O TRP C 293 N GLY C 271
SHEET 1 N 6 ALA C 652 THR C 653 0
SHEET 2 N 6 HIS C 629 TYR C 634 1 N TYR C 634 O ALA C 652
SHEET 3 N 6 VAL C 602 LEU C 606 1 N ILE C 605 O LYS C 631
SHEET 4 N 6 ALA C 664 VAL C 667 1 O ILE C 666 N ALA C 604
SHEET 5 N 6 ILE C 695 ALA C 698 1 O ALA C 696 N VAL C 667
SHEET 6 N 6 ILE C 718 ALA C 721 1 O VAL C 719 N LEU C 697
SHEET 1 O 2 GLU C 639 THR C 641 0
SHEET 2 O 2 VAL C 647 PRO C 649 -1 O LEU C 648 N VAL C 640
SHEET 1 P11 LEU D 400 ASP D 401 0
SHEET 2 P11 PHE D 277 ILE D 280 -1 N ARG D 278 O ASP D 401
SHEET 3 P11 ALA D 286 PRO D 295 -1 O VAL D 289 N PHE D 277
SHEET 4 P11 GLU D 333 PRO D 342 -1 O GLN D 339 N ARG D 290
SHEET 5 P11 GLN D 368 ARG D 377 -1 O GLN D 368 N PHE D 338
SHEET 6 P11 GLY D 131 PRO D 140 -1 N HIS D 135 O ARG D 377
SHEET 7 P11 THR D 160 SER D 167 -1 O PHE D 166 N SER D 132
SHEET 8 P11 GLY D 184 THR D 191 -1 O LYS D 188 N PHE D 163
SHEET 9 P11 GLY D 194 ASN D 201 -1 O PHE D 196 N PHE D 189
SHEET 10 P11 GLY D 271 PHE D 272 -1 O PHE D 272 N ASN D 201
SHEET 11 P11 ALA D 286 PRO D 295 -1 O TRP D 293 N GLY D 271
SHEET 1 Q 6 ALA D 652 THR D 653 0
SHEET 2 Q 6 HIS D 629 TYR D 634 1 N TYR D 634 O ALA D 652
SHEET 3 Q 6 VAL D 602 LEU D 606 1 N ILE D 605 O LEU D 633
SHEET 4 Q 6 ALA D 664 VAL D 667 1 O ILE D 666 N ALA D 604
SHEET 5 Q 6 ILE D 695 ALA D 698 1 O ALA D 696 N VAL D 667
SHEET 6 Q 6 ILE D 718 ALA D 721 1 O VAL D 719 N LEU D 697
SHEET 1 R 2 GLU D 639 THR D 641 0
SHEET 2 R 2 VAL D 647 PRO D 649 -1 O LEU D 648 N VAL D 640
LINK C PRO A 668 N OCS A 669 1555 1555 1.38
LINK C OCS A 669 N GLY A 670 1555 1555 1.34
LINK C PRO B 668 N OCS B 669 1555 1555 1.34
LINK C OCS B 669 N GLY B 670 1555 1555 1.34
LINK C PRO C 668 N OCS C 669 1555 1555 1.35
LINK C OCS C 669 N GLY C 670 1555 1555 1.33
LINK C PRO D 668 N OCS D 669 1555 1555 1.35
LINK C OCS D 669 N GLY D 670 1555 1555 1.35
LINK OH TYR A 415 FE HEM A 760 1555 1555 1.93
LINK OH TYR B 415 FE HEM B 760 1555 1555 1.96
LINK OH TYR C 415 FE HEM C 760 1555 1555 1.96
LINK OH TYR D 415 FE HEM D 760 1555 1555 1.93
CISPEP 1 ILE A 229 PRO A 230 0 9.32
CISPEP 2 GLU A 461 PRO A 462 0 1.05
CISPEP 3 TRP A 469 PRO A 470 0 -3.38
CISPEP 4 ILE B 229 PRO B 230 0 6.18
CISPEP 5 GLU B 461 PRO B 462 0 3.27
CISPEP 6 TRP B 469 PRO B 470 0 -4.04
CISPEP 7 ILE C 229 PRO C 230 0 1.37
CISPEP 8 GLU C 461 PRO C 462 0 2.28
CISPEP 9 TRP C 469 PRO C 470 0 -1.37
CISPEP 10 ILE D 229 PRO D 230 0 8.22
CISPEP 11 GLU D 461 PRO D 462 0 3.51
CISPEP 12 TRP D 469 PRO D 470 0 -0.12
SITE 1 AC1 23 ARG A 125 VAL A 127 HIS A 128 ARG A 165
SITE 2 AC1 23 GLY A 184 VAL A 199 GLY A 200 ASN A 201
SITE 3 AC1 23 PHE A 214 ILE A 274 HIS A 275 PHE A 391
SITE 4 AC1 23 LEU A 407 ARG A 411 SER A 414 TYR A 415
SITE 5 AC1 23 THR A 418 GLN A 419 ARG A 422 HOH A 791
SITE 6 AC1 23 HOH A 849 HOH A 879 ASP D 118
SITE 1 AC2 23 ARG B 125 VAL B 127 HIS B 128 ARG B 165
SITE 2 AC2 23 GLY B 184 VAL B 199 GLY B 200 ASN B 201
SITE 3 AC2 23 PHE B 214 ILE B 274 HIS B 275 PHE B 391
SITE 4 AC2 23 LEU B 407 ARG B 411 SER B 414 TYR B 415
SITE 5 AC2 23 THR B 418 GLN B 419 ARG B 422 HOH B 899
SITE 6 AC2 23 HOH B 928 HOH B3210 ASP C 118
SITE 1 AC3 22 ARG C 125 VAL C 127 HIS C 128 ARG C 165
SITE 2 AC3 22 GLY C 184 VAL C 199 GLY C 200 ASN C 201
SITE 3 AC3 22 PHE C 214 ILE C 274 HIS C 275 PHE C 391
SITE 4 AC3 22 LEU C 407 ARG C 411 SER C 414 TYR C 415
SITE 5 AC3 22 THR C 418 GLN C 419 ARG C 422 HOH C 871
SITE 6 AC3 22 HOH C 929 HOH C 964
SITE 1 AC4 22 ARG D 125 VAL D 127 HIS D 128 ARG D 165
SITE 2 AC4 22 GLY D 184 VAL D 199 GLY D 200 ASN D 201
SITE 3 AC4 22 PHE D 206 PHE D 214 HIS D 275 PHE D 391
SITE 4 AC4 22 LEU D 407 ARG D 411 SER D 414 TYR D 415
SITE 5 AC4 22 THR D 418 GLN D 419 ARG D 422 HOH D1295
SITE 6 AC4 22 HOH D1353 HOH D1388
CRYST1 93.560 133.050 122.640 90.00 109.29 90.00 P 1 21 1 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 0.010688 0.000000 0.003741 0.00000
SCALE2 0.000000 0.007516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008639 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
