HEADER OXIDOREDUCTASE 29-JAN-98 1A4E
TITLE CATALASE A FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.11.1.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 CELLULAR_LOCATION: PEROXISOMES
KEYWDS OXIDOREDUCTASE, CATALASE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.MATE
REVDAT 3 02-AUG-23 1A4E 1 REMARK LINK
REVDAT 2 24-FEB-09 1A4E 1 VERSN
REVDAT 1 13-AUG-99 1A4E 0
JRNL AUTH M.J.MATE,M.ZAMOCKY,L.M.NYKYRI,C.HERZOG,P.M.ALZARI,C.BETZEL,
JRNL AUTH 2 F.KOLLER,I.FITA
JRNL TITL STRUCTURE OF CATALASE-A FROM SACCHAROMYCES CEREVISIAE.
JRNL REF J.MOL.BIOL. V. 286 135 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 9931255
JRNL DOI 10.1006/JMBI.1998.2453
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 110950
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11084
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9968
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1106
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15728
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 194
REMARK 3 SOLVENT ATOMS : 957
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.28
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.640 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.550 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.610 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.928
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123230
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33000
REMARK 200 R SYM FOR SHELL (I) : 0.33000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.690
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 7CAT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.65900
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 203.31800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 152.48850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 254.14750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.82950
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 101.65900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 203.31800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 254.14750
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 152.48850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 50.82950
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: 47440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -332.0 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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLY A 454
REMARK 475 LYS A 455
REMARK 475 GLN A 456
REMARK 475 PRO A 457
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 42 NE2 HIS A 42 CD2 -0.069
REMARK 500 HIS A 58 NE2 HIS A 58 CD2 -0.072
REMARK 500 HIS A 70 NE2 HIS A 70 CD2 -0.068
REMARK 500 HIS A 72 NE2 HIS A 72 CD2 -0.071
REMARK 500 HIS A 158 NE2 HIS A 158 CD2 -0.068
REMARK 500 HIS A 161 NE2 HIS A 161 CD2 -0.072
REMARK 500 HIS A 210 NE2 HIS A 210 CD2 -0.067
REMARK 500 HIS A 215 NE2 HIS A 215 CD2 -0.073
REMARK 500 HIS A 227 NE2 HIS A 227 CD2 -0.066
REMARK 500 HIS A 232 NE2 HIS A 232 CD2 -0.069
REMARK 500 HIS A 359 NE2 HIS A 359 CD2 -0.067
REMARK 500 HIS A 368 NE2 HIS A 368 CD2 -0.071
REMARK 500 HIS A 421 NE2 HIS A 421 CD2 -0.070
REMARK 500 HIS A 433 NE2 HIS A 433 CD2 -0.069
REMARK 500 HIS A 470 NE2 HIS A 470 CD2 -0.069
REMARK 500 HIS B 42 NE2 HIS B 42 CD2 -0.068
REMARK 500 HIS B 58 NE2 HIS B 58 CD2 -0.067
REMARK 500 HIS B 70 NE2 HIS B 70 CD2 -0.068
REMARK 500 HIS B 72 NE2 HIS B 72 CD2 -0.068
REMARK 500 HIS B 158 NE2 HIS B 158 CD2 -0.067
REMARK 500 HIS B 161 NE2 HIS B 161 CD2 -0.072
REMARK 500 HIS B 191 NE2 HIS B 191 CD2 -0.068
REMARK 500 HIS B 215 NE2 HIS B 215 CD2 -0.070
REMARK 500 HIS B 227 NE2 HIS B 227 CD2 -0.066
REMARK 500 HIS B 232 NE2 HIS B 232 CD2 -0.069
REMARK 500 HIS B 359 NE2 HIS B 359 CD2 -0.070
REMARK 500 HIS B 368 NE2 HIS B 368 CD2 -0.071
REMARK 500 HIS B 421 NE2 HIS B 421 CD2 -0.070
REMARK 500 HIS B 433 NE2 HIS B 433 CD2 -0.067
REMARK 500 HIS B 470 NE2 HIS B 470 CD2 -0.069
REMARK 500 HIS C 42 NE2 HIS C 42 CD2 -0.068
REMARK 500 HIS C 58 NE2 HIS C 58 CD2 -0.067
REMARK 500 HIS C 70 NE2 HIS C 70 CD2 -0.068
REMARK 500 HIS C 158 NE2 HIS C 158 CD2 -0.074
REMARK 500 HIS C 161 NE2 HIS C 161 CD2 -0.075
REMARK 500 HIS C 191 NE2 HIS C 191 CD2 -0.067
REMARK 500 HIS C 210 NE2 HIS C 210 CD2 -0.070
REMARK 500 HIS C 215 NE2 HIS C 215 CD2 -0.069
REMARK 500 HIS C 227 NE2 HIS C 227 CD2 -0.070
REMARK 500 HIS C 232 NE2 HIS C 232 CD2 -0.069
REMARK 500 HIS C 359 NE2 HIS C 359 CD2 -0.069
REMARK 500 HIS C 368 NE2 HIS C 368 CD2 -0.070
REMARK 500 HIS C 421 NE2 HIS C 421 CD2 -0.071
REMARK 500 HIS C 433 NE2 HIS C 433 CD2 -0.067
REMARK 500 HIS C 470 NE2 HIS C 470 CD2 -0.067
REMARK 500 HIS D 42 NE2 HIS D 42 CD2 -0.068
REMARK 500 HIS D 58 NE2 HIS D 58 CD2 -0.070
REMARK 500 HIS D 70 NE2 HIS D 70 CD2 -0.069
REMARK 500 HIS D 72 NE2 HIS D 72 CD2 -0.068
REMARK 500 HIS D 158 NE2 HIS D 158 CD2 -0.075
REMARK 500
REMARK 500 THIS ENTRY HAS 60 BOND DEVIATIONS.
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 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TRP A 140 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 140 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP A 178 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP A 178 CE2 - CD2 - CG ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP A 178 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 219 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP A 219 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 226 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 226 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 274 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 274 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 300 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 300 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 425 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 425 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 434 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 434 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 CYS A 475 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 107 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 107 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 125 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 125 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TRP B 140 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP B 140 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR B 142 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 MET B 176 CA - CB - CG ANGL. DEV. = 10.7 DEGREES
REMARK 500 TRP B 178 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 178 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 219 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP B 219 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP B 226 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP B 226 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP B 274 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP B 274 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 300 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP B 300 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP B 425 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 425 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP B 434 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP B 434 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 107 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 125 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 125 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TRP C 140 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 95 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 PRO A 69 -153.97 -90.78
REMARK 500 VAL A 111 -58.76 -120.83
REMARK 500 LYS A 164 -124.14 -92.25
REMARK 500 TYR A 339 -2.55 73.13
REMARK 500 SER A 378 83.17 -152.28
REMARK 500 ASP A 387 -148.38 59.02
REMARK 500 GLN A 422 -137.40 -99.86
REMARK 500 PRO B 69 -154.88 -89.98
REMARK 500 PHE B 127 82.25 -150.06
REMARK 500 LYS B 164 -129.57 -97.45
REMARK 500 ASN B 254 88.28 -151.62
REMARK 500 SER B 378 83.49 -158.65
REMARK 500 ASP B 387 -145.94 60.12
REMARK 500 PHE B 396 18.90 58.47
REMARK 500 GLN B 422 -135.51 -99.66
REMARK 500 PRO C 69 -154.45 -91.63
REMARK 500 THR C 110 -168.56 -100.15
REMARK 500 VAL C 147 -168.02 -120.58
REMARK 500 LYS C 164 -121.70 -99.89
REMARK 500 SER C 208 53.57 -118.80
REMARK 500 VAL C 310 -55.89 -122.31
REMARK 500 SER C 378 81.80 -156.83
REMARK 500 ASP C 387 -147.73 57.05
REMARK 500 PHE C 396 19.52 55.03
REMARK 500 ILE C 418 -68.18 -93.78
REMARK 500 GLN C 422 -138.45 -107.06
REMARK 500 PRO D 69 -153.02 -91.93
REMARK 500 VAL D 147 -165.40 -118.65
REMARK 500 LYS D 164 -127.47 -96.99
REMARK 500 SER D 378 76.61 -157.20
REMARK 500 ASP D 387 -149.27 56.71
REMARK 500 GLN D 422 -132.91 -105.84
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 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 355 OH
REMARK 620 2 HEM A 503 NA 92.6
REMARK 620 3 HEM A 503 NB 90.8 89.9
REMARK 620 4 HEM A 503 NC 85.3 177.9 89.6
REMARK 620 5 HEM A 503 ND 85.6 90.0 176.4 90.3
REMARK 620 6 AZI A 504 N1 171.6 95.3 92.1 86.8 91.5
REMARK 620 7 AZI A 504 N2 149.6 114.9 101.4 67.2 81.9 22.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 355 OH
REMARK 620 2 HEM B 503 NA 91.2
REMARK 620 3 HEM B 503 NB 93.2 89.6
REMARK 620 4 HEM B 503 NC 87.3 178.4 89.9
REMARK 620 5 HEM B 503 ND 83.2 90.5 176.5 89.9
REMARK 620 6 AZI B 504 N1 176.3 88.0 90.4 93.5 93.2
REMARK 620 7 AZI B 504 N2 153.8 110.8 100.8 70.8 82.5 25.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 355 OH
REMARK 620 2 HEM C 503 NA 91.2
REMARK 620 3 HEM C 503 NB 90.1 89.6
REMARK 620 4 HEM C 503 NC 86.9 178.1 90.0
REMARK 620 5 HEM C 503 ND 87.0 90.0 177.1 90.3
REMARK 620 6 AZI C 504 N1 176.0 91.6 92.7 90.3 90.1
REMARK 620 7 AZI C 504 N2 154.1 112.3 100.5 69.6 82.3 22.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 355 OH
REMARK 620 2 HEM D 503 NA 88.1
REMARK 620 3 HEM D 503 NB 95.2 90.1
REMARK 620 4 HEM D 503 NC 90.0 178.0 89.6
REMARK 620 5 HEM D 503 ND 81.8 90.2 176.9 90.0
REMARK 620 6 AZI D 504 N1 171.4 88.8 92.9 93.2 90.2
REMARK 620 7 AZI D 504 N2 152.6 113.3 101.5 68.7 81.2 26.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 503
DBREF 1A4E A 15 502 UNP P15202 CATA_YEAST 15 502
DBREF 1A4E B 15 502 UNP P15202 CATA_YEAST 15 502
DBREF 1A4E C 15 502 UNP P15202 CATA_YEAST 15 502
DBREF 1A4E D 15 502 UNP P15202 CATA_YEAST 15 502
SEQRES 1 A 488 ASP VAL ARG GLU ASP ARG VAL VAL THR ASN SER THR GLY
SEQRES 2 A 488 ASN PRO ILE ASN GLU PRO PHE VAL THR GLN ARG ILE GLY
SEQRES 3 A 488 GLU HIS GLY PRO LEU LEU LEU GLN ASP TYR ASN LEU ILE
SEQRES 4 A 488 ASP SER LEU ALA HIS PHE ASN ARG GLU ASN ILE PRO GLN
SEQRES 5 A 488 ARG ASN PRO HIS ALA HIS GLY SER GLY ALA PHE GLY TYR
SEQRES 6 A 488 PHE GLU VAL THR ASP ASP ILE THR ASP ILE CYS GLY SER
SEQRES 7 A 488 ALA MET PHE SER LYS ILE GLY LYS ARG THR LYS CYS LEU
SEQRES 8 A 488 THR ARG PHE SER THR VAL GLY GLY ASP LYS GLY SER ALA
SEQRES 9 A 488 ASP THR VAL ARG ASP PRO ARG GLY PHE ALA THR LYS PHE
SEQRES 10 A 488 TYR THR GLU GLU GLY ASN LEU ASP TRP VAL TYR ASN ASN
SEQRES 11 A 488 THR PRO VAL PHE PHE ILE ARG ASP PRO SER LYS PHE PRO
SEQRES 12 A 488 HIS PHE ILE HIS THR GLN LYS ARG ASN PRO GLN THR ASN
SEQRES 13 A 488 LEU ARG ASP ALA ASP MET PHE TRP ASP PHE LEU THR THR
SEQRES 14 A 488 PRO GLU ASN GLN VAL ALA ILE HIS GLN VAL MET ILE LEU
SEQRES 15 A 488 PHE SER ASP ARG GLY THR PRO ALA ASN TYR ARG SER MET
SEQRES 16 A 488 HIS GLY TYR SER GLY HIS THR TYR LYS TRP SER ASN LYS
SEQRES 17 A 488 ASN GLY ASP TRP HIS TYR VAL GLN VAL HIS ILE LYS THR
SEQRES 18 A 488 ASP GLN GLY ILE LYS ASN LEU THR ILE GLU GLU ALA THR
SEQRES 19 A 488 LYS ILE ALA GLY SER ASN PRO ASP TYR CYS GLN GLN ASP
SEQRES 20 A 488 LEU PHE GLU ALA ILE GLN ASN GLY ASN TYR PRO SER TRP
SEQRES 21 A 488 THR VAL TYR ILE GLN THR MET THR GLU ARG ASP ALA LYS
SEQRES 22 A 488 LYS LEU PRO PHE SER VAL PHE ASP LEU THR LYS VAL TRP
SEQRES 23 A 488 PRO GLN GLY GLN PHE PRO LEU ARG ARG VAL GLY LYS ILE
SEQRES 24 A 488 VAL LEU ASN GLU ASN PRO LEU ASN PHE PHE ALA GLN VAL
SEQRES 25 A 488 GLU GLN ALA ALA PHE ALA PRO SER THR THR VAL PRO TYR
SEQRES 26 A 488 GLN GLU ALA SER ALA ASP PRO VAL LEU GLN ALA ARG LEU
SEQRES 27 A 488 PHE SER TYR ALA ASP ALA HIS ARG TYR ARG LEU GLY PRO
SEQRES 28 A 488 ASN PHE HIS GLN ILE PRO VAL ASN CYS PRO TYR ALA SER
SEQRES 29 A 488 LYS PHE PHE ASN PRO ALA ILE ARG ASP GLY PRO MET ASN
SEQRES 30 A 488 VAL ASN GLY ASN PHE GLY SER GLU PRO THR TYR LEU ALA
SEQRES 31 A 488 ASN ASP LYS SER TYR THR TYR ILE GLN GLN ASP ARG PRO
SEQRES 32 A 488 ILE GLN GLN HIS GLN GLU VAL TRP ASN GLY PRO ALA ILE
SEQRES 33 A 488 PRO TYR HIS TRP ALA THR SER PRO GLY ASP VAL ASP PHE
SEQRES 34 A 488 VAL GLN ALA ARG ASN LEU TYR ARG VAL LEU GLY LYS GLN
SEQRES 35 A 488 PRO GLY GLN GLN LYS ASN LEU ALA TYR ASN ILE GLY ILE
SEQRES 36 A 488 HIS VAL GLU GLY ALA CYS PRO GLN ILE GLN GLN ARG VAL
SEQRES 37 A 488 TYR ASP MET PHE ALA ARG VAL ASP LYS GLY LEU SER GLU
SEQRES 38 A 488 ALA ILE LYS LYS VAL ALA GLU
SEQRES 1 B 488 ASP VAL ARG GLU ASP ARG VAL VAL THR ASN SER THR GLY
SEQRES 2 B 488 ASN PRO ILE ASN GLU PRO PHE VAL THR GLN ARG ILE GLY
SEQRES 3 B 488 GLU HIS GLY PRO LEU LEU LEU GLN ASP TYR ASN LEU ILE
SEQRES 4 B 488 ASP SER LEU ALA HIS PHE ASN ARG GLU ASN ILE PRO GLN
SEQRES 5 B 488 ARG ASN PRO HIS ALA HIS GLY SER GLY ALA PHE GLY TYR
SEQRES 6 B 488 PHE GLU VAL THR ASP ASP ILE THR ASP ILE CYS GLY SER
SEQRES 7 B 488 ALA MET PHE SER LYS ILE GLY LYS ARG THR LYS CYS LEU
SEQRES 8 B 488 THR ARG PHE SER THR VAL GLY GLY ASP LYS GLY SER ALA
SEQRES 9 B 488 ASP THR VAL ARG ASP PRO ARG GLY PHE ALA THR LYS PHE
SEQRES 10 B 488 TYR THR GLU GLU GLY ASN LEU ASP TRP VAL TYR ASN ASN
SEQRES 11 B 488 THR PRO VAL PHE PHE ILE ARG ASP PRO SER LYS PHE PRO
SEQRES 12 B 488 HIS PHE ILE HIS THR GLN LYS ARG ASN PRO GLN THR ASN
SEQRES 13 B 488 LEU ARG ASP ALA ASP MET PHE TRP ASP PHE LEU THR THR
SEQRES 14 B 488 PRO GLU ASN GLN VAL ALA ILE HIS GLN VAL MET ILE LEU
SEQRES 15 B 488 PHE SER ASP ARG GLY THR PRO ALA ASN TYR ARG SER MET
SEQRES 16 B 488 HIS GLY TYR SER GLY HIS THR TYR LYS TRP SER ASN LYS
SEQRES 17 B 488 ASN GLY ASP TRP HIS TYR VAL GLN VAL HIS ILE LYS THR
SEQRES 18 B 488 ASP GLN GLY ILE LYS ASN LEU THR ILE GLU GLU ALA THR
SEQRES 19 B 488 LYS ILE ALA GLY SER ASN PRO ASP TYR CYS GLN GLN ASP
SEQRES 20 B 488 LEU PHE GLU ALA ILE GLN ASN GLY ASN TYR PRO SER TRP
SEQRES 21 B 488 THR VAL TYR ILE GLN THR MET THR GLU ARG ASP ALA LYS
SEQRES 22 B 488 LYS LEU PRO PHE SER VAL PHE ASP LEU THR LYS VAL TRP
SEQRES 23 B 488 PRO GLN GLY GLN PHE PRO LEU ARG ARG VAL GLY LYS ILE
SEQRES 24 B 488 VAL LEU ASN GLU ASN PRO LEU ASN PHE PHE ALA GLN VAL
SEQRES 25 B 488 GLU GLN ALA ALA PHE ALA PRO SER THR THR VAL PRO TYR
SEQRES 26 B 488 GLN GLU ALA SER ALA ASP PRO VAL LEU GLN ALA ARG LEU
SEQRES 27 B 488 PHE SER TYR ALA ASP ALA HIS ARG TYR ARG LEU GLY PRO
SEQRES 28 B 488 ASN PHE HIS GLN ILE PRO VAL ASN CYS PRO TYR ALA SER
SEQRES 29 B 488 LYS PHE PHE ASN PRO ALA ILE ARG ASP GLY PRO MET ASN
SEQRES 30 B 488 VAL ASN GLY ASN PHE GLY SER GLU PRO THR TYR LEU ALA
SEQRES 31 B 488 ASN ASP LYS SER TYR THR TYR ILE GLN GLN ASP ARG PRO
SEQRES 32 B 488 ILE GLN GLN HIS GLN GLU VAL TRP ASN GLY PRO ALA ILE
SEQRES 33 B 488 PRO TYR HIS TRP ALA THR SER PRO GLY ASP VAL ASP PHE
SEQRES 34 B 488 VAL GLN ALA ARG ASN LEU TYR ARG VAL LEU GLY LYS GLN
SEQRES 35 B 488 PRO GLY GLN GLN LYS ASN LEU ALA TYR ASN ILE GLY ILE
SEQRES 36 B 488 HIS VAL GLU GLY ALA CYS PRO GLN ILE GLN GLN ARG VAL
SEQRES 37 B 488 TYR ASP MET PHE ALA ARG VAL ASP LYS GLY LEU SER GLU
SEQRES 38 B 488 ALA ILE LYS LYS VAL ALA GLU
SEQRES 1 C 488 ASP VAL ARG GLU ASP ARG VAL VAL THR ASN SER THR GLY
SEQRES 2 C 488 ASN PRO ILE ASN GLU PRO PHE VAL THR GLN ARG ILE GLY
SEQRES 3 C 488 GLU HIS GLY PRO LEU LEU LEU GLN ASP TYR ASN LEU ILE
SEQRES 4 C 488 ASP SER LEU ALA HIS PHE ASN ARG GLU ASN ILE PRO GLN
SEQRES 5 C 488 ARG ASN PRO HIS ALA HIS GLY SER GLY ALA PHE GLY TYR
SEQRES 6 C 488 PHE GLU VAL THR ASP ASP ILE THR ASP ILE CYS GLY SER
SEQRES 7 C 488 ALA MET PHE SER LYS ILE GLY LYS ARG THR LYS CYS LEU
SEQRES 8 C 488 THR ARG PHE SER THR VAL GLY GLY ASP LYS GLY SER ALA
SEQRES 9 C 488 ASP THR VAL ARG ASP PRO ARG GLY PHE ALA THR LYS PHE
SEQRES 10 C 488 TYR THR GLU GLU GLY ASN LEU ASP TRP VAL TYR ASN ASN
SEQRES 11 C 488 THR PRO VAL PHE PHE ILE ARG ASP PRO SER LYS PHE PRO
SEQRES 12 C 488 HIS PHE ILE HIS THR GLN LYS ARG ASN PRO GLN THR ASN
SEQRES 13 C 488 LEU ARG ASP ALA ASP MET PHE TRP ASP PHE LEU THR THR
SEQRES 14 C 488 PRO GLU ASN GLN VAL ALA ILE HIS GLN VAL MET ILE LEU
SEQRES 15 C 488 PHE SER ASP ARG GLY THR PRO ALA ASN TYR ARG SER MET
SEQRES 16 C 488 HIS GLY TYR SER GLY HIS THR TYR LYS TRP SER ASN LYS
SEQRES 17 C 488 ASN GLY ASP TRP HIS TYR VAL GLN VAL HIS ILE LYS THR
SEQRES 18 C 488 ASP GLN GLY ILE LYS ASN LEU THR ILE GLU GLU ALA THR
SEQRES 19 C 488 LYS ILE ALA GLY SER ASN PRO ASP TYR CYS GLN GLN ASP
SEQRES 20 C 488 LEU PHE GLU ALA ILE GLN ASN GLY ASN TYR PRO SER TRP
SEQRES 21 C 488 THR VAL TYR ILE GLN THR MET THR GLU ARG ASP ALA LYS
SEQRES 22 C 488 LYS LEU PRO PHE SER VAL PHE ASP LEU THR LYS VAL TRP
SEQRES 23 C 488 PRO GLN GLY GLN PHE PRO LEU ARG ARG VAL GLY LYS ILE
SEQRES 24 C 488 VAL LEU ASN GLU ASN PRO LEU ASN PHE PHE ALA GLN VAL
SEQRES 25 C 488 GLU GLN ALA ALA PHE ALA PRO SER THR THR VAL PRO TYR
SEQRES 26 C 488 GLN GLU ALA SER ALA ASP PRO VAL LEU GLN ALA ARG LEU
SEQRES 27 C 488 PHE SER TYR ALA ASP ALA HIS ARG TYR ARG LEU GLY PRO
SEQRES 28 C 488 ASN PHE HIS GLN ILE PRO VAL ASN CYS PRO TYR ALA SER
SEQRES 29 C 488 LYS PHE PHE ASN PRO ALA ILE ARG ASP GLY PRO MET ASN
SEQRES 30 C 488 VAL ASN GLY ASN PHE GLY SER GLU PRO THR TYR LEU ALA
SEQRES 31 C 488 ASN ASP LYS SER TYR THR TYR ILE GLN GLN ASP ARG PRO
SEQRES 32 C 488 ILE GLN GLN HIS GLN GLU VAL TRP ASN GLY PRO ALA ILE
SEQRES 33 C 488 PRO TYR HIS TRP ALA THR SER PRO GLY ASP VAL ASP PHE
SEQRES 34 C 488 VAL GLN ALA ARG ASN LEU TYR ARG VAL LEU GLY LYS GLN
SEQRES 35 C 488 PRO GLY GLN GLN LYS ASN LEU ALA TYR ASN ILE GLY ILE
SEQRES 36 C 488 HIS VAL GLU GLY ALA CYS PRO GLN ILE GLN GLN ARG VAL
SEQRES 37 C 488 TYR ASP MET PHE ALA ARG VAL ASP LYS GLY LEU SER GLU
SEQRES 38 C 488 ALA ILE LYS LYS VAL ALA GLU
SEQRES 1 D 488 ASP VAL ARG GLU ASP ARG VAL VAL THR ASN SER THR GLY
SEQRES 2 D 488 ASN PRO ILE ASN GLU PRO PHE VAL THR GLN ARG ILE GLY
SEQRES 3 D 488 GLU HIS GLY PRO LEU LEU LEU GLN ASP TYR ASN LEU ILE
SEQRES 4 D 488 ASP SER LEU ALA HIS PHE ASN ARG GLU ASN ILE PRO GLN
SEQRES 5 D 488 ARG ASN PRO HIS ALA HIS GLY SER GLY ALA PHE GLY TYR
SEQRES 6 D 488 PHE GLU VAL THR ASP ASP ILE THR ASP ILE CYS GLY SER
SEQRES 7 D 488 ALA MET PHE SER LYS ILE GLY LYS ARG THR LYS CYS LEU
SEQRES 8 D 488 THR ARG PHE SER THR VAL GLY GLY ASP LYS GLY SER ALA
SEQRES 9 D 488 ASP THR VAL ARG ASP PRO ARG GLY PHE ALA THR LYS PHE
SEQRES 10 D 488 TYR THR GLU GLU GLY ASN LEU ASP TRP VAL TYR ASN ASN
SEQRES 11 D 488 THR PRO VAL PHE PHE ILE ARG ASP PRO SER LYS PHE PRO
SEQRES 12 D 488 HIS PHE ILE HIS THR GLN LYS ARG ASN PRO GLN THR ASN
SEQRES 13 D 488 LEU ARG ASP ALA ASP MET PHE TRP ASP PHE LEU THR THR
SEQRES 14 D 488 PRO GLU ASN GLN VAL ALA ILE HIS GLN VAL MET ILE LEU
SEQRES 15 D 488 PHE SER ASP ARG GLY THR PRO ALA ASN TYR ARG SER MET
SEQRES 16 D 488 HIS GLY TYR SER GLY HIS THR TYR LYS TRP SER ASN LYS
SEQRES 17 D 488 ASN GLY ASP TRP HIS TYR VAL GLN VAL HIS ILE LYS THR
SEQRES 18 D 488 ASP GLN GLY ILE LYS ASN LEU THR ILE GLU GLU ALA THR
SEQRES 19 D 488 LYS ILE ALA GLY SER ASN PRO ASP TYR CYS GLN GLN ASP
SEQRES 20 D 488 LEU PHE GLU ALA ILE GLN ASN GLY ASN TYR PRO SER TRP
SEQRES 21 D 488 THR VAL TYR ILE GLN THR MET THR GLU ARG ASP ALA LYS
SEQRES 22 D 488 LYS LEU PRO PHE SER VAL PHE ASP LEU THR LYS VAL TRP
SEQRES 23 D 488 PRO GLN GLY GLN PHE PRO LEU ARG ARG VAL GLY LYS ILE
SEQRES 24 D 488 VAL LEU ASN GLU ASN PRO LEU ASN PHE PHE ALA GLN VAL
SEQRES 25 D 488 GLU GLN ALA ALA PHE ALA PRO SER THR THR VAL PRO TYR
SEQRES 26 D 488 GLN GLU ALA SER ALA ASP PRO VAL LEU GLN ALA ARG LEU
SEQRES 27 D 488 PHE SER TYR ALA ASP ALA HIS ARG TYR ARG LEU GLY PRO
SEQRES 28 D 488 ASN PHE HIS GLN ILE PRO VAL ASN CYS PRO TYR ALA SER
SEQRES 29 D 488 LYS PHE PHE ASN PRO ALA ILE ARG ASP GLY PRO MET ASN
SEQRES 30 D 488 VAL ASN GLY ASN PHE GLY SER GLU PRO THR TYR LEU ALA
SEQRES 31 D 488 ASN ASP LYS SER TYR THR TYR ILE GLN GLN ASP ARG PRO
SEQRES 32 D 488 ILE GLN GLN HIS GLN GLU VAL TRP ASN GLY PRO ALA ILE
SEQRES 33 D 488 PRO TYR HIS TRP ALA THR SER PRO GLY ASP VAL ASP PHE
SEQRES 34 D 488 VAL GLN ALA ARG ASN LEU TYR ARG VAL LEU GLY LYS GLN
SEQRES 35 D 488 PRO GLY GLN GLN LYS ASN LEU ALA TYR ASN ILE GLY ILE
SEQRES 36 D 488 HIS VAL GLU GLY ALA CYS PRO GLN ILE GLN GLN ARG VAL
SEQRES 37 D 488 TYR ASP MET PHE ALA ARG VAL ASP LYS GLY LEU SER GLU
SEQRES 38 D 488 ALA ILE LYS LYS VAL ALA GLU
HET AZI A 504 3
HET SO4 A 1 5
HET HEM A 503 43
HET AZI B 504 3
HET HEM B 503 43
HET AZI C 504 3
HET HEM C 503 43
HET AZI D 504 3
HET SO4 D 2 5
HET HEM D 503 43
HETNAM AZI AZIDE ION
HETNAM SO4 SULFATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 AZI 4(N3 1-)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 7 HEM 4(C34 H32 FE N4 O4)
FORMUL 15 HOH *957(H2 O)
HELIX 1 1 TYR A 50 ARG A 61 1 12
HELIX 2 2 ALA A 93 PHE A 95 5 3
HELIX 3 3 PRO A 153 GLN A 163 5 11
HELIX 4 4 ALA A 174 THR A 182 1 9
HELIX 5 5 PRO A 184 PHE A 197 5 14
HELIX 6 6 ASP A 199 GLY A 201 5 3
HELIX 7 7 TYR A 206 SER A 208 5 3
HELIX 8 8 ILE A 244 SER A 253 1 10
HELIX 9 9 TYR A 257 GLN A 267 1 11
HELIX 10 10 GLU A 283 LYS A 288 1 6
HELIX 11 11 PHE A 322 GLN A 325 1 4
HELIX 12 12 PRO A 346 ARG A 362 1 17
HELIX 13 13 PHE A 367 GLN A 369 5 3
HELIX 14 14 PRO A 371 ASN A 373 5 3
HELIX 15 15 VAL A 441 GLY A 454 1 14
HELIX 16 16 GLN A 459 GLY A 473 1 15
HELIX 17 17 PRO A 476 ALA A 487 1 12
HELIX 18 18 LYS A 491 VAL A 500 1 10
HELIX 19 19 TYR B 50 ARG B 61 1 12
HELIX 20 20 ALA B 93 PHE B 95 5 3
HELIX 21 21 PRO B 153 GLN B 163 5 11
HELIX 22 22 ALA B 174 THR B 182 1 9
HELIX 23 23 PRO B 184 LEU B 196 5 13
HELIX 24 24 ASP B 199 GLY B 201 5 3
HELIX 25 25 TYR B 206 SER B 208 5 3
HELIX 26 26 ILE B 244 SER B 253 1 10
HELIX 27 27 TYR B 257 GLN B 267 1 11
HELIX 28 28 GLU B 283 LYS B 288 1 6
HELIX 29 29 PHE B 322 GLN B 325 1 4
HELIX 30 30 PRO B 346 ARG B 362 1 17
HELIX 31 31 PHE B 367 GLN B 369 5 3
HELIX 32 32 PRO B 371 ASN B 373 5 3
HELIX 33 33 VAL B 444 LYS B 455 1 12
HELIX 34 34 GLN B 459 GLY B 473 1 15
HELIX 35 35 PRO B 476 ALA B 487 1 12
HELIX 36 36 LYS B 491 VAL B 500 1 10
HELIX 37 37 TYR C 50 ARG C 61 1 12
HELIX 38 38 ALA C 93 PHE C 95 5 3
HELIX 39 39 PRO C 153 GLN C 163 5 11
HELIX 40 40 ALA C 174 THR C 182 1 9
HELIX 41 41 PRO C 184 LEU C 196 5 13
HELIX 42 42 ASP C 199 GLY C 201 5 3
HELIX 43 43 TYR C 206 SER C 208 5 3
HELIX 44 44 ILE C 244 SER C 253 1 10
HELIX 45 45 TYR C 257 GLN C 267 1 11
HELIX 46 46 GLU C 283 LYS C 288 1 6
HELIX 47 47 PHE C 322 GLN C 325 1 4
HELIX 48 48 PRO C 346 ARG C 362 1 17
HELIX 49 49 PHE C 367 GLN C 369 5 3
HELIX 50 50 PRO C 371 ASN C 373 5 3
HELIX 51 51 VAL C 444 GLY C 454 1 11
HELIX 52 52 GLN C 459 GLY C 473 1 15
HELIX 53 53 PRO C 476 ALA C 487 1 12
HELIX 54 54 LYS C 491 VAL C 500 1 10
HELIX 55 55 TYR D 50 ARG D 61 1 12
HELIX 56 56 ALA D 93 PHE D 95 5 3
HELIX 57 57 PRO D 153 GLN D 163 5 11
HELIX 58 58 ALA D 174 THR D 182 1 9
HELIX 59 59 PRO D 184 LEU D 196 5 13
HELIX 60 60 ASP D 199 GLY D 201 5 3
HELIX 61 61 TYR D 206 SER D 208 5 3
HELIX 62 62 ILE D 244 SER D 253 1 10
HELIX 63 63 TYR D 257 GLN D 267 1 11
HELIX 64 64 GLU D 283 LYS D 287 1 5
HELIX 65 65 PHE D 322 GLN D 325 1 4
HELIX 66 66 PRO D 346 ARG D 362 1 17
HELIX 67 67 PHE D 367 GLN D 369 5 3
HELIX 68 68 PRO D 371 ASN D 373 5 3
HELIX 69 69 VAL D 444 LYS D 455 1 12
HELIX 70 70 GLN D 459 GLY D 473 1 15
HELIX 71 71 PRO D 476 ALA D 487 1 12
HELIX 72 72 LYS D 491 VAL D 500 1 10
SHEET 1 A 9 GLY A 136 ASN A 143 0
SHEET 2 A 9 GLY A 126 THR A 133 -1 N THR A 133 O GLY A 136
SHEET 3 A 9 ARG A 101 SER A 109 -1 N SER A 109 O GLY A 126
SHEET 4 A 9 GLY A 73 VAL A 82 -1 N PHE A 80 O THR A 102
SHEET 5 A 9 ARG A 308 GLU A 317 -1 N GLU A 317 O PHE A 77
SHEET 6 A 9 PRO A 272 MET A 281 -1 N ILE A 278 O ARG A 308
SHEET 7 A 9 TRP A 226 THR A 235 -1 N LYS A 234 O THR A 275
SHEET 8 A 9 TYR A 217 SER A 220 -1 N TRP A 219 O HIS A 227
SHEET 9 A 9 GLN A 340 ALA A 342 -1 N GLU A 341 O LYS A 218
SHEET 1 B 9 GLY B 136 ASN B 143 0
SHEET 2 B 9 GLY B 126 THR B 133 -1 N THR B 133 O GLY B 136
SHEET 3 B 9 ARG B 101 SER B 109 -1 N SER B 109 O GLY B 126
SHEET 4 B 9 GLY B 73 VAL B 82 -1 N PHE B 80 O THR B 102
SHEET 5 B 9 ARG B 308 GLU B 317 -1 N GLU B 317 O PHE B 77
SHEET 6 B 9 PRO B 272 MET B 281 -1 N ILE B 278 O ARG B 308
SHEET 7 B 9 TRP B 226 THR B 235 -1 N LYS B 234 O THR B 275
SHEET 8 B 9 TYR B 217 SER B 220 -1 N TRP B 219 O HIS B 227
SHEET 9 B 9 GLN B 340 ALA B 342 -1 N GLU B 341 O LYS B 218
SHEET 1 C 9 GLY C 136 ASN C 143 0
SHEET 2 C 9 GLY C 126 THR C 133 -1 N THR C 133 O GLY C 136
SHEET 3 C 9 ARG C 101 SER C 109 -1 N SER C 109 O GLY C 126
SHEET 4 C 9 GLY C 73 VAL C 82 -1 N PHE C 80 O THR C 102
SHEET 5 C 9 ARG C 308 GLU C 317 -1 N GLU C 317 O PHE C 77
SHEET 6 C 9 SER C 273 MET C 281 -1 N ILE C 278 O ARG C 308
SHEET 7 C 9 TRP C 226 THR C 235 -1 N LYS C 234 O THR C 275
SHEET 8 C 9 TYR C 217 SER C 220 -1 N TRP C 219 O HIS C 227
SHEET 9 C 9 GLN C 340 ALA C 342 -1 N GLU C 341 O LYS C 218
SHEET 1 D 9 GLY D 136 ASN D 143 0
SHEET 2 D 9 GLY D 126 THR D 133 -1 N THR D 133 O GLY D 136
SHEET 3 D 9 ARG D 101 SER D 109 -1 N SER D 109 O GLY D 126
SHEET 4 D 9 GLY D 73 VAL D 82 -1 N PHE D 80 O THR D 102
SHEET 5 D 9 ARG D 308 GLU D 317 -1 N GLU D 317 O PHE D 77
SHEET 6 D 9 SER D 273 MET D 281 -1 N ILE D 278 O ARG D 308
SHEET 7 D 9 TRP D 226 THR D 235 -1 N LYS D 234 O THR D 275
SHEET 8 D 9 TYR D 217 SER D 220 -1 N TRP D 219 O HIS D 227
SHEET 9 D 9 GLN D 340 ALA D 342 -1 N GLU D 341 O LYS D 218
LINK OH TYR A 355 FE HEM A 503 1555 1555 1.89
LINK FE HEM A 503 N1 AZI A 504 1555 1555 2.10
LINK FE HEM A 503 N2 AZI A 504 1555 1555 3.10
LINK OH TYR B 355 FE HEM B 503 1555 1555 1.87
LINK FE HEM B 503 N1 AZI B 504 1555 1555 2.09
LINK FE HEM B 503 N2 AZI B 504 1555 1555 2.97
LINK OH TYR C 355 FE HEM C 503 1555 1555 1.88
LINK FE HEM C 503 N1 AZI C 504 1555 1555 2.11
LINK FE HEM C 503 N2 AZI C 504 1555 1555 3.10
LINK OH TYR D 355 FE HEM D 503 1555 1555 1.91
LINK FE HEM D 503 N1 AZI D 504 1555 1555 2.10
LINK FE HEM D 503 N2 AZI D 504 1555 1555 2.93
CISPEP 1 ASN A 68 PRO A 69 0 -5.32
CISPEP 2 ASN B 68 PRO B 69 0 -5.96
CISPEP 3 ASN C 68 PRO C 69 0 -7.05
CISPEP 4 ASN D 68 PRO D 69 0 -6.81
SITE 1 AC1 5 HIS A 70 ASN A 143 PHE A 148 PHE A 156
SITE 2 AC1 5 HEM A 503
SITE 1 AC2 6 PRO B 69 HIS B 70 ASN B 143 PHE B 148
SITE 2 AC2 6 PHE B 156 HEM B 503
SITE 1 AC3 6 PRO C 69 HIS C 70 ASN C 143 PHE C 148
SITE 2 AC3 6 PHE C 156 HEM C 503
SITE 1 AC4 6 PRO D 69 HIS D 70 ASN D 143 PHE D 148
SITE 2 AC4 6 PHE D 156 HEM D 503
SITE 1 AC5 8 ARG A 61 ARG B 360 TYR B 361 HOH B 608
SITE 2 AC5 8 ARG C 61 ARG D 360 TYR D 361 HOH D 601
SITE 1 AC6 8 ARG A 360 TYR A 361 HOH A 604 ARG B 61
SITE 2 AC6 8 ARG C 360 TYR C 361 HOH C 606 ARG D 61
SITE 1 AC7 24 ARG A 67 ASN A 68 PRO A 69 HIS A 70
SITE 2 AC7 24 ARG A 107 GLY A 126 VAL A 141 TYR A 142
SITE 3 AC7 24 ASN A 143 PHE A 156 SER A 213 PHE A 331
SITE 4 AC7 24 VAL A 347 ARG A 351 SER A 354 TYR A 355
SITE 5 AC7 24 ALA A 358 HIS A 359 ARG A 362 AZI A 504
SITE 6 AC7 24 HOH A 506 HOH A 509 HOH A 514 ASN D 60
SITE 1 AC8 23 ARG B 67 ASN B 68 HIS B 70 ARG B 107
SITE 2 AC8 23 GLY B 126 VAL B 141 TYR B 142 ASN B 143
SITE 3 AC8 23 PHE B 156 SER B 213 HIS B 215 PHE B 331
SITE 4 AC8 23 VAL B 347 ARG B 351 SER B 354 TYR B 355
SITE 5 AC8 23 HIS B 359 ARG B 362 AZI B 504 HOH B 511
SITE 6 AC8 23 HOH B 515 HOH B 523 ASN C 60
SITE 1 AC9 24 ASN B 60 ARG C 67 ASN C 68 HIS C 70
SITE 2 AC9 24 ARG C 107 GLY C 126 VAL C 141 TYR C 142
SITE 3 AC9 24 ASN C 143 PHE C 148 PHE C 156 SER C 213
SITE 4 AC9 24 PHE C 331 VAL C 347 ARG C 351 SER C 354
SITE 5 AC9 24 TYR C 355 ALA C 358 HIS C 359 ARG C 362
SITE 6 AC9 24 AZI C 504 HOH C 510 HOH C 515 HOH C 521
SITE 1 BC1 24 ASN A 60 ARG D 67 ASN D 68 HIS D 70
SITE 2 BC1 24 ARG D 107 GLY D 126 VAL D 141 TYR D 142
SITE 3 BC1 24 ASN D 143 PHE D 148 PHE D 156 SER D 213
SITE 4 BC1 24 PHE D 331 VAL D 347 ARG D 351 SER D 354
SITE 5 BC1 24 TYR D 355 ALA D 358 HIS D 359 ARG D 362
SITE 6 BC1 24 AZI D 504 HOH D 517 HOH D 521 HOH D 526
CRYST1 184.172 184.172 304.977 90.00 90.00 120.00 P 61 2 2 48
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 0.005430 0.003135 0.000000 0.00000
SCALE2 0.000000 0.006270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003279 0.00000
MTRIX1 1 -0.430200 -0.336200 -0.837800 206.62730 1
MTRIX2 1 -0.343800 -0.797100 0.496400 63.01170 1
MTRIX3 1 -0.834700 0.501500 0.227300 115.19950 1
MTRIX1 2 -0.999800 0.020000 -0.008100 238.11700 1
MTRIX2 2 0.020100 0.720800 -0.692900 27.64320 1
MTRIX3 2 -0.008000 -0.692900 -0.721000 75.69760 1
MTRIX1 3 0.429000 0.322300 0.843800 31.94150 1
MTRIX2 3 0.321200 -0.927500 0.191000 -2.89870 1
MTRIX3 3 0.844300 0.189100 -0.501500 -52.81780 1
(ATOM LINES ARE NOT SHOWN.)
END
