HEADER OXIDOREDUCTASE 02-SEP-03 1QWM
TITLE STRUCTURE OF HELICOBACTER PYLORI CATALASE WITH FORMIC ACID BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KATA CATALASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.11.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_TAXID: 210;
SOURCE 4 GENE: KATA (HP0875);
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: PSO100
KEYWDS BETA BARREL, AZIDE COMPLEX, FORMATE COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.LOEWEN,X.CARPENA,R.PEREZ-LUQUE,C.ROVIRA,R.HAAS,S.ODENBREIT,
AUTHOR 2 P.NICHOLLS,I.FITA
REVDAT 4 16-AUG-23 1QWM 1 REMARK LINK
REVDAT 3 13-JUL-11 1QWM 1 VERSN
REVDAT 2 24-FEB-09 1QWM 1 VERSN
REVDAT 1 30-MAR-04 1QWM 0
JRNL AUTH P.C.LOEWEN,X.CARPENA,C.ROVIRA,A.IVANCICH,R.PEREZ-LUQUE,
JRNL AUTH 2 R.HAAS,S.OBENBREIT,P.NICHOLLS,I.FITA
JRNL TITL STRUCTURE OF HELICOBACTER PYLORI CATALASE, WITH AND WITHOUT
JRNL TITL 2 FORMIC ACID BOUND, AT 1.6 A RESOLUTION
JRNL REF BIOCHEMISTRY V. 43 3089 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15023060
JRNL DOI 10.1021/BI035663I
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 118512
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6282
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8128
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 429
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8040
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 197
REMARK 3 SOLVENT ATOMS : 933
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : -0.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.698
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8503 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11480 ; 1.612 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 980 ; 6.067 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1128 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6641 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4021 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; 0.150 ; 0.200
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): 369 ; 0.202 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 126 ; 0.239 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4976 ; 0.924 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7948 ; 1.453 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3527 ; 2.319 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3532 ; 3.540 ; 4.500
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
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 490 6
REMARK 3 1 B 1 B 490 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 4017 ; 0.21 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 4017 ; 1.41 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020156.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-02
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1QWL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG MME 550, 0.1 M SODIUM CITRATE,
REMARK 280 10 MM ZNSO4, 3 MM NAN3, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 32.37800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.48050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.37800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.48050
REMARK 290 SMTRY3 4 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 62380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -266.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 64.75600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 154.96100
REMARK 350 BIOMT3 2 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 LYS A 491
REMARK 465 ASP A 492
REMARK 465 MET A 493
REMARK 465 HIS A 494
REMARK 465 GLY A 495
REMARK 465 LYS A 496
REMARK 465 ASP A 497
REMARK 465 MET A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 THR A 501
REMARK 465 LYS A 502
REMARK 465 LYS A 503
REMARK 465 LYS A 504
REMARK 465 LYS A 505
REMARK 465 LYS B 491
REMARK 465 ASP B 492
REMARK 465 MET B 493
REMARK 465 HIS B 494
REMARK 465 GLY B 495
REMARK 465 LYS B 496
REMARK 465 ASP B 497
REMARK 465 MET B 498
REMARK 465 HIS B 499
REMARK 465 HIS B 500
REMARK 465 THR B 501
REMARK 465 LYS B 502
REMARK 465 LYS B 503
REMARK 465 LYS B 504
REMARK 465 LYS B 505
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 O1 FMT A 1714 O HOH A 2694 1.83
REMARK 500 O HOH A 2935 O HOH A 3018 1.84
REMARK 500 O HOH A 2812 O HOH A 3011 2.09
REMARK 500 OE1 GLU A 89 O HOH A 2763 2.10
REMARK 500 O ARG B 101 O2 FMT B 1720 2.13
REMARK 500 O HOH B 2022 O HOH B 2201 2.17
REMARK 500 OH TYR A 371 O2 FMT A 1730 2.17
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 NE2 GLN A 154 O HOH A 2849 2665 1.45
REMARK 500 O HOH A 2930 O HOH B 2217 1554 1.91
REMARK 500 O2 FMT B 1721 O HOH B 2177 2665 1.94
REMARK 500 O HOH B 2009 O HOH B 2128 2665 2.17
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 LEU A 32 CA - CB - CG ANGL. DEV. = -16.2 DEGREES
REMARK 500 ASP A 109 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 446 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 18 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 109 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 125 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 279 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 399 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 35 76.05 -69.69
REMARK 500 LYS A 150 -137.40 -104.78
REMARK 500 SER A 198 -63.32 68.86
REMARK 500 ASN A 300 10.19 -140.61
REMARK 500 PRO A 328 27.41 -78.48
REMARK 500 ASP A 369 -146.27 72.60
REMARK 500 LYS B 150 -143.13 -99.03
REMARK 500 SER B 198 -65.62 73.91
REMARK 500 ASN B 300 11.44 -144.17
REMARK 500 PRO B 328 25.71 -79.89
REMARK 500 ASP B 369 -147.21 74.37
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 550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 339 OH
REMARK 620 2 HEM A 550 NA 98.4
REMARK 620 3 HEM A 550 NB 96.4 90.5
REMARK 620 4 HEM A 550 NC 88.9 172.5 87.5
REMARK 620 5 HEM A 550 ND 91.0 89.6 172.5 91.4
REMARK 620 6 FMT A1701 O2 162.7 96.9 91.4 75.9 81.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 339 OH
REMARK 620 2 HEM B 550 NA 99.2
REMARK 620 3 HEM B 550 NB 97.2 91.3
REMARK 620 4 HEM B 550 NC 89.6 171.2 86.6
REMARK 620 5 HEM B 550 ND 92.3 89.1 170.3 91.5
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 AZI A 2600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1708
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1714
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1715
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1716
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1717
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1718
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1719
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1720
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1721
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1722
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1723
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1724
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1725
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1726
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1727
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1728
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1729
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1730
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1731
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1732
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1733
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1734
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1735
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1736
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QWL RELATED DB: PDB
REMARK 900 STRUCTURE OF HELICOBACTER PYLORI CATALASE
DBREF 1QWM A 1 505 UNP P77872 CATA_HELPY 1 505
DBREF 1QWM B 1 505 UNP P77872 CATA_HELPY 1 505
SEQRES 1 A 505 MET VAL ASN LYS ASP VAL LYS GLN THR THR ALA PHE GLY
SEQRES 2 A 505 ALA PRO VAL TRP ASP ASP ASN ASN VAL ILE THR ALA GLY
SEQRES 3 A 505 PRO ARG GLY PRO VAL LEU LEU GLN SER THR TRP PHE LEU
SEQRES 4 A 505 GLU LYS LEU ALA ALA PHE ASP ARG GLU ARG ILE PRO GLU
SEQRES 5 A 505 ARG VAL VAL HIS ALA LYS GLY SER GLY ALA TYR GLY THR
SEQRES 6 A 505 PHE THR VAL THR LYS ASP ILE THR LYS TYR THR LYS ALA
SEQRES 7 A 505 LYS ILE PHE SER LYS VAL GLY LYS LYS THR GLU CYS PHE
SEQRES 8 A 505 PHE ARG PHE SER THR VAL ALA GLY GLU ARG GLY SER ALA
SEQRES 9 A 505 ASP ALA VAL ARG ASP PRO ARG GLY PHE ALA MET LYS TYR
SEQRES 10 A 505 TYR THR GLU GLU GLY ASN TRP ASP LEU VAL GLY ASN ASN
SEQRES 11 A 505 THR PRO VAL PHE PHE ILE ARG ASP ALA ILE LYS PHE PRO
SEQRES 12 A 505 ASP PHE ILE HIS THR GLN LYS ARG ASP PRO GLN THR ASN
SEQRES 13 A 505 LEU PRO ASN HIS ASP MET VAL TRP ASP PHE TRP SER ASN
SEQRES 14 A 505 VAL PRO GLU SER LEU TYR GLN VAL THR TRP VAL MET SER
SEQRES 15 A 505 ASP ARG GLY ILE PRO LYS SER PHE ARG HIS MET ASP GLY
SEQRES 16 A 505 PHE GLY SER HIS THR PHE SER LEU ILE ASN ALA LYS GLY
SEQRES 17 A 505 GLU ARG PHE TRP VAL LYS PHE HIS PHE HIS THR MET GLN
SEQRES 18 A 505 GLY VAL LYS HIS LEU THR ASN GLU GLU ALA ALA GLU ILE
SEQRES 19 A 505 ARG LYS HIS ASP PRO ASP SER ASN GLN ARG ASP LEU PHE
SEQRES 20 A 505 ASP ALA ILE ALA ARG GLY ASP TYR PRO LYS TRP LYS LEU
SEQRES 21 A 505 SER ILE GLN VAL MET PRO GLU GLU ASP ALA LYS LYS TYR
SEQRES 22 A 505 ARG PHE HIS PRO PHE ASP VAL THR LYS ILE TRP TYR THR
SEQRES 23 A 505 GLN ASP TYR PRO LEU MET GLU VAL GLY ILE VAL GLU LEU
SEQRES 24 A 505 ASN LYS ASN PRO GLU ASN TYR PHE ALA GLU VAL GLU GLN
SEQRES 25 A 505 ALA ALA PHE THR PRO ALA ASN VAL VAL PRO GLY ILE GLY
SEQRES 26 A 505 TYR SER PRO ASP ARG MET LEU GLN GLY ARG LEU PHE SER
SEQRES 27 A 505 TYR GLY ASP THR HIS ARG TYR ARG LEU GLY VAL ASN TYR
SEQRES 28 A 505 PRO GLN ILE PRO VAL ASN LYS PRO ARG CYS PRO PHE HIS
SEQRES 29 A 505 SER SER SER ARG ASP GLY TYR MET GLN ASN GLY TYR TYR
SEQRES 30 A 505 GLY SER LEU GLN ASN TYR THR PRO SER SER LEU PRO GLY
SEQRES 31 A 505 TYR LYS GLU ASP LYS SER ALA ARG ASP PRO LYS PHE ASN
SEQRES 32 A 505 LEU ALA HIS ILE GLU LYS GLU PHE GLU VAL TRP ASN TRP
SEQRES 33 A 505 ASP TYR ARG ALA ASP ASP SER ASP TYR TYR THR GLN PRO
SEQRES 34 A 505 GLY ASP TYR TYR ARG SER LEU PRO ALA ASP GLU LYS GLU
SEQRES 35 A 505 ARG LEU HIS ASP THR ILE GLY GLU SER LEU ALA HIS VAL
SEQRES 36 A 505 THR HIS LYS GLU ILE VAL ASP LYS GLN LEU GLU HIS PHE
SEQRES 37 A 505 LYS LYS ALA ASP PRO LYS TYR ALA GLU GLY VAL LYS LYS
SEQRES 38 A 505 ALA LEU GLU LYS HIS GLN LYS MET MET LYS ASP MET HIS
SEQRES 39 A 505 GLY LYS ASP MET HIS HIS THR LYS LYS LYS LYS
SEQRES 1 B 505 MET VAL ASN LYS ASP VAL LYS GLN THR THR ALA PHE GLY
SEQRES 2 B 505 ALA PRO VAL TRP ASP ASP ASN ASN VAL ILE THR ALA GLY
SEQRES 3 B 505 PRO ARG GLY PRO VAL LEU LEU GLN SER THR TRP PHE LEU
SEQRES 4 B 505 GLU LYS LEU ALA ALA PHE ASP ARG GLU ARG ILE PRO GLU
SEQRES 5 B 505 ARG VAL VAL HIS ALA LYS GLY SER GLY ALA TYR GLY THR
SEQRES 6 B 505 PHE THR VAL THR LYS ASP ILE THR LYS TYR THR LYS ALA
SEQRES 7 B 505 LYS ILE PHE SER LYS VAL GLY LYS LYS THR GLU CYS PHE
SEQRES 8 B 505 PHE ARG PHE SER THR VAL ALA GLY GLU ARG GLY SER ALA
SEQRES 9 B 505 ASP ALA VAL ARG ASP PRO ARG GLY PHE ALA MET LYS TYR
SEQRES 10 B 505 TYR THR GLU GLU GLY ASN TRP ASP LEU VAL GLY ASN ASN
SEQRES 11 B 505 THR PRO VAL PHE PHE ILE ARG ASP ALA ILE LYS PHE PRO
SEQRES 12 B 505 ASP PHE ILE HIS THR GLN LYS ARG ASP PRO GLN THR ASN
SEQRES 13 B 505 LEU PRO ASN HIS ASP MET VAL TRP ASP PHE TRP SER ASN
SEQRES 14 B 505 VAL PRO GLU SER LEU TYR GLN VAL THR TRP VAL MET SER
SEQRES 15 B 505 ASP ARG GLY ILE PRO LYS SER PHE ARG HIS MET ASP GLY
SEQRES 16 B 505 PHE GLY SER HIS THR PHE SER LEU ILE ASN ALA LYS GLY
SEQRES 17 B 505 GLU ARG PHE TRP VAL LYS PHE HIS PHE HIS THR MET GLN
SEQRES 18 B 505 GLY VAL LYS HIS LEU THR ASN GLU GLU ALA ALA GLU ILE
SEQRES 19 B 505 ARG LYS HIS ASP PRO ASP SER ASN GLN ARG ASP LEU PHE
SEQRES 20 B 505 ASP ALA ILE ALA ARG GLY ASP TYR PRO LYS TRP LYS LEU
SEQRES 21 B 505 SER ILE GLN VAL MET PRO GLU GLU ASP ALA LYS LYS TYR
SEQRES 22 B 505 ARG PHE HIS PRO PHE ASP VAL THR LYS ILE TRP TYR THR
SEQRES 23 B 505 GLN ASP TYR PRO LEU MET GLU VAL GLY ILE VAL GLU LEU
SEQRES 24 B 505 ASN LYS ASN PRO GLU ASN TYR PHE ALA GLU VAL GLU GLN
SEQRES 25 B 505 ALA ALA PHE THR PRO ALA ASN VAL VAL PRO GLY ILE GLY
SEQRES 26 B 505 TYR SER PRO ASP ARG MET LEU GLN GLY ARG LEU PHE SER
SEQRES 27 B 505 TYR GLY ASP THR HIS ARG TYR ARG LEU GLY VAL ASN TYR
SEQRES 28 B 505 PRO GLN ILE PRO VAL ASN LYS PRO ARG CYS PRO PHE HIS
SEQRES 29 B 505 SER SER SER ARG ASP GLY TYR MET GLN ASN GLY TYR TYR
SEQRES 30 B 505 GLY SER LEU GLN ASN TYR THR PRO SER SER LEU PRO GLY
SEQRES 31 B 505 TYR LYS GLU ASP LYS SER ALA ARG ASP PRO LYS PHE ASN
SEQRES 32 B 505 LEU ALA HIS ILE GLU LYS GLU PHE GLU VAL TRP ASN TRP
SEQRES 33 B 505 ASP TYR ARG ALA ASP ASP SER ASP TYR TYR THR GLN PRO
SEQRES 34 B 505 GLY ASP TYR TYR ARG SER LEU PRO ALA ASP GLU LYS GLU
SEQRES 35 B 505 ARG LEU HIS ASP THR ILE GLY GLU SER LEU ALA HIS VAL
SEQRES 36 B 505 THR HIS LYS GLU ILE VAL ASP LYS GLN LEU GLU HIS PHE
SEQRES 37 B 505 LYS LYS ALA ASP PRO LYS TYR ALA GLU GLY VAL LYS LYS
SEQRES 38 B 505 ALA LEU GLU LYS HIS GLN LYS MET MET LYS ASP MET HIS
SEQRES 39 B 505 GLY LYS ASP MET HIS HIS THR LYS LYS LYS LYS
HET AZI A2600 3
HET HEM A 550 43
HET FMT A1701 3
HET FMT A1704 3
HET FMT A1706 3
HET FMT A1709 3
HET FMT A1710 3
HET FMT A1711 3
HET FMT A1713 3
HET FMT A1714 3
HET FMT A1715 3
HET FMT A1716 3
HET FMT A1718 3
HET FMT A1719 3
HET FMT A1722 3
HET FMT A1723 3
HET FMT A1724 3
HET FMT A1725 3
HET FMT A1730 3
HET FMT A1732 3
HET FMT A1733 3
HET FMT A1734 3
HET FMT A1735 3
HET HEM B 550 43
HET FMT B1702 3
HET FMT B1703 3
HET FMT B1705 3
HET FMT B1707 3
HET FMT B1708 3
HET FMT B1712 3
HET FMT B1717 3
HET FMT B1720 3
HET FMT B1721 3
HET FMT B1726 3
HET FMT B1727 3
HET FMT B1728 3
HET FMT B1729 3
HET FMT B1731 3
HET FMT B1736 3
HETNAM AZI AZIDE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FMT FORMIC ACID
HETSYN HEM HEME
FORMUL 3 AZI N3 1-
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 FMT 36(C H2 O2)
FORMUL 42 HOH *933(H2 O)
HELIX 1 1 SER A 35 ASP A 46 1 12
HELIX 2 2 ALA A 78 SER A 82 5 5
HELIX 3 3 ASP A 138 ILE A 140 5 3
HELIX 4 4 LYS A 141 LYS A 150 1 10
HELIX 5 5 ASN A 159 VAL A 170 1 12
HELIX 6 6 SER A 173 SER A 182 1 10
HELIX 7 7 ASP A 183 ILE A 186 5 4
HELIX 8 8 SER A 189 MET A 193 5 5
HELIX 9 9 THR A 227 ASP A 238 1 12
HELIX 10 10 ASP A 240 ARG A 252 1 13
HELIX 11 11 GLU A 268 ALA A 270 5 3
HELIX 12 12 ASN A 305 VAL A 310 1 6
HELIX 13 13 ASP A 329 GLY A 348 1 20
HELIX 14 14 ASN A 350 LYS A 358 5 9
HELIX 15 15 ASP A 394 ARG A 398 5 5
HELIX 16 16 ASN A 403 ILE A 407 5 5
HELIX 17 17 ASP A 417 ASP A 422 1 6
HELIX 18 18 TYR A 426 LEU A 436 1 11
HELIX 19 19 PRO A 437 ALA A 453 1 17
HELIX 20 20 HIS A 457 ASP A 472 1 16
HELIX 21 21 ASP A 472 MET A 490 1 19
HELIX 22 22 SER B 35 ASP B 46 1 12
HELIX 23 23 ALA B 78 SER B 82 5 5
HELIX 24 24 ASP B 138 ILE B 140 5 3
HELIX 25 25 LYS B 141 LYS B 150 1 10
HELIX 26 26 ASN B 159 VAL B 170 1 12
HELIX 27 27 SER B 173 SER B 182 1 10
HELIX 28 28 ASP B 183 ILE B 186 5 4
HELIX 29 29 SER B 189 MET B 193 5 5
HELIX 30 30 THR B 227 ASP B 238 1 12
HELIX 31 31 ASP B 240 ARG B 252 1 13
HELIX 32 32 GLU B 268 ALA B 270 5 3
HELIX 33 33 ASN B 305 VAL B 310 1 6
HELIX 34 34 ASP B 329 GLY B 348 1 20
HELIX 35 35 ASN B 350 LYS B 358 5 9
HELIX 36 36 ASP B 394 ARG B 398 5 5
HELIX 37 37 ASN B 403 ILE B 407 5 5
HELIX 38 38 ASP B 417 ASP B 422 1 6
HELIX 39 39 TYR B 426 LEU B 436 1 11
HELIX 40 40 PRO B 437 ALA B 453 1 17
HELIX 41 41 HIS B 457 ASP B 472 1 16
HELIX 42 42 ASP B 472 MET B 490 1 19
SHEET 1 A11 ILE A 324 GLY A 325 0
SHEET 2 A11 PHE A 201 ILE A 204 -1 N SER A 202 O GLY A 325
SHEET 3 A11 ARG A 210 THR A 219 -1 O PHE A 211 N LEU A 203
SHEET 4 A11 LYS A 257 PRO A 266 -1 O MET A 265 N TRP A 212
SHEET 5 A11 MET A 292 LYS A 301 -1 O VAL A 294 N LEU A 260
SHEET 6 A11 GLY A 59 VAL A 68 -1 N THR A 67 O ILE A 296
SHEET 7 A11 LYS A 87 SER A 95 -1 O PHE A 92 N ALA A 62
SHEET 8 A11 GLY A 112 THR A 119 -1 O ALA A 114 N ARG A 93
SHEET 9 A11 GLY A 122 ASN A 129 -1 O GLY A 128 N PHE A 113
SHEET 10 A11 GLY A 195 PHE A 196 -1 O PHE A 196 N ASN A 129
SHEET 11 A11 ARG A 210 THR A 219 -1 O PHE A 217 N GLY A 195
SHEET 1 B11 ILE B 324 GLY B 325 0
SHEET 2 B11 PHE B 201 ILE B 204 -1 N SER B 202 O GLY B 325
SHEET 3 B11 ARG B 210 THR B 219 -1 O PHE B 211 N LEU B 203
SHEET 4 B11 LYS B 257 PRO B 266 -1 O MET B 265 N TRP B 212
SHEET 5 B11 MET B 292 LYS B 301 -1 O VAL B 294 N LEU B 260
SHEET 6 B11 GLY B 59 VAL B 68 -1 N TYR B 63 O LYS B 301
SHEET 7 B11 LYS B 87 SER B 95 -1 O PHE B 94 N SER B 60
SHEET 8 B11 GLY B 112 THR B 119 -1 O ALA B 114 N ARG B 93
SHEET 9 B11 GLY B 122 ASN B 129 -1 O TRP B 124 N TYR B 117
SHEET 10 B11 GLY B 195 PHE B 196 -1 O PHE B 196 N ASN B 129
SHEET 11 B11 ARG B 210 THR B 219 -1 O PHE B 217 N GLY B 195
LINK O BARG A 101 O2 FMT A1710 1555 1555 1.96
LINK O1 FMT A1735 N1 AZI A2600 1555 1555 1.73
LINK OH TYR A 339 FE HEM A 550 1555 1555 1.87
LINK FE HEM A 550 O2 FMT A1701 1555 1555 2.64
LINK OH TYR B 339 FE HEM B 550 1555 1555 1.93
CISPEP 1 THR A 384 PRO A 385 0 -8.72
CISPEP 2 THR B 384 PRO B 385 0 -3.10
SITE 1 AC1 6 ARG A 47 ARG A 344 FMT A1713 FMT A1735
SITE 2 AC1 6 ARG B 47 TYR B 345
SITE 1 AC2 27 ASP A 46 ARG A 53 VAL A 54 VAL A 55
SITE 2 AC2 27 HIS A 56 ARG A 93 GLY A 112 VAL A 127
SITE 3 AC2 27 GLY A 128 ASN A 129 ALA A 139 PHE A 142
SITE 4 AC2 27 GLY A 197 SER A 198 HIS A 199 PHE A 315
SITE 5 AC2 27 MET A 331 ARG A 335 SER A 338 TYR A 339
SITE 6 AC2 27 THR A 342 HIS A 343 ARG A 346 FMT A1701
SITE 7 AC2 27 HOH A2606 HOH A2629 HOH A2668
SITE 1 AC3 28 ASP B 46 ARG B 53 VAL B 54 VAL B 55
SITE 2 AC3 28 HIS B 56 ARG B 93 GLY B 112 PHE B 113
SITE 3 AC3 28 ALA B 114 VAL B 127 GLY B 128 ASN B 129
SITE 4 AC3 28 ALA B 139 PHE B 142 GLY B 197 SER B 198
SITE 5 AC3 28 PHE B 315 MET B 331 ARG B 335 SER B 338
SITE 6 AC3 28 TYR B 339 THR B 342 HIS B 343 ARG B 346
SITE 7 AC3 28 FMT B1702 HOH B1739 HOH B1745 HOH B1792
SITE 1 AC4 5 HIS A 56 ASN A 129 PHE A 134 PHE A 142
SITE 2 AC4 5 HEM A 550
SITE 1 AC5 5 HIS B 56 VAL B 97 ASN B 129 PHE B 134
SITE 2 AC5 5 HEM B 550
SITE 1 AC6 6 ARG B 108 ASP B 109 PRO B 110 PHE B 135
SITE 2 AC6 6 GLN B 149 VAL B 180
SITE 1 AC7 5 GLN A 149 VAL A 163 TRP A 167 MET A 181
SITE 2 AC7 5 HOH A3041
SITE 1 AC8 7 GLN B 149 PRO B 158 VAL B 163 FMT B1707
SITE 2 AC8 7 HOH B1827 HOH B2015 HOH B2224
SITE 1 AC9 4 PRO A 158 HIS A 160 HOH A2784 HOH A2855
SITE 1 BC1 3 FMT B1705 HOH B1977 HOH B2112
SITE 1 BC2 6 HIS B 160 GLU B 450 SER B 451 HIS B 454
SITE 2 BC2 6 HOH B1817 HOH B1986
SITE 1 BC3 6 ASP A 183 ARG A 184 VAL A 223 GLU A 440
SITE 2 BC3 6 HOH A2717 HOH A2732
SITE 1 BC4 8 LYS A 58 ARG A 101 GLY A 102 ARG A 151
SITE 2 BC4 8 ASN A 156 FMT A1734 HOH A2845 HOH A2890
SITE 1 BC5 5 LYS A 150 ARG A 151 HOH A2607 HOH A2652
SITE 2 BC5 5 HOH A3040
SITE 1 BC6 8 ALA B 57 LYS B 58 GLY B 59 ARG B 101
SITE 2 BC6 8 TYR B 306 GLU B 311 FMT B1720 HOH B2207
SITE 1 BC7 5 ARG A 47 TYR A 345 AZI A2600 HOH A2654
SITE 2 BC7 5 ARG B 344
SITE 1 BC8 5 ASN A 130 TRP A 179 ARG A 184 ASP A 194
SITE 2 BC8 5 HOH A2694
SITE 1 BC9 2 TYR A 371 TYR B 371
SITE 1 CC1 7 PRO A 352 GLN A 353 PRO A 359 PHE A 363
SITE 2 CC1 7 HOH A2791 HOH A2860 ALA B 11
SITE 1 CC2 3 TYR B 285 THR B 286 HOH B2133
SITE 1 CC3 4 PHE A 247 ALA A 251 ASN A 302 HOH A2725
SITE 1 CC4 5 LYS A 77 GLY A 323 SER A 396 ALA A 397
SITE 2 CC4 5 ARG A 398
SITE 1 CC5 8 LYS B 58 ARG B 101 GLY B 102 ARG B 151
SITE 2 CC5 8 ASN B 156 FMT B1712 HOH B2050 HOH B2207
SITE 1 CC6 8 HOH A2634 ARG B 49 ARG B 101 HOH B1801
SITE 2 CC6 8 HOH B1916 HOH B2050 HOH B2085 HOH B2177
SITE 1 CC7 4 ASP A 194 HIS A 218 THR A 219 HOH A2928
SITE 1 CC8 4 VAL A 223 LYS A 224 HOH A2688 HOH A2978
SITE 1 CC9 3 LYS A 188 HOH A2688 HOH A2925
SITE 1 DC1 4 LYS A 188 LEU A 226 HOH A2925 HOH A2956
SITE 1 DC2 3 VAL B 223 LYS B 224 HOH B1830
SITE 1 DC3 3 ASP B 183 HIS B 225 GLU B 440
SITE 1 DC4 4 LYS B 188 LYS B 224 HOH B1830 HOH B2143
SITE 1 DC5 9 SER B 182 ASP B 183 ARG B 184 TYR B 432
SITE 2 DC5 9 LEU B 436 GLU B 440 HOH B1897 HOH B2000
SITE 3 DC5 9 HOH B2225
SITE 1 DC6 4 TYR A 371 FMT A1735 PRO B 51 TYR B 345
SITE 1 DC7 5 LEU B 336 PHE B 337 ASP B 341 ARG B 344
SITE 2 DC7 5 FMT B1736
SITE 1 DC8 4 LEU A 336 PHE A 337 ARG A 344 FMT A1733
SITE 1 DC9 9 ALA A 318 ARG A 344 FMT A1732 HOH A2787
SITE 2 DC9 9 THR B 36 LEU B 39 GLU B 40 HOH B1800
SITE 3 DC9 9 HOH B2160
SITE 1 EC1 8 ALA A 57 LYS A 58 GLY A 59 ARG A 101
SITE 2 EC1 8 TYR A 306 GLU A 311 FMT A1710 HOH A2845
SITE 1 EC2 7 ARG A 344 FMT A1730 AZI A2600 HOH A2727
SITE 2 EC2 7 HOH A2867 ARG B 47 TYR B 345
SITE 1 EC3 9 THR A 36 LEU A 39 GLU A 40 ALA B 318
SITE 2 EC3 9 ARG B 344 FMT B1731 HOH B1917 HOH B2011
SITE 3 EC3 9 HOH B2179
CRYST1 64.756 154.961 96.163 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015443 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END