HEADER OXIDOREDUCTASE 14-MAR-13 4JMZ
TITLE CRYSTAL STRUCTURE OF CYTOCHROME C PEROXIDASE W191G-GATELESS IN COMPLEX
TITLE 2 WITH N-METHYL-1H-BENZIMIDAZOL-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 72-362, DELETIONS G192-A193;
COMPND 5 EC: 1.11.1.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 285006;
SOURCE 5 STRAIN: RM11-1A;
SOURCE 6 GENE: CCP1 CCP CPO YKR066C, SCRG_04081;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS MODEL SYSTEM, BULK SOLVENT, ORDERED WATERS, DOCKING, LIGAND BINDING,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BARELIER,M.FISCHER
REVDAT 3 28-FEB-24 4JMZ 1 REMARK SEQADV
REVDAT 2 28-AUG-13 4JMZ 1 JRNL
REVDAT 1 01-MAY-13 4JMZ 0
JRNL AUTH S.BARELIER,S.E.BOYCE,I.FISH,M.FISCHER,D.B.GOODIN,
JRNL AUTH 2 B.K.SHOICHET
JRNL TITL ROLES FOR ORDERED AND BULK SOLVENT IN LIGAND RECOGNITION AND
JRNL TITL 2 DOCKING IN TWO RELATED CAVITIES.
JRNL REF PLOS ONE V. 8 69153 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23874896
JRNL DOI 10.1371/JOURNAL.PONE.0069153
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 36760
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 : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1888
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2323
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1840
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 482
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.50000
REMARK 3 B22 (A**2) : 1.01000
REMARK 3 B33 (A**2) : -0.51000
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): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.914
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2553 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1731 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3483 ; 2.395 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4208 ; 0.938 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 310 ; 5.890 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 135 ;34.926 ;25.111
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 419 ;12.828 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;23.992 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 336 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2960 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 559 ; 0.009 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4JMZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115869
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37823
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: APO CRYSTAL GROWN IN 100MM KPI, PH
REMARK 280 6.0. SOAKED INTO 20MM ZINC00039393 (10MIN), VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 52.57500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.59000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.28500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.59000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.57500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.28500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 ASP A 150 CB - CG - OD1 ANGL. DEV. = 6.3 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 ASP A 33 59.92 -90.49
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 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 HEM A 301 NA 96.4
REMARK 620 3 HEM A 301 NB 90.5 88.9
REMARK 620 4 HEM A 301 NC 90.4 172.1 95.0
REMARK 620 5 HEM A 301 ND 93.9 87.4 174.5 88.3
REMARK 620 6 HOH A 707 O 174.3 83.0 83.8 90.6 91.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1M2 A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KXN RELATED DB: PDB
REMARK 900 RELATED ID: 1KXM RELATED DB: PDB
REMARK 900 RELATED ID: 4JM5 RELATED DB: PDB
REMARK 900 RELATED ID: 4JM6 RELATED DB: PDB
REMARK 900 RELATED ID: 4JM8 RELATED DB: PDB
REMARK 900 RELATED ID: 4JM9 RELATED DB: PDB
REMARK 900 RELATED ID: 4JMA RELATED DB: PDB
REMARK 900 RELATED ID: 4JMW RELATED DB: PDB
REMARK 900 RELATED ID: 4JPL RELATED DB: PDB
REMARK 900 RELATED ID: 4JPT RELATED DB: PDB
REMARK 900 RELATED ID: 4JPU RELATED DB: PDB
REMARK 900 RELATED ID: 4JQJ RELATED DB: PDB
REMARK 900 RELATED ID: 4JQK RELATED DB: PDB
REMARK 900 RELATED ID: 4JQM RELATED DB: PDB
REMARK 900 RELATED ID: 4JQN RELATED DB: PDB
REMARK 900 RELATED ID: 4JMB RELATED DB: PDB
REMARK 900 RELATED ID: 4JMS RELATED DB: PDB
REMARK 900 RELATED ID: 4JMT RELATED DB: PDB
REMARK 900 RELATED ID: 4JMV RELATED DB: PDB
REMARK 900 RELATED ID: 4JN0 RELATED DB: PDB
DBREF 4JMZ A 4 292 UNP B3LRE1 B3LRE1_YEAS1 72 362
SEQADV 4JMZ GLY A 190 UNP B3LRE1 PRO 258 ENGINEERED MUTATION
SEQADV 4JMZ GLY A 191 UNP B3LRE1 TRP 259 ENGINEERED MUTATION
SEQADV 4JMZ A UNP B3LRE1 GLY 260 DELETION
SEQADV 4JMZ A UNP B3LRE1 ALA 261 DELETION
SEQRES 1 A 289 LEU VAL HIS VAL ALA SER VAL GLU LYS GLY ARG SER TYR
SEQRES 2 A 289 GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE ALA LEU LYS
SEQRES 3 A 289 LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR ILE GLY TYR
SEQRES 4 A 289 GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS ILE SER GLY
SEQRES 5 A 289 THR TRP ASP LYS HIS ASP ASN THR GLY GLY SER TYR GLY
SEQRES 6 A 289 GLY THR TYR ARG PHE LYS LYS GLU PHE ASN ASP PRO SER
SEQRES 7 A 289 ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE LEU GLU PRO
SEQRES 8 A 289 ILE HIS LYS GLU PHE PRO TRP ILE SER SER GLY ASP LEU
SEQRES 9 A 289 PHE SER LEU GLY GLY VAL THR ALA VAL GLN GLU MET GLN
SEQRES 10 A 289 GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG VAL ASP THR
SEQRES 11 A 289 PRO GLU ASP THR THR PRO ASP ASN GLY ARG LEU PRO ASP
SEQRES 12 A 289 ALA ASP LYS ASP ALA GLY TYR VAL ARG THR PHE PHE GLN
SEQRES 13 A 289 ARG LEU ASN MET ASN ASP ARG GLU VAL VAL ALA LEU MET
SEQRES 14 A 289 GLY ALA HIS ALA LEU GLY LYS THR HIS LEU LYS ASN SER
SEQRES 15 A 289 GLY TYR GLU GLY GLY GLY ALA ASN ASN VAL PHE THR ASN
SEQRES 16 A 289 GLU PHE TYR LEU ASN LEU LEU ASN GLU ASP TRP LYS LEU
SEQRES 17 A 289 GLU LYS ASN ASP ALA ASN ASN GLU GLN TRP ASP SER LYS
SEQRES 18 A 289 SER GLY TYR MET MET LEU PRO THR ASP TYR SER LEU ILE
SEQRES 19 A 289 GLN ASP PRO LYS TYR LEU SER ILE VAL LYS GLU TYR ALA
SEQRES 20 A 289 ASN ASP GLN ASP LYS PHE PHE LYS ASP PHE SER LYS ALA
SEQRES 21 A 289 PHE GLU LYS LEU LEU GLU ASN GLY ILE THR PHE PRO LYS
SEQRES 22 A 289 ASP ALA PRO SER PRO PHE ILE PHE LYS THR LEU GLU GLU
SEQRES 23 A 289 GLN GLY LEU
HET HEM A 301 43
HET 1M2 A 302 11
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 1M2 N-METHYL-1H-BENZIMIDAZOL-2-AMINE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 1M2 C8 H9 N3
FORMUL 4 HOH *482(H2 O)
HELIX 1 1 SER A 15 ASP A 33 1 19
HELIX 2 2 GLU A 35 ILE A 40 1 6
HELIX 3 3 TYR A 42 GLY A 55 1 14
HELIX 4 4 GLY A 69 ARG A 72 5 4
HELIX 5 5 PHE A 73 ASN A 78 1 6
HELIX 6 6 ASP A 79 GLY A 84 5 6
HELIX 7 7 LEU A 85 PHE A 99 1 15
HELIX 8 8 SER A 103 MET A 119 1 17
HELIX 9 9 PRO A 134 THR A 138 5 5
HELIX 10 10 ASP A 150 ARG A 160 1 11
HELIX 11 11 ASN A 164 GLY A 173 1 10
HELIX 12 12 ALA A 174 LEU A 177 5 4
HELIX 13 13 HIS A 181 GLY A 186 1 6
HELIX 14 14 ASN A 198 GLU A 207 1 10
HELIX 15 15 LEU A 230 ASP A 239 1 10
HELIX 16 16 ASP A 239 ASN A 251 1 13
HELIX 17 17 ASP A 252 ASN A 270 1 19
HELIX 18 18 THR A 286 GLY A 291 1 6
SHEET 1 A 2 HIS A 6 VAL A 7 0
SHEET 2 A 2 ILE A 272 THR A 273 1 O THR A 273 N HIS A 6
SHEET 1 B 3 TRP A 209 LYS A 213 0
SHEET 2 B 3 GLU A 219 SER A 223 -1 O GLN A 220 N GLU A 212
SHEET 3 B 3 MET A 228 MET A 229 -1 O MET A 229 N TRP A 221
LINK NE2 HIS A 175 FE HEM A 301 1555 1555 2.09
LINK FE HEM A 301 O HOH A 707 1555 1555 2.17
SITE 1 AC1 22 PRO A 44 ARG A 48 TRP A 51 PRO A 145
SITE 2 AC1 22 ASP A 146 ALA A 147 LEU A 171 ALA A 174
SITE 3 AC1 22 HIS A 175 GLY A 178 LYS A 179 THR A 180
SITE 4 AC1 22 HIS A 181 ASN A 184 SER A 185 LEU A 230
SITE 5 AC1 22 THR A 232 1M2 A 302 HOH A 431 HOH A 448
SITE 6 AC1 22 HOH A 471 HOH A 707
SITE 1 AC2 12 HIS A 175 ALA A 176 LEU A 177 GLY A 178
SITE 2 AC2 12 LYS A 179 THR A 180 GLY A 191 LEU A 230
SITE 3 AC2 12 ASP A 233 HEM A 301 HOH A 735 HOH A 737
CRYST1 105.150 74.570 51.180 90.00 90.00 90.00 P 21 21 21 4
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 0.009510 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019539 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
