HEADER OXIDOREDUCTASE 26-JAN-15 4XV8
TITLE CCP GATELESS CAVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 71-361;
COMPND 5 SYNONYM: CCP;
COMPND 6 EC: 1.11.1.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: CCP1, CCP, CPO, YKR066C;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MODEL SYSTEM, FLEXIBILITY, THERMODYNAMICS, CRYPTIC SITE, TRANSIENT
KEYWDS 2 PROTEIN SITES, LIGAND BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FISCHER,J.S.FRASER
REVDAT 7 28-FEB-24 4XV8 1 REMARK
REVDAT 6 11-DEC-19 4XV8 1 REMARK
REVDAT 5 27-NOV-19 4XV8 1 REMARK
REVDAT 4 20-SEP-17 4XV8 1 SOURCE REMARK
REVDAT 3 29-JUL-15 4XV8 1 JRNL
REVDAT 2 24-JUN-15 4XV8 1 JRNL
REVDAT 1 18-FEB-15 4XV8 0
JRNL AUTH M.FISCHER,B.K.SHOICHET,J.S.FRASER
JRNL TITL ONE CRYSTAL, TWO TEMPERATURES: CRYOCOOLING PENALTIES ALTER
JRNL TITL 2 LIGAND BINDING TO TRANSIENT PROTEIN SITES.
JRNL REF CHEMBIOCHEM V. 16 1560 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 26032594
JRNL DOI 10.1002/CBIC.201500196
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.FISCHER,R.G.COLEMAN,J.S.FRASER,B.K.SHOICHET
REMARK 1 TITL INCORPORATION OF PROTEIN FLEXIBILITY AND CONFORMATIONAL
REMARK 1 TITL 2 ENERGY PENALTIES IN DOCKING SCREENS TO IMPROVE LIGAND
REMARK 1 TITL 3 DISCOVERY.
REMARK 1 REF NAT CHEM V. 6 575 2014
REMARK 1 REFN ESSN 1755-4349
REMARK 1 PMID 24950326
REMARK 1 DOI 10.1038/NCHEM.1954
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 60160
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.110
REMARK 3 R VALUE (WORKING SET) : 0.108
REMARK 3 FREE R VALUE : 0.140
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3040
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7685 - 4.3973 0.97 2750 141 0.1112 0.1467
REMARK 3 2 4.3973 - 3.4909 0.98 2639 136 0.0919 0.1148
REMARK 3 3 3.4909 - 3.0499 0.99 2658 120 0.1078 0.1309
REMARK 3 4 3.0499 - 2.7711 0.99 2620 139 0.1112 0.1415
REMARK 3 5 2.7711 - 2.5725 0.99 2584 142 0.1139 0.1477
REMARK 3 6 2.5725 - 2.4209 0.99 2636 137 0.1119 0.1322
REMARK 3 7 2.4209 - 2.2996 1.00 2580 147 0.1020 0.1291
REMARK 3 8 2.2996 - 2.1995 1.00 2623 114 0.0970 0.1288
REMARK 3 9 2.1995 - 2.1149 1.00 2604 136 0.0932 0.1407
REMARK 3 10 2.1149 - 2.0419 1.00 2584 131 0.0981 0.1319
REMARK 3 11 2.0419 - 1.9780 1.00 2563 143 0.0936 0.1455
REMARK 3 12 1.9780 - 1.9215 1.00 2564 152 0.0938 0.1228
REMARK 3 13 1.9215 - 1.8709 1.00 2606 142 0.0969 0.1212
REMARK 3 14 1.8709 - 1.8253 1.00 2564 153 0.1002 0.1581
REMARK 3 15 1.8253 - 1.7838 1.00 2585 122 0.1123 0.1532
REMARK 3 16 1.7838 - 1.7458 1.00 2582 134 0.1246 0.1614
REMARK 3 17 1.7458 - 1.7109 1.00 2540 134 0.1306 0.1293
REMARK 3 18 1.7109 - 1.6786 1.00 2602 132 0.1459 0.1772
REMARK 3 19 1.6786 - 1.6486 1.00 2589 154 0.1548 0.1954
REMARK 3 20 1.6486 - 1.6207 1.00 2552 141 0.1493 0.1928
REMARK 3 21 1.6207 - 1.5945 1.00 2555 140 0.1638 0.2161
REMARK 3 22 1.5945 - 1.5700 1.00 2540 150 0.1696 0.1975
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.52
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.017 2653
REMARK 3 ANGLE : 1.592 3631
REMARK 3 CHIRALITY : 0.108 351
REMARK 3 PLANARITY : 0.010 490
REMARK 3 DIHEDRAL : 15.167 987
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 273
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) : 0.95372
REMARK 200 MONOCHROMATOR : KOHZU DUAL DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.3.3.3
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60219
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 39.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: COMPOUND SOAKED INTO CRYSTAL GROWN IN
REMARK 280 EQUAL VOLUME OF 500MM MES BUFFER AND 25% MPD, PH 6, VAPOR
REMARK 280 DIFFUSION, HANGING 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 25.73000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.85500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.47500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.85500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.73000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.47500
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 300 REMARK: BIOLOGICAL ASSEMBLY IS A MONOMER
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
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 252 89.70 -150.15
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 94.7
REMARK 620 3 HEM A 301 NB 90.3 88.9
REMARK 620 4 HEM A 301 NC 87.6 177.6 90.7
REMARK 620 5 HEM A 301 ND 92.2 91.3 177.4 89.1
REMARK 620 6 HOH A 459 O 177.7 85.1 87.4 92.5 90.0
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 BEN A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NVC RELATED DB: PDB
REMARK 900 COLLECTED AT RT ON THE SAME CRYSTAL AS 4NVC
REMARK 900 RELATED ID: 4XV4 RELATED DB: PDB
REMARK 900 RELATED ID: 4XV5 RELATED DB: PDB
REMARK 900 RELATED ID: 4XV6 RELATED DB: PDB
REMARK 900 RELATED ID: 4XV7 RELATED DB: PDB
REMARK 900 RELATED ID: 4XVA RELATED DB: PDB
DBREF 4XV8 A 4 292 UNP P00431 CCPR_YEAST 71 361
SEQADV 4XV8 MET A 1 UNP P00431 INITIATING METHIONINE
SEQADV 4XV8 LYS A 2 UNP P00431 EXPRESSION TAG
SEQADV 4XV8 THR A 3 UNP P00431 EXPRESSION TAG
SEQADV 4XV8 ILE A 53 UNP P00431 THR 120 CONFLICT
SEQADV 4XV8 GLY A 152 UNP P00431 ASP 219 CONFLICT
SEQADV 4XV8 GLY A 190 UNP P00431 PRO 257 ENGINEERED MUTATION
SEQADV 4XV8 GLY A 191 UNP P00431 TRP 258 ENGINEERED MUTATION
SEQADV 4XV8 A UNP P00431 GLY 259 DELETION
SEQADV 4XV8 A UNP P00431 ALA 260 DELETION
SEQRES 1 A 292 MET LYS THR LEU VAL HIS VAL ALA SER VAL GLU LYS GLY
SEQRES 2 A 292 ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE
SEQRES 3 A 292 ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR
SEQRES 4 A 292 ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS
SEQRES 5 A 292 ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR GLY GLY
SEQRES 6 A 292 SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU PHE ASN
SEQRES 7 A 292 ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE
SEQRES 8 A 292 LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE SER SER
SEQRES 9 A 292 GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA VAL GLN
SEQRES 10 A 292 GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG
SEQRES 11 A 292 VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN GLY ARG
SEQRES 12 A 292 LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL ARG THR
SEQRES 13 A 292 PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU VAL VAL
SEQRES 14 A 292 ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR HIS LEU
SEQRES 15 A 292 LYS ASN SER GLY TYR GLU GLY GLY GLY ALA ASN ASN VAL
SEQRES 16 A 292 PHE THR ASN GLU PHE TYR LEU ASN LEU LEU ASN GLU ASP
SEQRES 17 A 292 TRP LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU GLN TRP
SEQRES 18 A 292 ASP SER LYS SER GLY TYR MET MET LEU PRO THR ASP TYR
SEQRES 19 A 292 SER LEU ILE GLN ASP PRO LYS TYR LEU SER ILE VAL LYS
SEQRES 20 A 292 GLU TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS ASP PHE
SEQRES 21 A 292 SER LYS ALA PHE GLU LYS LEU LEU GLU ASN GLY ILE THR
SEQRES 22 A 292 PHE PRO LYS ASP ALA PRO SER PRO PHE ILE PHE LYS THR
SEQRES 23 A 292 LEU GLU GLU GLN GLY LEU
HET HEM A 301 43
HET BEN A 302 9
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM BEN BENZAMIDINE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 BEN C7 H8 N2
FORMUL 4 HOH *295(H2 O)
HELIX 1 AA1 SER A 15 ASP A 33 1 19
HELIX 2 AA2 GLU A 35 ILE A 40 1 6
HELIX 3 AA3 TYR A 42 GLY A 55 1 14
HELIX 4 AA4 GLY A 69 ARG A 72 5 4
HELIX 5 AA5 PHE A 73 ASN A 78 1 6
HELIX 6 AA6 ASP A 79 GLY A 84 5 6
HELIX 7 AA7 LEU A 85 PHE A 99 1 15
HELIX 8 AA8 SER A 103 MET A 119 1 17
HELIX 9 AA9 PRO A 134 THR A 138 5 5
HELIX 10 AB1 ASP A 150 ARG A 160 1 11
HELIX 11 AB2 ASN A 164 GLY A 173 1 10
HELIX 12 AB3 ALA A 174 LEU A 177 5 4
HELIX 13 AB4 HIS A 181 GLY A 186 1 6
HELIX 14 AB5 ASN A 198 GLU A 207 1 10
HELIX 15 AB6 LEU A 230 ASP A 239 1 10
HELIX 16 AB7 ASP A 239 ASN A 251 1 13
HELIX 17 AB8 ASP A 252 ASN A 270 1 19
HELIX 18 AB9 THR A 286 GLY A 291 1 6
SHEET 1 AA1 2 HIS A 6 VAL A 7 0
SHEET 2 AA1 2 ILE A 272 THR A 273 1 O THR A 273 N HIS A 6
SHEET 1 AA2 3 LYS A 210 LYS A 213 0
SHEET 2 AA2 3 GLU A 219 ASP A 222 -1 O ASP A 222 N LYS A 210
SHEET 3 AA2 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 2.22
LINK FE HEM A 301 O HOH A 459 1555 1555 2.19
SITE 1 AC1 23 PRO A 44 ARG A 48 TRP A 51 PRO A 145
SITE 2 AC1 23 ASP A 146 ALA A 147 LEU A 171 ALA A 174
SITE 3 AC1 23 HIS A 175 LEU A 177 GLY A 178 LYS A 179
SITE 4 AC1 23 THR A 180 HIS A 181 ASN A 184 SER A 185
SITE 5 AC1 23 LEU A 230 THR A 232 BEN A 302 HOH A 459
SITE 6 AC1 23 HOH A 471 HOH A 500 HOH A 504
SITE 1 AC2 8 HIS A 175 LEU A 177 MET A 228 MET A 229
SITE 2 AC2 8 ASP A 233 HEM A 301 HOH A 475 HOH A 485
CRYST1 51.460 76.950 107.710 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 0.019433 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012995 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009284 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
