HEADER LYASE 06-MAY-09 3HCN
TITLE HG AND PROTOPORPHYRIN BOUND HUMAN FERROCHELATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERROCHELATASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 65-423;
COMPND 5 SYNONYM: PROTOHEME FERRO-LYASE, HEME SYNTHETASE;
COMPND 6 EC: 4.99.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HEMH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERROCHELATASE, METAL SELECTIVITY, DISEASE MUTATION, HEME
KEYWDS 2 BIOSYNTHESIS, IRON, IRON-SULFUR, LYASE, MEMBRANE, METAL-BINDING,
KEYWDS 3 MITOCHONDRION, MITOCHONDRION INNER MEMBRANE, PORPHYRIN BIOSYNTHESIS,
KEYWDS 4 TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.MEDLOCK,H.A.DAILEY,W.N.LANZILOTTA
REVDAT 3 21-FEB-24 3HCN 1 REMARK LINK
REVDAT 2 13-JUL-11 3HCN 1 VERSN
REVDAT 1 10-NOV-09 3HCN 0
JRNL AUTH A.E.MEDLOCK,M.CARTER,T.A.DAILEY,H.A.DAILEY,W.N.LANZILOTTA
JRNL TITL PRODUCT RELEASE RATHER THAN CHELATION DETERMINES METAL
JRNL TITL 2 SPECIFICITY FOR FERROCHELATASE.
JRNL REF J.MOL.BIOL. V. 393 308 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19703464
JRNL DOI 10.1016/J.JMB.2009.08.042
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 453335.480
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 219931
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) : 0.214
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 10806
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 32703
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1695
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 245
REMARK 3 SOLVENT ATOMS : 798
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.92000
REMARK 3 B22 (A**2) : -4.74000
REMARK 3 B33 (A**2) : 8.66000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.760 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.800 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.670 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 60.59
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : FES.PARAM
REMARK 3 PARAMETER FILE 4 : HEME.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : FES.TOP
REMARK 3 TOPOLOGY FILE 4 : HEME.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3HCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 86.479
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : 1.0
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 224027
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.2000
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) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : 0.24000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M AMMONIUM SULFATE, 0.1 M BIS
REMARK 280 -TRIS PH 6.5, 20 % PENTAERYTHRITOLETHYLOXYLATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
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 43.23950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.68000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.48200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.68000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.23950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.48200
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 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 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 ILE A 103 53.39 34.63
REMARK 500 THR A 198 -84.48 -112.56
REMARK 500 THR A 198 -85.28 -112.56
REMARK 500 TRP A 227 54.46 -165.00
REMARK 500 SER A 303 -92.27 -126.01
REMARK 500 SER A 303 11.05 49.03
REMARK 500 LYS A 304 152.69 -45.27
REMARK 500 ASN A 372 -114.31 23.07
REMARK 500 ILE B 603 51.74 35.51
REMARK 500 THR B 698 -86.23 -111.46
REMARK 500 TRP B 727 54.75 -165.82
REMARK 500 SER B 803 18.52 57.00
REMARK 500 ASN B 872 -108.86 29.40
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 424 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BCT A 1 O2
REMARK 620 2 HEM A 424 NA 96.0
REMARK 620 3 HEM A 424 NB 89.4 89.4
REMARK 620 4 HEM A 424 NC 82.4 178.4 90.6
REMARK 620 5 HEM A 424 ND 89.0 88.9 177.6 91.0
REMARK 620 6 IMD A 2 N1 173.1 90.8 89.4 90.8 92.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 196 SG
REMARK 620 2 FES A 501 S1 111.5
REMARK 620 3 FES A 501 S2 111.1 104.8
REMARK 620 4 CYS A 403 SG 96.9 109.9 122.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 406 SG
REMARK 620 2 FES A 501 S1 111.7
REMARK 620 3 FES A 501 S2 112.2 104.4
REMARK 620 4 CYS A 411 SG 104.1 107.0 117.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 926 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 IMD B 3 N1
REMARK 620 2 HEM B 926 NA 93.3
REMARK 620 3 HEM B 926 NB 91.1 88.4
REMARK 620 4 HEM B 926 NC 86.9 179.2 90.8
REMARK 620 5 HEM B 926 ND 88.7 90.5 178.9 90.3
REMARK 620 6 IMD B 925 N1 173.7 92.9 89.2 86.8 91.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 696 SG
REMARK 620 2 FES B 502 S1 110.6
REMARK 620 3 FES B 502 S2 111.3 104.8
REMARK 620 4 CYS B 903 SG 96.9 111.3 121.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 906 SG
REMARK 620 2 FES B 502 S1 111.9
REMARK 620 3 FES B 502 S2 110.9 104.6
REMARK 620 4 CYS B 911 SG 105.1 106.6 117.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 424
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 924
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 925
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 926
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 927
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HCO RELATED DB: PDB
REMARK 900 RELATED ID: 3HCP RELATED DB: PDB
REMARK 900 RELATED ID: 3HCR RELATED DB: PDB
DBREF 3HCN A 65 423 UNP P22830 HEMH_HUMAN 65 423
DBREF 3HCN B 565 923 UNP P22830 HEMH_HUMAN 65 423
SEQRES 1 A 359 ARG LYS PRO LYS THR GLY ILE LEU MET LEU ASN MET GLY
SEQRES 2 A 359 GLY PRO GLU THR LEU GLY ASP VAL HIS ASP PHE LEU LEU
SEQRES 3 A 359 ARG LEU PHE LEU ASP ARG ASP LEU MET THR LEU PRO ILE
SEQRES 4 A 359 GLN ASN LYS LEU ALA PRO PHE ILE ALA LYS ARG ARG THR
SEQRES 5 A 359 PRO LYS ILE GLN GLU GLN TYR ARG ARG ILE GLY GLY GLY
SEQRES 6 A 359 SER PRO ILE LYS ILE TRP THR SER LYS GLN GLY GLU GLY
SEQRES 7 A 359 MET VAL LYS LEU LEU ASP GLU LEU SER PRO ASN THR ALA
SEQRES 8 A 359 PRO HIS LYS TYR TYR ILE GLY PHE ARG TYR VAL HIS PRO
SEQRES 9 A 359 LEU THR GLU GLU ALA ILE GLU GLU MET GLU ARG ASP GLY
SEQRES 10 A 359 LEU GLU ARG ALA ILE ALA PHE THR GLN TYR PRO GLN TYR
SEQRES 11 A 359 SER CYS SER THR THR GLY SER SER LEU ASN ALA ILE TYR
SEQRES 12 A 359 ARG TYR TYR ASN GLN VAL GLY ARG LYS PRO THR MET LYS
SEQRES 13 A 359 TRP SER THR ILE ASP ARG TRP PRO THR HIS HIS LEU LEU
SEQRES 14 A 359 ILE GLN CYS PHE ALA ASP HIS ILE LEU LYS GLU LEU ASP
SEQRES 15 A 359 HIS PHE PRO LEU GLU LYS ARG SER GLU VAL VAL ILE LEU
SEQRES 16 A 359 PHE SER ALA HIS SER LEU PRO MET SER VAL VAL ASN ARG
SEQRES 17 A 359 GLY ASP PRO TYR PRO GLN GLU VAL SER ALA THR VAL GLN
SEQRES 18 A 359 LYS VAL MET GLU ARG LEU GLU TYR CYS ASN PRO TYR ARG
SEQRES 19 A 359 LEU VAL TRP GLN SER LYS VAL GLY PRO MET PRO TRP LEU
SEQRES 20 A 359 GLY PRO GLN THR ASP GLU SER ILE LYS GLY LEU CYS GLU
SEQRES 21 A 359 ARG GLY ARG LYS ASN ILE LEU LEU VAL PRO ILE ALA PHE
SEQRES 22 A 359 THR SER ASP HIS ILE GLU THR LEU TYR GLU LEU ASP ILE
SEQRES 23 A 359 GLU TYR SER GLN VAL LEU ALA LYS GLU CYS GLY VAL GLU
SEQRES 24 A 359 ASN ILE ARG ARG ALA GLU SER LEU ASN GLY ASN PRO LEU
SEQRES 25 A 359 PHE SER LYS ALA LEU ALA ASP LEU VAL HIS SER HIS ILE
SEQRES 26 A 359 GLN SER ASN GLU LEU CYS SER LYS GLN LEU THR LEU SER
SEQRES 27 A 359 CYS PRO LEU CYS VAL ASN PRO VAL CYS ARG GLU THR LYS
SEQRES 28 A 359 SER PHE PHE THR SER GLN GLN LEU
SEQRES 1 B 359 ARG LYS PRO LYS THR GLY ILE LEU MET LEU ASN MET GLY
SEQRES 2 B 359 GLY PRO GLU THR LEU GLY ASP VAL HIS ASP PHE LEU LEU
SEQRES 3 B 359 ARG LEU PHE LEU ASP ARG ASP LEU MET THR LEU PRO ILE
SEQRES 4 B 359 GLN ASN LYS LEU ALA PRO PHE ILE ALA LYS ARG ARG THR
SEQRES 5 B 359 PRO LYS ILE GLN GLU GLN TYR ARG ARG ILE GLY GLY GLY
SEQRES 6 B 359 SER PRO ILE LYS ILE TRP THR SER LYS GLN GLY GLU GLY
SEQRES 7 B 359 MET VAL LYS LEU LEU ASP GLU LEU SER PRO ASN THR ALA
SEQRES 8 B 359 PRO HIS LYS TYR TYR ILE GLY PHE ARG TYR VAL HIS PRO
SEQRES 9 B 359 LEU THR GLU GLU ALA ILE GLU GLU MET GLU ARG ASP GLY
SEQRES 10 B 359 LEU GLU ARG ALA ILE ALA PHE THR GLN TYR PRO GLN TYR
SEQRES 11 B 359 SER CYS SER THR THR GLY SER SER LEU ASN ALA ILE TYR
SEQRES 12 B 359 ARG TYR TYR ASN GLN VAL GLY ARG LYS PRO THR MET LYS
SEQRES 13 B 359 TRP SER THR ILE ASP ARG TRP PRO THR HIS HIS LEU LEU
SEQRES 14 B 359 ILE GLN CYS PHE ALA ASP HIS ILE LEU LYS GLU LEU ASP
SEQRES 15 B 359 HIS PHE PRO LEU GLU LYS ARG SER GLU VAL VAL ILE LEU
SEQRES 16 B 359 PHE SER ALA HIS SER LEU PRO MET SER VAL VAL ASN ARG
SEQRES 17 B 359 GLY ASP PRO TYR PRO GLN GLU VAL SER ALA THR VAL GLN
SEQRES 18 B 359 LYS VAL MET GLU ARG LEU GLU TYR CYS ASN PRO TYR ARG
SEQRES 19 B 359 LEU VAL TRP GLN SER LYS VAL GLY PRO MET PRO TRP LEU
SEQRES 20 B 359 GLY PRO GLN THR ASP GLU SER ILE LYS GLY LEU CYS GLU
SEQRES 21 B 359 ARG GLY ARG LYS ASN ILE LEU LEU VAL PRO ILE ALA PHE
SEQRES 22 B 359 THR SER ASP HIS ILE GLU THR LEU TYR GLU LEU ASP ILE
SEQRES 23 B 359 GLU TYR SER GLN VAL LEU ALA LYS GLU CYS GLY VAL GLU
SEQRES 24 B 359 ASN ILE ARG ARG ALA GLU SER LEU ASN GLY ASN PRO LEU
SEQRES 25 B 359 PHE SER LYS ALA LEU ALA ASP LEU VAL HIS SER HIS ILE
SEQRES 26 B 359 GLN SER ASN GLU LEU CYS SER LYS GLN LEU THR LEU SER
SEQRES 27 B 359 CYS PRO LEU CYS VAL ASN PRO VAL CYS ARG GLU THR LYS
SEQRES 28 B 359 SER PHE PHE THR SER GLN GLN LEU
HET FES A 501 4
HET CHD A 3 29
HET CHD A 4 29
HET IMD A 2 5
HET BCT A 1 4
HET HEM A 424 43
HET SO4 A 425 5
HET FES B 502 4
HET CHD B 1 29
HET CHD B 2 29
HET GOL B 924 12
HET IMD B 925 5
HET IMD B 3 5
HET HEM B 926 43
HET SO4 B 927 5
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM CHD CHOLIC ACID
HETNAM IMD IMIDAZOLE
HETNAM BCT BICARBONATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FES 2(FE2 S2)
FORMUL 4 CHD 4(C24 H40 O5)
FORMUL 6 IMD 3(C3 H5 N2 1+)
FORMUL 7 BCT C H O3 1-
FORMUL 8 HEM 2(C34 H32 FE N4 O4)
FORMUL 9 SO4 2(O4 S 2-)
FORMUL 13 GOL C3 H8 O3
FORMUL 18 HOH *798(H2 O)
HELIX 1 1 THR A 81 GLY A 83 5 3
HELIX 2 2 ASP A 84 LEU A 94 1 11
HELIX 3 3 ILE A 103 ILE A 126 1 24
HELIX 4 4 PRO A 131 SER A 151 1 21
HELIX 5 5 PRO A 152 ALA A 155 5 4
HELIX 6 6 LEU A 169 ASP A 180 1 12
HELIX 7 7 THR A 198 VAL A 213 1 16
HELIX 8 8 HIS A 230 ASP A 246 1 17
HELIX 9 9 LYS A 252 VAL A 256 5 5
HELIX 10 10 PRO A 266 ASN A 271 1 6
HELIX 11 11 PRO A 275 LEU A 291 1 17
HELIX 12 12 GLN A 314 ARG A 325 1 12
HELIX 13 13 THR A 344 ASP A 349 1 6
HELIX 14 14 ASP A 349 CYS A 360 1 12
HELIX 15 15 ASN A 374 ASN A 392 1 19
HELIX 16 16 SER A 396 LEU A 401 5 6
HELIX 17 17 PRO A 409 SER A 420 1 12
HELIX 18 18 THR B 581 GLY B 583 5 3
HELIX 19 19 ASP B 584 LEU B 594 1 11
HELIX 20 20 ILE B 603 ILE B 626 1 24
HELIX 21 21 PRO B 631 SER B 651 1 21
HELIX 22 22 PRO B 652 ALA B 655 5 4
HELIX 23 23 LEU B 669 ASP B 680 1 12
HELIX 24 24 THR B 698 GLY B 714 1 17
HELIX 25 25 HIS B 730 ASP B 746 1 17
HELIX 26 26 HIS B 747 PHE B 748 5 2
HELIX 27 27 PRO B 749 VAL B 756 5 8
HELIX 28 28 PRO B 766 ASN B 771 1 6
HELIX 29 29 PRO B 775 LEU B 791 1 17
HELIX 30 30 GLN B 814 ARG B 825 1 12
HELIX 31 31 THR B 844 ASP B 849 1 6
HELIX 32 32 ASP B 849 CYS B 860 1 12
HELIX 33 33 ASN B 874 ASN B 892 1 19
HELIX 34 34 LYS B 897 LEU B 901 5 5
HELIX 35 35 PRO B 909 SER B 920 1 12
SHEET 1 A 4 HIS A 157 PHE A 163 0
SHEET 2 A 4 THR A 69 ASN A 75 1 N MET A 73 O TYR A 160
SHEET 3 A 4 ARG A 184 THR A 189 1 O ARG A 184 N GLY A 70
SHEET 4 A 4 LYS A 220 ILE A 224 1 O LYS A 220 N ALA A 185
SHEET 1 B 4 TYR A 297 GLN A 302 0
SHEET 2 B 4 VAL A 257 HIS A 263 1 N PHE A 260 O VAL A 300
SHEET 3 B 4 ASN A 329 VAL A 333 1 O LEU A 331 N LEU A 259
SHEET 4 B 4 ASN A 364 ARG A 367 1 O ARG A 366 N LEU A 332
SHEET 1 C 4 HIS B 657 PHE B 663 0
SHEET 2 C 4 THR B 569 ASN B 575 1 N MET B 573 O TYR B 660
SHEET 3 C 4 ARG B 684 THR B 689 1 O ARG B 684 N GLY B 570
SHEET 4 C 4 LYS B 720 ILE B 724 1 O LYS B 720 N ALA B 685
SHEET 1 D 4 TYR B 797 GLN B 802 0
SHEET 2 D 4 VAL B 757 HIS B 763 1 N PHE B 760 O VAL B 800
SHEET 3 D 4 ASN B 829 VAL B 833 1 O LEU B 831 N LEU B 759
SHEET 4 D 4 ASN B 864 ARG B 867 1 O ARG B 866 N LEU B 832
LINK O2 BCT A 1 FE HEM A 424 1555 1555 2.59
LINK N1 IMD A 2 FE HEM A 424 1555 1555 2.16
LINK SG CYS A 196 FE2 FES A 501 1555 1555 2.30
LINK SG CYS A 403 FE2 FES A 501 1555 1555 2.33
LINK SG CYS A 406 FE1 FES A 501 1555 1555 2.32
LINK SG CYS A 411 FE1 FES A 501 1555 1555 2.35
LINK N1 IMD B 3 FE HEM B 926 1555 1555 2.33
LINK FE2 FES B 502 SG CYS B 696 1555 1555 2.31
LINK FE2 FES B 502 SG CYS B 903 1555 1555 2.35
LINK FE1 FES B 502 SG CYS B 906 1555 1555 2.32
LINK FE1 FES B 502 SG CYS B 911 1555 1555 2.34
LINK N1 IMD B 925 FE HEM B 926 1555 1555 2.28
CISPEP 1 ALA A 155 PRO A 156 0 0.00
CISPEP 2 HIS A 167 PRO A 168 0 -0.20
CISPEP 3 GLY A 312 PRO A 313 0 0.16
CISPEP 4 ALA B 655 PRO B 656 0 0.12
CISPEP 5 HIS B 667 PRO B 668 0 -0.03
CISPEP 6 GLY B 812 PRO B 813 0 0.13
SITE 1 AC1 5 CYS A 196 SER A 402 CYS A 403 CYS A 406
SITE 2 AC1 5 CYS A 411
SITE 1 AC2 10 CHD A 4 THR A 100 LEU A 101 ARG A 115
SITE 2 AC2 10 PRO A 266 VAL A 305 GLY A 306 MET A 308
SITE 3 AC2 10 HEM A 424 HOH A 447
SITE 1 AC3 4 CHD A 3 LEU A 101 LYS B 606 PHE B 610
SITE 1 AC4 5 HIS A 263 SER A 264 GLN A 302 SER A 303
SITE 2 AC4 5 HEM A 424
SITE 1 AC5 7 MET A 76 LEU A 98 TYR A 165 TYR A 191
SITE 2 AC5 7 SER A 197 THR A 198 HEM A 424
SITE 1 AC6 24 BCT A 1 IMD A 2 CHD A 3 HOH A 39
SITE 2 AC6 24 MET A 76 LEU A 92 PHE A 93 LEU A 98
SITE 3 AC6 24 ARG A 115 ILE A 119 TYR A 123 SER A 197
SITE 4 AC6 24 THR A 198 HIS A 263 LEU A 265 PRO A 266
SITE 5 AC6 24 TYR A 276 VAL A 305 ALA A 336 HIS A 341
SITE 6 AC6 24 ILE A 342 HOH A 432 HOH A 541 HOH A 672
SITE 1 AC7 4 ARG A 115 LYS A 118 LYS A 304 VAL A 305
SITE 1 AC8 6 CYS B 696 ARG B 772 SER B 902 CYS B 903
SITE 2 AC8 6 CYS B 906 CYS B 911
SITE 1 AC9 14 CHD B 2 HOH B 52 HOH B 164 HOH B 314
SITE 2 AC9 14 HOH B 315 HOH B 316 HOH B 447 LEU B 601
SITE 3 AC9 14 ARG B 614 ARG B 615 PRO B 766 SER B 768
SITE 4 AC9 14 GLY B 806 HEM B 926
SITE 1 BC1 6 LYS A 106 CHD B 1 HOH B 315 LEU B 601
SITE 2 BC1 6 PHE B 610 ARG B 614
SITE 1 BC2 12 HOH A 29 HOH A 33 PRO A 277 GLN A 278
SITE 2 BC2 12 SER A 281 TRP A 301 HOH B 32 PRO B 777
SITE 3 BC2 12 GLN B 778 SER B 781 TRP B 801 LEU B 811
SITE 1 BC3 5 HIS B 763 SER B 764 SER B 803 TRP B 810
SITE 2 BC3 5 HEM B 926
SITE 1 BC4 6 HOH B 92 MET B 576 LEU B 598 TYR B 665
SITE 2 BC4 6 SER B 697 HEM B 926
SITE 1 BC5 22 CHD B 1 IMD B 3 HOH B 48 HOH B 80
SITE 2 BC5 22 HOH B 540 MET B 576 LEU B 592 PHE B 593
SITE 3 BC5 22 ARG B 615 ILE B 619 TYR B 623 TYR B 691
SITE 4 BC5 22 SER B 697 THR B 698 HIS B 763 LEU B 765
SITE 5 BC5 22 PRO B 766 VAL B 805 ALA B 836 HIS B 841
SITE 6 BC5 22 ILE B 842 IMD B 925
SITE 1 BC6 4 ARG B 615 LYS B 618 VAL B 805 GLY B 806
CRYST1 86.479 92.964 109.360 90.00 90.00 90.00 P 21 21 21 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 0.011564 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010757 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
