HEADER OXYGEN STORAGE/TRANSPORT 13-DEC-04 1Y8I
TITLE HORSE METHEMOGLOBIN LOW SALT, PH 7.0 (98% RELATIVE HUMIDITY)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAINS;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: SLOW AND FAST;
COMPND 5 OTHER_DETAILS: PH 7.0 AQUOMET STRUCTURE;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HEMOGLOBIN BETA CHAIN;
COMPND 8 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 7 ORGANISM_COMMON: HORSE;
SOURCE 8 ORGANISM_TAXID: 9796
KEYWDS AQUO METHEMOGLOBIN, QUARTERNARY ASSOCIATION, ALLOSTERIC TRANSITION,
KEYWDS 2 PROTEIN HYDRATION, OXYGEN STORAGE-TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SANKARANARAYANAN,B.K.BISWAL,M.VIJAYAN
REVDAT 3 23-AUG-23 1Y8I 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Y8I 1 VERSN
REVDAT 1 26-JUL-05 1Y8I 0
JRNL AUTH R.SANKARANARAYANAN,B.K.BISWAL,M.VIJAYAN
JRNL TITL A NEW RELAXED STATE IN HORSE METHEMOGLOBIN CHARACTERIZED BY
JRNL TITL 2 CRYSTALLOGRAPHIC STUDIES.
JRNL REF PROTEINS V. 60 547 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15887226
JRNL DOI 10.1002/PROT.20510
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.K.BISWAL,M.VIJAYAN
REMARK 1 TITL STRUCTURE OF HUMAN METHAEMOGLOBIN: THE VARIATION OF A THEME
REMARK 1 REF CURR.SCI. V. 81 1100 2001
REMARK 1 REFN ISSN 0011-3891
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.K.BISWAL,M.VIJAYAN
REMARK 1 TITL STRUCTURES OF HUMAN OXY- AND DEOXYHAEMOGLOBIN AT DIFFERENT
REMARK 1 TITL 2 LEVELS OF HUMIDITY: VARIABILITY IN THE T STATE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 1155 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.4
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 231708.250
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 17215
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) : 0.167
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT : 999
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2500
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4406
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.91000
REMARK 3 B22 (A**2) : 7.11000
REMARK 3 B33 (A**2) : -3.20000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.120
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 48.25
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 : PARAM19X.HEME
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TOPH19X.HEME
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14300
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47400
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: AMORE
REMARK 200 STARTING MODEL: HORSE METHEMOGLOBIN, PDB ENTRY 2MHB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M PHOSPHATE BUFFER, 30% PEG 3350,
REMARK 280 PH 7.0, LIQUID DIFFUSION, TEMPERATURE 293K
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 31.39900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.07950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.45350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.07950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.39900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.45350
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 B 79 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TYR C 140 N - CA - C ANGL. DEV. = 20.3 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 LEU A 2 89.68 62.36
REMARK 500 HIS A 72 49.90 -142.70
REMARK 500 LYS A 139 58.27 -141.21
REMARK 500 GLU B 22 -71.01 -96.53
REMARK 500 HIS B 77 48.03 -90.61
REMARK 500 ASP B 79 52.73 -104.80
REMARK 500 ASN B 80 60.77 173.98
REMARK 500 HIS B 97 43.97 71.18
REMARK 500 ASP C 75 65.68 -154.36
REMARK 500 LYS C 139 67.59 -107.66
REMARK 500 TYR C 140 -148.57 -93.29
REMARK 500 GLN D 2 99.76 71.70
REMARK 500 HIS D 77 45.13 -141.43
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 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 142 NA 88.9
REMARK 620 3 HEM A 142 NB 85.4 90.8
REMARK 620 4 HEM A 142 NC 87.5 176.4 89.0
REMARK 620 5 HEM A 142 ND 95.3 91.1 177.9 89.1
REMARK 620 6 HOH A 900 O 170.5 98.6 88.6 85.0 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 147 NA 94.0
REMARK 620 3 HEM B 147 NB 90.9 89.0
REMARK 620 4 HEM B 147 NC 92.6 173.2 89.8
REMARK 620 5 HEM B 147 ND 95.9 91.1 173.2 89.3
REMARK 620 6 HOH B 901 O 168.3 92.0 79.2 81.2 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HEM C 142 NA 92.7
REMARK 620 3 HEM C 142 NB 91.3 89.4
REMARK 620 4 HEM C 142 NC 87.5 179.8 90.7
REMARK 620 5 HEM C 142 ND 93.3 89.9 175.3 90.0
REMARK 620 6 HOH C 902 O 171.4 95.3 92.1 84.6 83.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HEM D 147 NA 95.8
REMARK 620 3 HEM D 147 NB 90.9 88.2
REMARK 620 4 HEM D 147 NC 87.9 176.3 91.4
REMARK 620 5 HEM D 147 ND 87.4 91.1 178.1 89.5
REMARK 620 6 HOH D 903 O 172.0 92.1 87.6 84.3 94.2
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 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 147
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JY7 RELATED DB: PDB
REMARK 900 RELATED ID: 1LFQ RELATED DB: PDB
REMARK 900 RELATED ID: 1Y8H RELATED DB: PDB
REMARK 900 RELATED ID: 1Y8K RELATED DB: PDB
DBREF 1Y8I A 1 141 UNP P01958 HBA_HORSE 1 141
DBREF 1Y8I C 1 141 UNP P01958 HBA_HORSE 1 141
DBREF 1Y8I B 1 146 UNP P02062 HBB_HORSE 1 146
DBREF 1Y8I D 1 146 UNP P02062 HBB_HORSE 1 146
SEQADV 1Y8I ASP A 82 UNP P01958 ASN 82 CONFLICT
SEQADV 1Y8I ASN A 85 UNP P01958 ASP 85 CONFLICT
SEQADV 1Y8I ASP C 82 UNP P01958 ASN 82 CONFLICT
SEQADV 1Y8I ASN C 85 UNP P01958 ASP 85 CONFLICT
SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP SER LYS VAL GLY GLY HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU GLY PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL GLY ASP ALA
SEQRES 6 A 141 LEU THR LEU ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY
SEQRES 7 A 141 ALA LEU SER ASP LEU SER ASN LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU SER THR LEU ALA VAL HIS LEU PRO ASN ASP PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU SER
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL GLN LEU SER GLY GLU GLU LYS ALA ALA VAL LEU ALA
SEQRES 2 B 146 LEU TRP ASP LYS VAL ASN GLU GLU GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER ASN PRO GLY
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU HIS SER PHE GLY GLU GLY VAL HIS HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG HIS
SEQRES 10 B 146 PHE GLY LYS ASP PHE THR PRO GLU LEU GLN ALA SER TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP SER LYS VAL GLY GLY HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU GLY PHE PRO THR THR
SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 C 141 ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL GLY ASP ALA
SEQRES 6 C 141 LEU THR LEU ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY
SEQRES 7 C 141 ALA LEU SER ASP LEU SER ASN LEU HIS ALA HIS LYS LEU
SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 C 141 LEU LEU SER THR LEU ALA VAL HIS LEU PRO ASN ASP PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU SER
SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 146 VAL GLN LEU SER GLY GLU GLU LYS ALA ALA VAL LEU ALA
SEQRES 2 D 146 LEU TRP ASP LYS VAL ASN GLU GLU GLU VAL GLY GLY GLU
SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 D 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER ASN PRO GLY
SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 D 146 LYS VAL LEU HIS SER PHE GLY GLU GLY VAL HIS HIS LEU
SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU
SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG HIS
SEQRES 10 D 146 PHE GLY LYS ASP PHE THR PRO GLU LEU GLN ALA SER TYR
SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 D 146 LYS TYR HIS
HET HEM A 142 43
HET HEM B 147 43
HET HEM C 142 43
HET HEM D 147 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 HOH *304(H2 O)
HELIX 1 1 SER A 3 GLY A 18 1 16
HELIX 2 2 HIS A 20 PHE A 36 1 17
HELIX 3 3 PRO A 37 PHE A 43 5 7
HELIX 4 4 SER A 52 GLY A 71 1 20
HELIX 5 5 ASP A 75 LEU A 80 1 6
HELIX 6 6 LEU A 80 HIS A 89 1 10
HELIX 7 7 PRO A 95 LEU A 113 1 19
HELIX 8 8 THR A 118 SER A 138 1 21
HELIX 9 9 SER B 4 LYS B 17 1 14
HELIX 10 10 GLU B 22 TYR B 35 1 14
HELIX 11 11 PRO B 36 GLY B 46 5 11
HELIX 12 12 ASN B 50 ASN B 57 1 8
HELIX 13 13 ASN B 57 HIS B 77 1 21
HELIX 14 14 ASN B 80 PHE B 85 1 6
HELIX 15 15 PHE B 85 LYS B 95 1 11
HELIX 16 16 PRO B 100 GLY B 119 1 20
HELIX 17 17 LYS B 120 PHE B 122 5 3
HELIX 18 18 THR B 123 ALA B 142 1 20
HELIX 19 19 SER C 3 GLY C 18 1 16
HELIX 20 20 HIS C 20 PHE C 36 1 17
HELIX 21 21 PRO C 37 PHE C 43 5 7
HELIX 22 22 SER C 52 HIS C 72 1 21
HELIX 23 23 ASP C 75 LEU C 80 1 6
HELIX 24 24 LEU C 80 HIS C 89 1 10
HELIX 25 25 PRO C 95 LEU C 113 1 19
HELIX 26 26 THR C 118 SER C 138 1 21
HELIX 27 27 SER D 4 ASP D 16 1 13
HELIX 28 28 ASN D 19 TYR D 35 1 17
HELIX 29 29 PRO D 36 GLY D 46 5 11
HELIX 30 30 ASN D 50 ASN D 57 1 8
HELIX 31 31 ASN D 57 HIS D 76 1 20
HELIX 32 32 ASN D 80 ASP D 94 1 15
HELIX 33 33 PRO D 100 GLY D 119 1 20
HELIX 34 34 LYS D 120 PHE D 122 5 3
HELIX 35 35 THR D 123 ALA D 142 1 20
HELIX 36 36 HIS D 143 HIS D 146 5 4
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.17
LINK FE HEM A 142 O HOH A 900 1555 1555 2.14
LINK NE2 HIS B 92 FE HEM B 147 1555 1555 2.11
LINK FE HEM B 147 O HOH B 901 1555 1555 2.13
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.11
LINK FE HEM C 142 O HOH C 902 1555 1555 2.14
LINK NE2 HIS D 92 FE HEM D 147 1555 1555 2.11
LINK FE HEM D 147 O HOH D 903 1555 1555 2.15
SITE 1 AC1 12 TYR A 42 PHE A 43 HIS A 45 HIS A 58
SITE 2 AC1 12 LYS A 61 HIS A 87 LEU A 91 VAL A 93
SITE 3 AC1 12 PHE A 98 LEU A 136 HOH A 190 HOH A 900
SITE 1 AC2 11 PHE B 41 PHE B 42 HIS B 63 LYS B 66
SITE 2 AC2 11 SER B 70 PHE B 71 HIS B 92 VAL B 98
SITE 3 AC2 11 ASN B 102 LEU B 141 HOH B 901
SITE 1 AC3 13 TYR C 42 PHE C 43 HIS C 45 PHE C 46
SITE 2 AC3 13 HIS C 58 LYS C 61 LEU C 83 HIS C 87
SITE 3 AC3 13 LEU C 91 VAL C 93 PHE C 98 LEU C 101
SITE 4 AC3 13 HOH C 902
SITE 1 AC4 12 LYS C 11 PHE D 41 HIS D 63 PHE D 71
SITE 2 AC4 12 HIS D 92 LEU D 96 ASN D 102 LEU D 106
SITE 3 AC4 12 LEU D 141 HOH D 235 HOH D 328 HOH D 903
CRYST1 62.798 80.907 112.159 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 0.015924 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012360 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008916 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
