HEADER OXYGEN STORAGE, OXYGEN TRANSPORT 15-MAY-08 3D4X
TITLE CRYSTAL STRUCTURE DETERMINATION OF CAT (FELIS SILVESTRIS CATUS)
TITLE 2 HEMOGLOBIN AT 2.2 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: HEMOGLOBIN ALPHA CHAIN, ALPHA-GLOBIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN SUBUNIT BETA-A/B;
COMPND 7 CHAIN: B, D;
COMPND 8 SYNONYM: HEMOGLOBIN BETA-A/B CHAIN, BETA-A/B-GLOBIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FELIS SILVESTRIS CATUS;
SOURCE 3 ORGANISM_COMMON: CAT;
SOURCE 4 ORGANISM_TAXID: 9685;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 CELL: RED BLOOD CELLS;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: FELIS SILVESTRIS CATUS;
SOURCE 9 ORGANISM_COMMON: CAT;
SOURCE 10 ORGANISM_TAXID: 9685;
SOURCE 11 TISSUE: BLOOD;
SOURCE 12 CELL: RED BLOOD CELLS
KEYWDS FELIS SILVESTRIS CATUS, MONOCLINIC, HEMOGLOBIN, LOW OXYGEN AFFINITY,
KEYWDS 2 ALLOSTERIC MECHANISM, HEME, IRON, TRANSPORT, OXYGEN STORAGE, OXYGEN
KEYWDS 3 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BALASUBRAMANIAN,P.SATHYA MOORTHY,K.NEELAGANDAN,M.N.PONNUSWAMY
REVDAT 4 01-NOV-23 3D4X 1 REMARK LINK
REVDAT 3 18-DEC-19 3D4X 1 REMARK
REVDAT 2 21-DEC-16 3D4X 1 AUTHOR VERSN
REVDAT 1 19-MAY-09 3D4X 0
JRNL AUTH M.BALASUBRAMANIAN,P.SATHYA MOORTHY,K.NEELAGANDAN,
JRNL AUTH 2 M.N.PONNUSWAMY
JRNL TITL CRYSTAL STRUCTURE DETERMINATION OF CAT (FELIS SILVESTRIS
JRNL TITL 2 CATUS) HEMOGLOBIN AT 2.2 ANGSTROM RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.NEELAGANDAN,P.SATHYA MOORTHY,M.BALASUBRAMANIAN,
REMARK 1 AUTH 2 M.N.PONNUSWAMY
REMARK 1 TITL CRYSTALLIZATION OF SHEEP (OVIS ARIES) AND GOAT (CAPRA
REMARK 1 TITL 2 HIRCUS) HAEMOGLOBINS UNDER UNBUFFERED LOW-SALT CONDITIONS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 887 2007
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 17909297
REMARK 1 DOI 10.1107/S1744309107044296
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.BALASUBRAMANIAN,P.SATHYA MOORTHY,K.NEELAGANDAN,
REMARK 1 AUTH 2 M.N.PONNUSWAMY
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDY OF LOW OXYGEN-AFFINITY HAEMOGLOBIN
REMARK 1 TITL 3 FROM CAT (FELIS SILVESTRIS CATUS) IN TWO DIFFERENT CRYSTAL
REMARK 1 TITL 4 FORMS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 65 313 2009
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 19255493
REMARK 1 DOI 10.1107/S1744309109004503
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.BALASUBRAMANIAN,P.SATHYA MOORTHY,K.NEELAGANDAN,
REMARK 1 AUTH 2 M.N.PONNUSWAMY
REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC STUDY OF HEMOGLOBIN FROM
REMARK 1 TITL 2 BUFFALO (BUBALUS BUBALIS): A LOW OXYGEN AFFINITY SPECIES
REMARK 1 REF PROTEIN PEPT.LETT. V. 16 213 2009
REMARK 1 REFN ISSN 0929-8665
REMARK 1 PMID 19200047
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.SATHYA MOORTHY,K.NEELAGANDAN,M.BALASUBRAMANIAN,
REMARK 1 AUTH 2 M.N.PONNUSWAMY
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY
REMARK 1 TITL 2 DIFFRACTION STUDIES ON GOAT (CAPRA HIRCUS) HEMOGLOBIN - A
REMARK 1 TITL 3 LOW OXYGEN AFFINITY SPECIES
REMARK 1 REF PROTEIN PEPT.LETT. V. 16 454 2009
REMARK 1 REFN ISSN 0929-8665
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 25202
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2838
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1805
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 207
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4404
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 157
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.76000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.40000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.379
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.259
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.223
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4716 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6448 ; 1.319 ; 2.048
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 568 ; 5.466 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;35.713 ;24.082
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 720 ;16.481 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.968 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 682 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3602 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2110 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3187 ; 0.293 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 168 ; 0.167 ; 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): 43 ; 0.294 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.294 ; 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): 2896 ; 0.948 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4526 ; 1.239 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2026 ; 2.154 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1914 ; 3.155 ; 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 : 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 : 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: NULL
REMARK 4
REMARK 4 3D4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-08
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28427
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 2.460
REMARK 200 R MERGE (I) : 0.06850
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30360
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: PDB ENTRY 1HDA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% PEG 3350, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 37.09750
REMARK 290 SMTRY3 2 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
REMARK 350 TOTAL BURIED SURFACE AREA: 10850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL
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: 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 -152.66 -141.32
REMARK 500 PHE A 43 53.01 -116.47
REMARK 500 TYR A 140 102.24 -39.64
REMARK 500 ASP B 80 59.44 -140.73
REMARK 500 TYR D 35 76.01 -113.85
REMARK 500 ASN D 77 42.74 -108.03
REMARK 500 ASP D 80 66.69 -154.64
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 143 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 143 NA 90.7
REMARK 620 3 HEM A 143 NB 84.5 86.2
REMARK 620 4 HEM A 143 NC 89.5 175.7 89.6
REMARK 620 5 HEM A 143 ND 97.8 94.2 177.6 90.0
REMARK 620 6 HOH A 142 O 166.5 97.8 85.6 81.3 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 148 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 148 NA 92.5
REMARK 620 3 HEM B 148 NB 91.6 89.9
REMARK 620 4 HEM B 148 NC 88.8 178.4 89.2
REMARK 620 5 HEM B 148 ND 91.7 86.7 175.4 94.2
REMARK 620 6 HOH B 151 O 172.8 93.8 92.0 85.0 85.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 143 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HEM C 143 NA 86.8
REMARK 620 3 HEM C 143 NB 88.0 88.7
REMARK 620 4 HEM C 143 NC 91.8 178.2 90.0
REMARK 620 5 HEM C 143 ND 93.7 94.3 176.6 87.0
REMARK 620 6 HOH C 142 O 175.5 95.8 88.4 85.5 89.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 148 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HEM D 148 NA 93.7
REMARK 620 3 HEM D 148 NB 92.4 90.9
REMARK 620 4 HEM D 148 NC 83.0 176.5 88.4
REMARK 620 5 HEM D 148 ND 85.9 93.2 175.6 87.4
REMARK 620 6 HOH D 164 O 173.6 92.3 89.9 91.1 91.4
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 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 148
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QU0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE DETERMINATION OF SHEEP METHEMOGLOBIN AT 2.7
REMARK 900 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 2RI4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE DETERMINATION OF GOAT METHEMOGLOBIN AT 2.7
REMARK 900 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 3CY5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE DETERMINATION OF BUFFALO (BUBALUS BUBALIS) AT 2
REMARK 900 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 3D1A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE DETERMINATION OF GOAT HEMOGLOBIN AT 2.61 ANGSTROM
REMARK 900 RESOLUTION
DBREF 3D4X A 1 141 UNP P07405 HBA_FELCA 1 141
DBREF 3D4X B 2 146 UNP P07412 HBB_FELCA 2 146
DBREF 3D4X C 1 141 UNP P07405 HBA_FELCA 1 141
DBREF 3D4X D 2 146 UNP P07412 HBB_FELCA 2 146
SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS SER ASN VAL LYS ALA CYS
SEQRES 2 A 141 TRP GLY LYS ILE GLY SER HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG THR PHE CYS SER 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 GLN LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR GLN ALA VAL ALA HIS MET ASP ASP LEU PRO THR
SEQRES 7 A 141 ALA MET SER ALA LEU SER ASP LEU HIS ALA TYR LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS PHE LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA CYS HIS HIS PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE PHE SER
SEQRES 11 A 141 ALA VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 145 PHE LEU THR ALA GLU GLU LYS GLY LEU VAL ASN GLY LEU
SEQRES 2 B 145 TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU ALA
SEQRES 3 B 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG
SEQRES 4 B 145 PHE PHE GLU SER PHE GLY ASP LEU SER SER ALA ASP ALA
SEQRES 5 B 145 ILE MET SER ASN ALA LYS VAL LYS ALA HIS GLY LYS LYS
SEQRES 6 B 145 VAL LEU ASN SER PHE SER ASP GLY LEU LYS ASN ILE ASP
SEQRES 7 B 145 ASP LEU LYS GLY ALA PHE ALA LYS LEU SER GLU LEU HIS
SEQRES 8 B 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG LEU
SEQRES 9 B 145 LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS PHE
SEQRES 10 B 145 GLY HIS ASP PHE ASN PRO GLN VAL GLN ALA ALA PHE GLN
SEQRES 11 B 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS LYS
SEQRES 12 B 145 TYR HIS
SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS SER ASN VAL LYS ALA CYS
SEQRES 2 C 141 TRP GLY LYS ILE GLY SER HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG THR PHE CYS SER 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 GLN LYS VAL ALA ASP ALA
SEQRES 6 C 141 LEU THR GLN ALA VAL ALA HIS MET ASP ASP LEU PRO THR
SEQRES 7 C 141 ALA MET SER ALA LEU SER ASP LEU HIS ALA TYR LYS LEU
SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS PHE LEU SER HIS CYS
SEQRES 9 C 141 LEU LEU VAL THR LEU ALA CYS HIS HIS PRO ALA GLU PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE PHE SER
SEQRES 11 C 141 ALA VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 145 PHE LEU THR ALA GLU GLU LYS GLY LEU VAL ASN GLY LEU
SEQRES 2 D 145 TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU ALA
SEQRES 3 D 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG
SEQRES 4 D 145 PHE PHE GLU SER PHE GLY ASP LEU SER SER ALA ASP ALA
SEQRES 5 D 145 ILE MET SER ASN ALA LYS VAL LYS ALA HIS GLY LYS LYS
SEQRES 6 D 145 VAL LEU ASN SER PHE SER ASP GLY LEU LYS ASN ILE ASP
SEQRES 7 D 145 ASP LEU LYS GLY ALA PHE ALA LYS LEU SER GLU LEU HIS
SEQRES 8 D 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG LEU
SEQRES 9 D 145 LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS PHE
SEQRES 10 D 145 GLY HIS ASP PHE ASN PRO GLN VAL GLN ALA ALA PHE GLN
SEQRES 11 D 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS LYS
SEQRES 12 D 145 TYR HIS
HET HEM A 143 43
HET HEM B 148 43
HET HEM C 143 43
HET HEM D 148 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 HOH *157(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 HIS A 72 1 21
HELIX 5 5 ASP A 75 MET A 80 1 6
HELIX 6 6 MET A 80 TYR A 89 1 10
HELIX 7 7 PRO A 95 HIS A 113 1 19
HELIX 8 8 THR A 118 THR A 137 1 20
HELIX 9 9 THR B 4 GLY B 16 1 13
HELIX 10 10 ASN B 19 TYR B 35 1 17
HELIX 11 11 PRO B 36 GLY B 46 5 11
HELIX 12 12 SER B 50 ASN B 57 1 8
HELIX 13 13 ASN B 57 ASN B 77 1 21
HELIX 14 14 ASP B 80 LYS B 95 1 16
HELIX 15 15 PRO B 100 GLY B 119 1 20
HELIX 16 16 HIS B 120 PHE B 122 5 3
HELIX 17 17 ASN B 123 HIS B 143 1 21
HELIX 18 18 SER C 3 GLY C 18 1 16
HELIX 19 19 HIS C 20 PHE C 36 1 17
HELIX 20 20 PRO C 37 PHE C 43 5 7
HELIX 21 21 SER C 52 HIS C 72 1 21
HELIX 22 22 ASP C 75 MET C 80 1 6
HELIX 23 23 MET C 80 LYS C 90 1 11
HELIX 24 24 PRO C 95 HIS C 113 1 19
HELIX 25 25 THR C 118 SER C 138 1 21
HELIX 26 26 THR D 4 GLY D 16 1 13
HELIX 27 27 ASN D 19 TYR D 35 1 17
HELIX 28 28 PRO D 36 GLY D 46 5 11
HELIX 29 29 SER D 50 SER D 56 1 7
HELIX 30 30 ASN D 57 ASN D 77 1 21
HELIX 31 31 ASP D 80 LYS D 95 1 16
HELIX 32 32 GLU D 101 GLY D 119 1 19
HELIX 33 33 HIS D 120 PHE D 122 5 3
HELIX 34 34 ASN D 123 HIS D 143 1 21
LINK NE2 HIS A 87 FE HEM A 143 1555 1555 2.25
LINK O HOH A 142 FE HEM A 143 1555 1555 2.44
LINK NE2 HIS B 92 FE HEM B 148 1555 1555 2.26
LINK FE HEM B 148 O HOH B 151 1555 1555 2.10
LINK NE2 HIS C 87 FE HEM C 143 1555 1555 2.35
LINK O HOH C 142 FE HEM C 143 1555 1555 2.31
LINK NE2 HIS D 92 FE HEM D 148 1555 1555 2.34
LINK FE HEM D 148 O HOH D 164 1555 1555 2.14
SITE 1 AC1 17 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC1 17 HIS A 58 LYS A 61 LEU A 83 LEU A 86
SITE 3 AC1 17 HIS A 87 LEU A 91 VAL A 93 ASN A 97
SITE 4 AC1 17 PHE A 98 LEU A 101 LEU A 136 HOH A 142
SITE 5 AC1 17 HOH A 155
SITE 1 AC2 12 PHE B 41 PHE B 42 HIS B 63 SER B 70
SITE 2 AC2 12 HIS B 92 LEU B 96 VAL B 98 ASN B 102
SITE 3 AC2 12 LEU B 106 LEU B 141 HOH B 151 HOH B 171
SITE 1 AC3 16 TYR C 42 PHE C 43 HIS C 45 HIS C 58
SITE 2 AC3 16 LYS C 61 LEU C 83 HIS C 87 LEU C 91
SITE 3 AC3 16 VAL C 93 ASN C 97 PHE C 98 LEU C 101
SITE 4 AC3 16 LEU C 136 HOH C 142 HOH C 156 HOH C 179
SITE 1 AC4 13 THR D 38 PHE D 41 PHE D 42 HIS D 63
SITE 2 AC4 13 LYS D 66 SER D 70 LEU D 88 HIS D 92
SITE 3 AC4 13 LEU D 96 ASN D 102 PHE D 103 LEU D 141
SITE 4 AC4 13 HOH D 164
CRYST1 56.045 74.195 72.272 90.00 102.80 90.00 P 1 21 1 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 0.017843 0.000000 0.004054 0.00000
SCALE2 0.000000 0.013478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014189 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
