HEADER OXYGEN STORAGE/TRANSPORT 05-OCT-00 1G0A
TITLE CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 8.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: HEMOGLOBIN BETA CHAIN;
COMPND 6 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: CATTLE;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 TISSUE: BLOOD
KEYWDS BOVINE, HEMOGLOBIN, LIGANDED, CARBONMONOXY, PROTOPORPHYRIN IX, OXYGEN
KEYWDS 2 STORAGE-TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.C.MUESER,P.H.ROGERS,A.ARNONE
REVDAT 3 07-FEB-24 1G0A 1 REMARK LINK
REVDAT 2 24-FEB-09 1G0A 1 VERSN
REVDAT 1 27-DEC-00 1G0A 0
JRNL AUTH T.C.MUESER,P.H.ROGERS,A.ARNONE
JRNL TITL INTERFACE SLIDING AS ILLUSTRATED BY THE MULTIPLE QUATERNARY
JRNL TITL 2 STRUCTURES OF LIGANDED HEMOGLOBIN.
JRNL REF BIOCHEMISTRY V. 39 15353 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11112521
JRNL DOI 10.1021/BI0012944
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 36902
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 37869
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4386
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.009 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.023 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012072.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-92
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.5
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38330
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 35.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 7.950
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.19700
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: NULL
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM TAPS, AMMONIUM SULPHATE,
REMARK 280 POTASSIUM CHLORIDE, POLYETHYLENE GLYCOL 3350, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 36.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.55000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.70000
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: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSTRUCTED FROM
REMARK 300 THE HETERODIMER OF CHAIN A (ALPHA) AND CHAIN B (BETA) AND
REMARK 300 THE HETERODIMER OF CHAIN C (ALPHA) AND CHAIN D (BETA)
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: 11610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 HIS A 50 CG ND1 CD2 CE1 NE2
REMARK 480 ARG A 141 CD NE CZ NH1 NH2
REMARK 480 GLU B 6 CG CD OE1 OE2
REMARK 480 GLU B 22 CD OE1 OE2
REMARK 480 HIS C 50 NE2
REMARK 480 GLU D 6 CD OE1 OE2
REMARK 480 LYS D 95 NZ
REMARK 480 ARG D 144 NH1
REMARK 480 HIS D 146 OXT
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HIS A 45 O HOH C 164 2564 1.62
REMARK 500 C HIS A 45 O HOH C 164 2564 1.63
REMARK 500 OD2 ASP B 52 O HOH C 169 4556 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 ARG C 92 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 141 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG D 116 NE - CZ - NH1 ANGL. DEV. = 3.0 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 75 63.64 -156.31
REMARK 500 GLU B 6 -70.74 -68.88
REMARK 500 ASP B 21 -73.23 -45.55
REMARK 500 ASP C 75 69.94 -155.04
REMARK 500 LYS C 139 77.43 -103.51
REMARK 500 ARG D 144 -9.43 -59.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 92 0.10 SIDE CHAIN
REMARK 500 ARG C 141 0.08 SIDE CHAIN
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 90.8
REMARK 620 3 HEM A 142 NB 91.6 90.9
REMARK 620 4 HEM A 142 NC 89.9 179.1 89.6
REMARK 620 5 HEM A 142 ND 91.2 90.0 177.1 89.6
REMARK 620 6 CMO A 143 C 175.3 93.5 90.2 85.8 86.9
REMARK 620 7 CMO A 143 O 172.7 96.2 86.2 83.1 90.9 4.9
REMARK 620 N 1 2 3 4 5 6
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 87.8
REMARK 620 3 HEM B 147 NB 93.5 89.4
REMARK 620 4 HEM B 147 NC 90.8 178.4 89.9
REMARK 620 5 HEM B 147 ND 85.8 91.6 178.8 89.1
REMARK 620 6 CMO B 148 C 173.7 95.4 92.0 86.1 88.7
REMARK 620 7 CMO B 148 O 174.1 97.3 89.5 84.2 91.1 3.1
REMARK 620 N 1 2 3 4 5 6
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 86.9
REMARK 620 3 HEM C 142 NB 89.4 89.7
REMARK 620 4 HEM C 142 NC 91.3 178.1 90.0
REMARK 620 5 HEM C 142 ND 93.5 91.7 176.9 88.6
REMARK 620 6 CMO C 143 C 174.3 89.5 95.0 92.4 82.3
REMARK 620 7 CMO C 143 O 177.6 95.5 90.2 86.4 86.9 7.7
REMARK 620 N 1 2 3 4 5 6
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 77.6
REMARK 620 3 HEM D 147 NB 89.9 88.8
REMARK 620 4 HEM D 147 NC 91.0 168.4 89.1
REMARK 620 5 HEM D 147 ND 80.3 91.2 170.0 88.9
REMARK 620 6 CMO D 148 C 161.6 101.2 108.4 90.3 81.4
REMARK 620 7 CMO D 148 O 177.7 100.6 91.6 90.8 98.2 16.9
REMARK 620 N 1 2 3 4 5 6
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 CMO A 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO B 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO C 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO D 148
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G08 RELATED DB: PDB
REMARK 900 CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 5.0
REMARK 900 RELATED ID: 1G09 RELATED DB: PDB
REMARK 900 CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 7.2
REMARK 900 RELATED ID: 1G0B RELATED DB: PDB
REMARK 900 CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5
DBREF 1G0A A 1 141 UNP P01966 HBA_BOVIN 1 141
DBREF 1G0A C 1 141 UNP P01966 HBA_BOVIN 1 141
DBREF 1G0A B 2 146 UNP P02070 HBB_BOVIN 1 145
DBREF 1G0A D 2 146 UNP P02070 HBB_BOVIN 1 145
SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY GLY HIS ALA ALA GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU 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 GLY HIS GLY ALA LYS VAL ALA ALA ALA
SEQRES 6 A 141 LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY
SEQRES 7 A 141 ALA LEU SER GLU LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS SER
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE
SEQRES 2 B 145 TRP GLY LYS VAL LYS 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 THR ALA ASP ALA
SEQRES 5 B 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS
SEQRES 6 B 145 VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP
SEQRES 7 B 145 ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS
SEQRES 8 B 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU
SEQRES 9 B 145 LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE
SEQRES 10 B 145 GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN
SEQRES 11 B 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG
SEQRES 12 B 145 TYR HIS
SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP GLY LYS VAL GLY GLY HIS ALA ALA GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU 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 GLY HIS GLY ALA LYS VAL ALA ALA ALA
SEQRES 6 C 141 LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY
SEQRES 7 C 141 ALA LEU SER GLU LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS SER
SEQRES 9 C 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 C 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE
SEQRES 2 D 145 TRP GLY LYS VAL LYS 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 THR ALA ASP ALA
SEQRES 5 D 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS
SEQRES 6 D 145 VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP
SEQRES 7 D 145 ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS
SEQRES 8 D 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU
SEQRES 9 D 145 LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE
SEQRES 10 D 145 GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN
SEQRES 11 D 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG
SEQRES 12 D 145 TYR HIS
HET HEM A 142 43
HET CMO A 143 2
HET HEM B 147 43
HET CMO B 148 2
HET HEM C 142 43
HET CMO C 143 2
HET HEM D 147 43
HET CMO D 148 2
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CMO CARBON MONOXIDE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 CMO 4(C O)
FORMUL 13 HOH *145(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 SER A 81 1 7
HELIX 6 6 LEU A 80 ALA A 88 1 9
HELIX 7 7 PRO A 95 LEU 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 LYS B 19 TYR B 35 1 17
HELIX 11 11 PRO B 36 GLU B 43 5 8
HELIX 12 12 PHE B 42 GLY B 46 5 5
HELIX 13 13 THR B 50 ASN B 57 1 8
HELIX 14 14 ASN B 57 HIS B 77 1 21
HELIX 15 15 ASP B 80 PHE B 85 1 6
HELIX 16 16 PHE B 85 LYS B 95 1 11
HELIX 17 17 PRO B 100 GLY B 119 1 20
HELIX 18 18 LYS B 120 PHE B 122 5 3
HELIX 19 19 THR B 123 ALA B 142 1 20
HELIX 20 20 HIS B 143 TYR B 145 5 3
HELIX 21 21 SER C 3 GLY C 18 1 16
HELIX 22 22 HIS C 20 PHE C 36 1 17
HELIX 23 23 PRO C 37 PHE C 43 5 7
HELIX 24 24 SER C 52 HIS C 72 1 21
HELIX 25 25 ASP C 75 LEU C 80 1 6
HELIX 26 26 LEU C 80 HIS C 89 1 10
HELIX 27 27 PRO C 95 LEU C 113 1 19
HELIX 28 28 THR C 118 THR C 137 1 20
HELIX 29 29 THR D 4 GLY D 16 1 13
HELIX 30 30 LYS D 19 TYR D 35 1 17
HELIX 31 31 PRO D 36 GLU D 43 5 8
HELIX 32 32 PHE D 42 GLY D 46 5 5
HELIX 33 33 THR D 50 ASN D 57 1 8
HELIX 34 34 ASN D 57 MET D 75 1 19
HELIX 35 35 ASP D 80 PHE D 85 1 6
HELIX 36 36 PHE D 85 LYS D 95 1 11
HELIX 37 37 PRO D 100 GLY D 119 1 20
HELIX 38 38 LYS D 120 PHE D 122 5 3
HELIX 39 39 THR D 123 ALA D 142 1 20
HELIX 40 40 HIS D 143 TYR D 145 5 3
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.05
LINK FE HEM A 142 C CMO A 143 1555 1555 1.77
LINK FE HEM A 142 O CMO A 143 1555 1555 2.93
LINK NE2 HIS B 92 FE HEM B 147 1555 1555 2.10
LINK FE HEM B 147 C CMO B 148 1555 1555 1.76
LINK FE HEM B 147 O CMO B 148 1555 1555 2.92
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.15
LINK FE HEM C 142 C CMO C 143 1555 1555 1.77
LINK FE HEM C 142 O CMO C 143 1555 1555 2.89
LINK NE2 HIS D 92 FE HEM D 147 1555 1555 2.21
LINK FE HEM D 147 C CMO D 148 1555 1555 1.75
LINK FE HEM D 147 O CMO D 148 1555 1555 2.72
SITE 1 AC1 16 TYR A 42 PHE A 43 HIS A 45 HIS A 58
SITE 2 AC1 16 LYS A 61 LEU A 86 HIS A 87 LEU A 91
SITE 3 AC1 16 VAL A 93 ASN A 97 PHE A 98 LEU A 101
SITE 4 AC1 16 VAL A 132 LEU A 136 CMO A 143 HOH A 154
SITE 1 AC2 3 HIS A 58 VAL A 62 HEM A 142
SITE 1 AC3 10 THR B 38 PHE B 41 PHE B 42 HIS B 63
SITE 2 AC3 10 SER B 70 HIS B 92 LEU B 96 ASN B 102
SITE 3 AC3 10 LEU B 106 CMO B 148
SITE 1 AC4 3 HIS B 63 VAL B 67 HEM B 147
SITE 1 AC5 14 ALA A 12 TYR C 42 PHE C 43 HIS C 45
SITE 2 AC5 14 HIS C 58 LYS C 61 HIS C 87 LEU C 91
SITE 3 AC5 14 VAL C 93 ASN C 97 PHE C 98 LEU C 101
SITE 4 AC5 14 LEU C 136 CMO C 143
SITE 1 AC6 3 HIS C 58 VAL C 62 HEM C 142
SITE 1 AC7 12 THR D 38 PHE D 41 HIS D 63 SER D 70
SITE 2 AC7 12 LEU D 88 HIS D 92 LEU D 96 VAL D 98
SITE 3 AC7 12 ASN D 102 LEU D 106 LEU D 141 CMO D 148
SITE 1 AC8 3 HIS D 63 VAL D 67 HEM D 147
CRYST1 73.800 131.400 63.100 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 0.013550 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015848 0.00000
(ATOM LINES ARE NOT SHOWN.)
END