HEADER OXYGEN TRANSPORT 07-MAR-84 2HHB
TITLE THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN (DEOXY) (ALPHA CHAIN);
COMPND 3 CHAIN: A, C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: HEMOGLOBIN (DEOXY) (BETA CHAIN);
COMPND 6 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS OXYGEN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR G.FERMI,M.F.PERUTZ
REVDAT 7 15-MAR-23 2HHB 1 REMARK
REVDAT 6 08-FEB-23 2HHB 1 REMARK LINK SCALE MTRIX
REVDAT 6 2 1 ATOM
REVDAT 5 13-JUL-11 2HHB 1 VERSN
REVDAT 4 24-FEB-09 2HHB 1 VERSN
REVDAT 3 01-APR-03 2HHB 1 JRNL
REVDAT 2 15-OCT-89 2HHB 3 MTRIX
REVDAT 1 18-JUL-84 2HHB 0
SPRSDE 18-JUL-84 2HHB 1HHB
JRNL AUTH G.FERMI,M.F.PERUTZ,B.SHAANAN,R.FOURME
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 A
JRNL TITL 2 RESOLUTION
JRNL REF J.MOL.BIOL. V. 175 159 1984
JRNL REFN ISSN 0022-2836
JRNL PMID 6726807
JRNL DOI 10.1016/0022-2836(84)90472-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.F.PERUTZ,S.S.HASNAIN,P.J.DUKE,J.L.SESSLER,J.E.HAHN
REMARK 1 TITL STEREOCHEMISTRY OF IRON IN DEOXYHAEMOGLOBIN
REMARK 1 REF NATURE V. 295 535 1982
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.FERMI,M.F.PERUTZ
REMARK 1 REF HAEMOGLOBIN AND MYOGLOBIN. V. 2 1981
REMARK 1 REF 2 ATLAS OF MOLECULAR
REMARK 1 REF 3 STRUCTURES IN BIOLOGY
REMARK 1 PUBL OXFORD UNIVERSITY PRESS
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.F.PERUTZ
REMARK 1 TITL REGULATION OF OXYGEN AFFINITY OF HEMOGLOBIN. INFLUENCE OF
REMARK 1 TITL 2 STRUCTURE OF THE GLOBIN ON THE HEME IRON
REMARK 1 REF ANNU.REV.BIOCHEM. V. 48 327 1979
REMARK 1 REFN ISSN 0066-4154
REMARK 1 REFERENCE 4
REMARK 1 AUTH L.F.TENEYCK,A.ARNONE
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN DEOXYHEMOGLOBIN
REMARK 1 TITL 2 AT 2.5 ANGSTROMS RESOLUTION, I.X-RAY ANALYSIS
REMARK 1 REF J.MOL.BIOL. V. 100 3 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.FERMI
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN
REMARK 1 TITL 2 DEOXYHAEMOGLOBIN AT 2.5 ANGSTROMS RESOLUTION, REFINEMENT OF
REMARK 1 TITL 3 THE ATOMIC MODEL
REMARK 1 REF J.MOL.BIOL. V. 97 237 1975
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH H.MUIRHEAD,J.GREER
REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN
REMARK 1 TITL 2 DEOXYHAEMOGLOBIN AT 3.5 ANGSTROMS RESOLUTION
REMARK 1 REF NATURE V. 228 516 1970
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 7
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 56 1972
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 8
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 64 1972
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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 SET) : 0.160
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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4384
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 174
REMARK 3 SOLVENT ATOMS : 221
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE COORDINATES GIVEN HERE ARE IN THE ORTHOGONAL ANGSTROM
REMARK 3 SYSTEM STANDARD FOR HEMOGLOBINS. THE Y AXIS IS THE
REMARK 3 (NON CRYSTALLOGRAPHIC) MOLECULAR DIAD AND THE X AXIS IS THE
REMARK 3 PSEUDO DIAD WHICH RELATES THE ALPHA-1 AND BETA-1 CHAINS.
REMARK 3 THE TRANSFORMATION GIVEN IN THE *MTRIX* RECORDS BELOW
REMARK 3 WILL GENERATE COORDINATES FOR THE *C* AND *D* CHAINS FROM
REMARK 3 THE *A* AND *B* CHAINS RESPECTIVELY.
REMARK 4
REMARK 4 2HHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 41.79500
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: 11610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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 400
REMARK 400 COMPOUND
REMARK 400 THREE SETS OF COORDINATES FOR HUMAN HEMOGLOBIN WERE
REMARK 400 DEPOSITED SIMULTANEOUSLY.
REMARK 400 2HHB. REFINED BY THE METHOD OF JACK AND LEVITT. THIS
REMARK 400 ENTRY PRESENTS THE BEST ESTIMATE OF THE
REMARK 400 COORDINATES.
REMARK 400 3HHB. SYMMETRY AVERAGED ABOUT THE (NON-CRYSTALLOGRAPHIC)
REMARK 400 MOLECULAR AXIS AND THEN RE-REGULARIZED BY THE
REMARK 400 ENERGY REFINEMENT METHOD OF LEVITT. THIS ENTRY
REMARK 400 PRESENTS COORDINATES THAT ARE ADEQUATE FOR MOST
REMARK 400 PURPOSES, SUCH AS COMPARISON WITH OTHER STRUCTURES.
REMARK 400 4HHB. UNRESTRAINED REFINEMENT. THIS ENTRY PRESENTS
REMARK 400 COORDINATES THAT ARE USEFUL FOR STATISTICAL STUDIES
REMARK 400 (E.G. PHI/PSI ANGLES) WHERE DATA UNBIASED BY
REMARK 400 RESTRAINTS IS REQUIRED.
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 OD2 ASP C 85 O HOH B 205 2657 1.42
REMARK 500 O HOH B 205 O HOH C 160 2647 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 138 CB SER A 138 OG -0.103
REMARK 500 HIS D 2 CG HIS D 2 CD2 0.063
REMARK 500 HIS D 143 CG HIS D 143 CD2 0.054
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 A 31 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 THR A 137 CA - CB - CG2 ANGL. DEV. = 14.7 DEGREES
REMARK 500 SER B 44 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP B 73 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 LEU B 78 CB - CG - CD1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 THR C 38 OG1 - CB - CG2 ANGL. DEV. = -14.8 DEGREES
REMARK 500 LEU C 83 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG C 92 CD - NE - CZ ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG C 92 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 THR C 118 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 THR C 118 CA - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 LYS C 139 CD - CE - NZ ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 LYS D 17 CB - CG - CD ANGL. DEV. = -15.7 DEGREES
REMARK 500 ASP D 21 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG D 30 CD - NE - CZ ANGL. DEV. = 20.8 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH2 ANGL. DEV. = -13.5 DEGREES
REMARK 500 LEU D 32 CB - CG - CD1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG D 40 N - CA - CB ANGL. DEV. = -14.4 DEGREES
REMARK 500 ARG D 40 CG - CD - NE ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG D 40 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 GLU D 43 CB - CG - CD ANGL. DEV. = -20.6 DEGREES
REMARK 500 ASN D 139 CA - CB - CG ANGL. DEV. = -14.8 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 42.08 -146.30
REMARK 500 ASN B 80 66.27 -161.15
REMARK 500 ASP C 75 48.84 -151.70
REMARK 500 HIS D 77 47.00 -140.71
REMARK 500 ASN D 80 67.62 -152.14
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 TYR A 24 0.07 SIDE CHAIN
REMARK 500 ARG C 92 0.12 SIDE CHAIN
REMARK 500 ARG D 30 0.11 SIDE CHAIN
REMARK 500 ARG D 40 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PO4 B 147
REMARK 610 PO4 D 147
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 99.8
REMARK 620 3 HEM A 142 NB 100.5 87.1
REMARK 620 4 HEM A 142 NC 103.7 156.4 85.7
REMARK 620 5 HEM A 142 ND 105.5 92.0 153.8 84.8
REMARK 620 N 1 2 3 4
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 95.2
REMARK 620 3 HEM B 148 NB 99.8 87.8
REMARK 620 4 HEM B 148 NC 102.7 162.0 90.7
REMARK 620 5 HEM B 148 ND 99.5 89.3 160.7 86.2
REMARK 620 N 1 2 3 4
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 93.6
REMARK 620 3 HEM C 142 NB 93.5 85.8
REMARK 620 4 HEM C 142 NC 106.7 159.7 92.1
REMARK 620 5 HEM C 142 ND 104.4 88.9 161.7 86.7
REMARK 620 N 1 2 3 4
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 92.1
REMARK 620 3 HEM D 148 NB 99.6 87.0
REMARK 620 4 HEM D 148 NC 109.4 158.3 86.7
REMARK 620 5 HEM D 148 ND 101.4 89.9 158.9 88.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM 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 HEM D 148
DBREF 2HHB A 1 141 UNP P01922 HBA_HUMAN 1 141
DBREF 2HHB B 1 146 UNP P02023 HBB_HUMAN 1 146
DBREF 2HHB C 1 141 UNP P01922 HBA_HUMAN 1 141
DBREF 2HHB D 1 146 UNP P02023 HBB_HUMAN 1 146
SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY 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 LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA 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 CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP 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 GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR 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 CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA 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 PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY 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 LYS LYS VAL ALA ASP ALA
SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 C 141 ALA LEU SER ALA 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 CYS
SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP 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 GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA THR 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 CYS VAL LEU ALA HIS HIS
SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA 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 PO4 B 147 1
HET HEM B 148 43
HET HEM C 142 43
HET PO4 D 147 1
HET HEM D 148 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM PO4 PHOSPHATE ION
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 11 HOH *221(H2 O)
HELIX 1 AA SER A 3 GLY A 18 1 16
HELIX 2 AB HIS A 20 SER A 35 1 16
HELIX 3 AC PHE A 36 TYR A 42 1 7
HELIX 4 AD HIS A 50 GLY A 51 1DEGEN 2 RES HLX RETAIN HOMOL 2
HELIX 5 AE SER A 52 ALA A 71 1 20
HELIX 6 AF LEU A 80 ALA A 88 1 9
HELIX 7 AG ASP A 94 HIS A 112 1 19
HELIX 8 AH THR A 118 SER A 138 1 21
HELIX 9 BA THR B 4 VAL B 18 1 15
HELIX 10 BB ASN B 19 VAL B 34 1 16
HELIX 11 BC TYR B 35 PHE B 41 1 7
HELIX 12 BD THR B 50 GLY B 56 1 7
HELIX 13 BE ASN B 57 ALA B 76 1 20
HELIX 14 BF PHE B 85 CYS B 93 1 9
HELIX 15 BG ASP B 99 HIS B 117 1 19
HELIX 16 BH THR B 123 HIS B 143 1 21
HELIX 17 CA SER C 3 GLY C 18 1 16
HELIX 18 CB HIS C 20 SER C 35 1 16
HELIX 19 CC PHE C 36 TYR C 42 1 7
HELIX 20 CD HIS C 50 GLY C 51 1DEGEN 2 RES HLX RETAIN HOMOL 2
HELIX 21 CE SER C 52 ALA C 71 1 20
HELIX 22 CF LEU C 80 ALA C 88 1 9
HELIX 23 CG ASP C 94 HIS C 112 1 19
HELIX 24 CH THR C 118 SER C 138 1 21
HELIX 25 DA THR D 4 VAL D 18 1 15
HELIX 26 DB ASN D 19 VAL D 34 1 16
HELIX 27 DC TYR D 35 PHE D 41 1 7
HELIX 28 DD THR D 50 GLY D 56 1 7
HELIX 29 DE ASN D 57 ALA D 76 1 20
HELIX 30 DF PHE D 85 CYS D 93 1 9
HELIX 31 DG ASP D 99 HIS D 117 1 19
HELIX 32 DH THR D 123 HIS D 143 1 21
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.15
LINK NE2 HIS B 92 FE HEM B 148 1555 1555 2.15
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.17
LINK NE2 HIS D 92 FE HEM D 148 1555 1555 2.03
SITE 1 AC1 1 VAL D 1
SITE 1 AC2 1 HOH B 198
SITE 1 AC3 16 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC3 16 HIS A 58 LYS A 61 LEU A 86 HIS A 87
SITE 3 AC3 16 LEU A 91 VAL A 93 ASN A 97 PHE A 98
SITE 4 AC3 16 LEU A 101 LEU A 136 HOH A 144 HOH A 160
SITE 1 AC4 12 ALA A 53 PHE B 42 HIS B 63 LYS B 66
SITE 2 AC4 12 VAL B 67 HIS B 92 LEU B 96 ASN B 102
SITE 3 AC4 12 PHE B 103 LEU B 141 HOH B 176 HOH B 194
SITE 1 AC5 15 TYR C 42 PHE C 43 HIS C 45 HIS C 58
SITE 2 AC5 15 LYS C 61 LEU C 83 LEU C 86 HIS C 87
SITE 3 AC5 15 LEU C 91 VAL C 93 ASN C 97 PHE C 98
SITE 4 AC5 15 LEU C 136 HOH C 149 HOH C 163
SITE 1 AC6 9 HIS D 63 LYS D 66 VAL D 67 LEU D 91
SITE 2 AC6 9 HIS D 92 LEU D 96 ASN D 102 LEU D 106
SITE 3 AC6 9 LEU D 141
CRYST1 63.150 83.590 53.800 90.00 99.34 90.00 P 1 21 1 4
ORIGX1 0.985646 -0.158954 -0.056388 -5.70439
ORIGX2 0.153472 0.983904 -0.091380 -11.43529
ORIGX3 0.069996 0.081402 0.994230 -41.45281
SCALE1 0.015835 0.000000 0.002604 0.00000
SCALE2 0.000000 0.011963 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018837 0.00000
MTRIX1 1 -0.952899 0.301963 -0.028045 17.04968 1
MTRIX2 1 0.302014 0.936202 -0.179824 4.93604 1
MTRIX3 1 -0.028043 -0.179784 -0.983303 81.78229 1
(ATOM LINES ARE NOT SHOWN.)
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