HEADER OXYGEN TRANSPORT 18-AUG-76 1FDH
TITLE STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN F (DEOXY) (ALPHA CHAIN);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN F (DEOXY) (GAMMA CHAIN);
COMPND 7 CHAIN: G, H;
COMPND 8 ENGINEERED: YES
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 J.A.FRIERJUNIOR
REVDAT 12 27-SEP-23 1FDH 1 REMARK LINK SCALE MTRIX
REVDAT 12 2 1 ATOM
REVDAT 11 13-JUL-11 1FDH 1 VERSN
REVDAT 10 24-FEB-09 1FDH 1 VERSN
REVDAT 9 30-SEP-83 1FDH 1 REVDAT
REVDAT 8 27-JAN-82 1FDH 1 COMPND
REVDAT 7 20-APR-81 1FDH 1 HELIX
REVDAT 6 31-DEC-80 1FDH 1 REMARK
REVDAT 5 13-JUN-80 1FDH 1 SEQRES
REVDAT 4 20-JUL-78 1FDH 3 ATOM
REVDAT 3 01-NOV-77 1FDH 1 COMPND AUTHOR JRNL REMARK
REVDAT 3 2 1 FORMUL
REVDAT 2 13-JUN-77 1FDH 1 JRNL REMARK HET
REVDAT 1 19-AUG-76 1FDH 0
JRNL AUTH J.A.FRIER,M.F.PERUTZ
JRNL TITL STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN.
JRNL REF J.MOL.BIOL. V. 112 97 1977
JRNL REFN ISSN 0022-2836
JRNL PMID 881729
JRNL DOI 10.1016/S0022-2836(77)80158-7
REMARK 1
REMARK 1 REFERENCE 1
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 2
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 77 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. 2.50 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) : 2.50
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) : NULL
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 : 4404
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 0
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: NULL
REMARK 4
REMARK 4 1FDH 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_1000173243.
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 (%): 49.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 31.40000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.05000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.05000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.40000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.55000
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, G, B, H
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 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 100.4
REMARK 620 3 HEM A 142 NB 98.4 84.0
REMARK 620 4 HEM A 142 NC 112.6 146.6 86.8
REMARK 620 5 HEM A 142 ND 114.4 83.8 146.5 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM G 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 92 NE2
REMARK 620 2 HEM G 147 NA 97.6
REMARK 620 3 HEM G 147 NB 104.4 86.3
REMARK 620 4 HEM G 147 NC 110.2 152.2 86.5
REMARK 620 5 HEM G 147 ND 103.2 86.9 152.1 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 87 NE2
REMARK 620 2 HEM B 142 NA 100.4
REMARK 620 3 HEM B 142 NB 98.4 84.0
REMARK 620 4 HEM B 142 NC 112.6 146.7 86.8
REMARK 620 5 HEM B 142 ND 114.4 83.9 146.6 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM H 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 92 NE2
REMARK 620 2 HEM H 147 NA 97.6
REMARK 620 3 HEM H 147 NB 104.5 86.3
REMARK 620 4 HEM H 147 NC 110.3 152.1 86.5
REMARK 620 5 HEM H 147 ND 103.2 86.9 152.1 87.0
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 HEM A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM H 147
DBREF 1FDH A 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1FDH G 1 146 UNP P69891 HBG1_HUMAN 7 152
DBREF 1FDH B 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1FDH H 1 146 UNP P69891 HBG1_HUMAN 7 152
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 G 147 ACE GLY HIS PHE THR GLU GLU ASP LYS ALA THR ILE THR
SEQRES 2 G 147 SER LEU TRP GLY LYS VAL ASN VAL GLU ASP ALA GLY GLY
SEQRES 3 G 147 GLU THR LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR
SEQRES 4 G 147 GLN ARG PHE PHE ASP SER PHE GLY ASN LEU SER SER ALA
SEQRES 5 G 147 SER ALA ILE MET GLY ASN PRO LYS VAL LYS ALA HIS GLY
SEQRES 6 G 147 LYS LYS VAL LEU THR SER LEU GLY ASP ALA ILE LYS HIS
SEQRES 7 G 147 LEU ASP ASP LEU LYS GLY THR PHE ALA GLN LEU SER GLU
SEQRES 8 G 147 LEU HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE
SEQRES 9 G 147 LYS LEU LEU GLY ASN VAL LEU VAL THR VAL LEU ALA ILE
SEQRES 10 G 147 HIS PHE GLY LYS GLU PHE THR PRO GLU VAL GLN ALA SER
SEQRES 11 G 147 TRP GLN LYS MET VAL THR GLY VAL ALA SER ALA LEU SER
SEQRES 12 G 147 SER ARG TYR HIS
SEQRES 1 B 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 B 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 B 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 B 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 B 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 B 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 B 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 B 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 B 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 B 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 B 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 H 147 ACE GLY HIS PHE THR GLU GLU ASP LYS ALA THR ILE THR
SEQRES 2 H 147 SER LEU TRP GLY LYS VAL ASN VAL GLU ASP ALA GLY GLY
SEQRES 3 H 147 GLU THR LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR
SEQRES 4 H 147 GLN ARG PHE PHE ASP SER PHE GLY ASN LEU SER SER ALA
SEQRES 5 H 147 SER ALA ILE MET GLY ASN PRO LYS VAL LYS ALA HIS GLY
SEQRES 6 H 147 LYS LYS VAL LEU THR SER LEU GLY ASP ALA ILE LYS HIS
SEQRES 7 H 147 LEU ASP ASP LEU LYS GLY THR PHE ALA GLN LEU SER GLU
SEQRES 8 H 147 LEU HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE
SEQRES 9 H 147 LYS LEU LEU GLY ASN VAL LEU VAL THR VAL LEU ALA ILE
SEQRES 10 H 147 HIS PHE GLY LYS GLU PHE THR PRO GLU VAL GLN ALA SER
SEQRES 11 H 147 TRP GLN LYS MET VAL THR GLY VAL ALA SER ALA LEU SER
SEQRES 12 H 147 SER ARG TYR HIS
HET ACE G 0 3
HET ACE H 0 3
HET HEM A 142 43
HET HEM G 147 43
HET HEM B 142 43
HET HEM H 147 43
HETNAM ACE ACETYL GROUP
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 ACE 2(C2 H4 O)
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
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 AE SER A 52 ALA A 71 1 20
HELIX 5 AF LEU A 80 ALA A 88 1 9
HELIX 6 AG ASP A 94 HIS A 112 1 19
HELIX 7 AH THR A 118 SER A 138 1 21
HELIX 8 GA THR G 4 VAL G 18 1 15
HELIX 9 GB ASN G 19 VAL G 34 1 16
HELIX 10 GC TYR G 35 PHE G 41 1 7
HELIX 11 GD SER G 50 GLY G 56 1 7
HELIX 12 GE ASN G 57 LYS G 76 1 20
HELIX 13 GF PHE G 85 CYS G 93 1 9
HELIX 14 GG ASP G 99 HIS G 117 1 19
HELIX 15 GH THR G 123 SER G 143 1 21
HELIX 16 CA SER B 3 GLY B 18 1 16
HELIX 17 CB HIS B 20 SER B 35 1 16
HELIX 18 CC PHE B 36 TYR B 42 1 7
HELIX 19 CE SER B 52 ALA B 71 1 20
HELIX 20 CF LEU B 80 ALA B 88 1 9
HELIX 21 CG ASP B 94 HIS B 112 1 19
HELIX 22 CH THR B 118 SER B 138 1 21
HELIX 23 HA THR H 4 VAL H 18 1 15
HELIX 24 HB ASN H 19 VAL H 34 1 16
HELIX 25 HC TYR H 35 PHE H 41 1 7
HELIX 26 HD SER H 50 GLY H 56 1 7
HELIX 27 HE ASN H 57 LYS H 76 1 20
HELIX 28 HF PHE H 85 CYS H 93 1 9
HELIX 29 HG ASP H 99 HIS H 117 1 19
HELIX 30 HH THR H 123 SER H 143 1 21
LINK C ACE G 0 N GLY G 1 1555 1555 1.32
LINK O ACE G 0 C GLY G 1 1555 1555 2.03
LINK C ACE G 0 C GLY G 1 1555 1555 1.43
LINK CH3 ACE G 0 N HIS G 2 1555 1555 1.76
LINK CH3 ACE G 0 CA HIS G 2 1555 1555 1.41
LINK C ACE G 0 N HIS G 2 1555 1555 1.33
LINK C ACE H 0 N GLY H 1 1555 1555 1.32
LINK O ACE H 0 C GLY H 1 1555 1555 2.03
LINK C ACE H 0 C GLY H 1 1555 1555 1.43
LINK CH3 ACE H 0 CA HIS H 2 1555 1555 1.41
LINK CH3 ACE H 0 N HIS H 2 1555 1555 1.76
LINK C ACE H 0 N HIS H 2 1555 1555 1.33
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 1.99
LINK NE2 HIS G 92 FE HEM G 147 1555 1555 2.23
LINK NE2 HIS B 87 FE HEM B 142 1555 1555 1.99
LINK NE2 HIS H 92 FE HEM H 147 1555 1555 2.23
SITE 1 AC1 15 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC1 15 HIS A 58 LYS A 61 LEU A 83 LEU A 86
SITE 3 AC1 15 HIS A 87 LEU A 91 VAL A 93 ASN A 97
SITE 4 AC1 15 PHE A 98 LEU A 101 LEU A 136
SITE 1 AC2 12 HIS G 63 VAL G 67 SER G 70 PHE G 85
SITE 2 AC2 12 LEU G 88 LEU G 91 HIS G 92 LEU G 96
SITE 3 AC2 12 ASN G 102 LEU G 106 LEU G 141 GLU H 5
SITE 1 AC3 15 TYR B 42 PHE B 43 HIS B 45 PHE B 46
SITE 2 AC3 15 HIS B 58 LYS B 61 LEU B 83 LEU B 86
SITE 3 AC3 15 HIS B 87 LEU B 91 VAL B 93 ASN B 97
SITE 4 AC3 15 PHE B 98 LEU B 101 LEU B 136
SITE 1 AC4 12 HIS B 72 HIS H 63 VAL H 67 SER H 70
SITE 2 AC4 12 PHE H 85 LEU H 88 LEU H 91 HIS H 92
SITE 3 AC4 12 LEU H 96 ASN H 102 LEU H 106 LEU H 141
CRYST1 62.800 95.100 102.100 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 -0.986002 0.124528 0.105448 36.89608
ORIGX2 0.147453 0.957014 0.250488 -62.53129
ORIGX3 -0.069461 0.262521 -0.963059 58.77933
SCALE1 0.015924 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009794 0.00000
MTRIX1 1 -0.956478 0.282472 0.073934 81.04358 1
MTRIX2 1 0.282138 0.831161 0.479286 -40.04943 1
MTRIX3 1 0.073769 0.478784 -0.874684 105.30560 1
(ATOM LINES ARE NOT SHOWN.)
END
