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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 MOL_ID: 2; SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR J.A.FRIERJUNIOR 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 ASTM JMOBAK UK ISSN 0022-2836 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 REMARK 1 PUBL 2 SPRING,MD. REMARK 1 REFN ISBN 0-912466-02-2 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 REMARK 1 PUBL 2 SPRING,MD. REMARK 1 REFN ISBN 0-912466-02-2 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. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) 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 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 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 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 -0.977822 0.052755 -0.202836 -25.57735 REMARK 290 SMTRY2 2 0.052684 -0.874684 -0.481829 17.41741 REMARK 290 SMTRY3 2 -0.202556 -0.481809 0.852505 -51.34522 REMARK 290 SMTRY1 3 -0.968972 0.238274 0.065371 11.30443 REMARK 290 SMTRY2 3 0.238451 0.831161 0.502386 58.29339 REMARK 290 SMTRY3 3 0.065410 0.502311 -0.862189 -36.68128 REMARK 290 SMTRY1 4 0.946794 -0.291028 0.137464 -25.03914 REMARK 290 SMTRY2 4 -0.291135 -0.956478 -0.020557 50.13602 REMARK 290 SMTRY3 4 0.137146 -0.020502 -0.990316 10.30180 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 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 146 GLY HIS PHE THR GLU GLU ASP LYS ALA THR ILE THR SER SEQRES 2 G 146 LEU TRP GLY LYS VAL ASN VAL GLU ASP ALA GLY GLY GLU SEQRES 3 G 146 THR LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 G 146 ARG PHE PHE ASP SER PHE GLY ASN LEU SER SER ALA SER SEQRES 5 G 146 ALA ILE MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 G 146 LYS VAL LEU THR SER LEU GLY ASP ALA ILE LYS HIS LEU SEQRES 7 G 146 ASP ASP LEU LYS GLY THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 G 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS SEQRES 9 G 146 LEU LEU GLY ASN VAL LEU VAL THR VAL LEU ALA ILE HIS SEQRES 10 G 146 PHE GLY LYS GLU PHE THR PRO GLU VAL GLN ALA SER TRP SEQRES 11 G 146 GLN LYS MET VAL THR GLY VAL ALA SER ALA LEU SER SER SEQRES 12 G 146 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 146 GLY HIS PHE THR GLU GLU ASP LYS ALA THR ILE THR SER SEQRES 2 H 146 LEU TRP GLY LYS VAL ASN VAL GLU ASP ALA GLY GLY GLU SEQRES 3 H 146 THR LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 H 146 ARG PHE PHE ASP SER PHE GLY ASN LEU SER SER ALA SER SEQRES 5 H 146 ALA ILE MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 H 146 LYS VAL LEU THR SER LEU GLY ASP ALA ILE LYS HIS LEU SEQRES 7 H 146 ASP ASP LEU LYS GLY THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 H 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS SEQRES 9 H 146 LEU LEU GLY ASN VAL LEU VAL THR VAL LEU ALA ILE HIS SEQRES 10 H 146 PHE GLY LYS GLU PHE THR PRO GLU VAL GLN ALA SER TRP SEQRES 11 H 146 GLN LYS MET VAL THR GLY VAL ALA SER ALA LEU SER SER SEQRES 12 H 146 ARG TYR HIS HET ACE G 0 3 HET ACE H 0 3 HET HEM A 1 43 HET HEM G 1 43 HET HEM B 1 43 HET HEM H 1 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 ACE 2(C2 H4 O) FORMUL 7 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 LINK C ACE H 0 N GLY H 1 CRYST1 62.800 95.100 102.100 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 -0.015720 0.002350 -0.001110 0.79220 SCALE2 0.001310 0.010060 0.002760 0.41850 SCALE3 0.001030 0.002450 -0.009420 0.66890 MTRIX1 1 -1.000000 0.000000 0.000000 0.00000 1 MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1 MTRIX3 1 0.000000 0.000000 -1.000000 0.00000 1