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HEADER OXYGEN TRANSPORT 05-MAR-99 1T1N TITLE CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (HEMOGLOBIN); COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HBTNCO; COMPND 5 OTHER_DETAILS: HEM GROUP IS COMPLEXED WITH CARBON MONOXIDE; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN (HEMOGLOBIN); COMPND 8 CHAIN: B; COMPND 9 SYNONYM: HBTNCO; COMPND 10 OTHER_DETAILS: HEM GROUP IS COMPLEXED WITH CARBON MONOXIDE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TREMATOMUS NEWNESI; SOURCE 3 ORGANISM_COMMON: FISH; SOURCE 4 TISSUE: BLOOD; SOURCE 5 CELL: RED BLOOD CELLS; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: TREMATOMUS NEWNESI; SOURCE 8 ORGANISM_COMMON: FISH; SOURCE 9 TISSUE: BLOOD; SOURCE 10 CELL: RED BLOOD CELLS KEYWDS OXYGEN TRANSPORT, HEMOGLOBIN EXPDTA X-RAY DIFFRACTION AUTHOR L.MAZZARELLA,L.VITAGLIANO,C.SAVINO,A.ZAGARI REVDAT 2 01-APR-03 1T1N 1 JRNL REVDAT 1 29-APR-99 1T1N 0 JRNL AUTH L.MAZZARELLA,R.D'AVINO,G.DI PRISCO,C.SAVINO, JRNL AUTH 2 L.VITAGLIANO,P.C.MOODY,A.ZAGARI JRNL TITL CRYSTAL STRUCTURE OF TREMATOMUS NEWNESI JRNL TITL 2 HAEMOGLOBIN RE-OPENS THE ROOT EFFECT QUESTION. JRNL REF J.MOL.BIOL. V. 287 897 1999 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.4 REMARK 3 NUMBER OF REFLECTIONS : 18129 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.192 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 : 2247 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 51 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.00 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) : 0.011 REMARK 3 BOND ANGLES (DEGREES) : 2.36 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.79 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.57 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 0.860 ; 1.400 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.510 ; 1.400 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.500 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.370 ; 2.000 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: BULK SOLVENT MODEL USED REMARK 4 REMARK 4 1T1N 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 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB000597. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-1993 REMARK 200 TEMPERATURE (KELVIN) : 293.0 REMARK 200 PH : 8.00 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 : GRAPHITE REMARK 200 OPTICS : COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25207 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.07700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: 1PBX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.58500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.03000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.58500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.03000 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 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, B 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 N SER A 1 O ACE A 0 2.02 REMARK 500 ND HEM B 147 C CMO B 148 2.09 DBREF 1T1N A 1 142 UNP P45718 HBA1_TRENE 1 142 DBREF 1T1N B 1 146 UNP P45720 HBB_TRENE 1 146 SEQRES 1 A 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 A 142 TRP SER LYS ILE GLY LYS SER SER ASP ALA ILE GLY ASN SEQRES 3 A 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 A 142 LYS ILE TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 A 142 SER PRO ASN ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 A 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 A 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 A 142 LEU ARG VAL ASP PRO SER ASN PHE LYS ILE LEU ASN HIS SEQRES 9 A 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 A 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 A 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 B 146 VAL GLU TRP THR ASP LYS GLU ARG SER ILE ILE SER ASP SEQRES 2 B 146 ILE PHE SER HIS MET ASP TYR ASP ASP ILE GLY PRO LYS SEQRES 3 B 146 ALA LEU SER ARG CYS LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE SER GLY PHE GLY ASN LEU TYR ASN ALA GLU SEQRES 5 B 146 GLY ILE MET SER ASN ALA ASN VAL ALA ALA HIS GLY ILE SEQRES 6 B 146 LYS VAL LEU HIS GLY LEU ASP ARG GLY MET LYS ASN MET SEQRES 7 B 146 ASP ASN ILE ALA ASP ALA TYR THR ASP LEU SER THR LEU SEQRES 8 B 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 B 146 LEU LEU SER ASP CYS ILE THR ILE VAL LEU ALA ALA LYS SEQRES 10 B 146 MET GLY HIS ALA PHE THR ALA GLU THR GLN GLY ALA PHE SEQRES 11 B 146 GLN LYS PHE LEU ALA ALA VAL VAL SER ALA LEU GLY LYS SEQRES 12 B 146 GLN TYR HIS MODRES 1T1N ACE A 0 ACETYL GROUP HET ACE A 0 3 HET HEM A 143 43 HET CMO A 144 2 HET HEM B 147 43 HET CMO B 148 2 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 3 ACE C2 H4 O FORMUL 4 HEM 2(C34 H32 FE N4 O4) FORMUL 5 CMO 2(C O) FORMUL 8 HOH *51(H2 O) HELIX 1 AA SER A 3 GLY A 18 1 16 HELIX 2 BA SER A 20 VAL A 35 1 16 HELIX 3 CA TYR A 36 TYR A 42 1 7 HELIX 4 EA SER A 53 SER A 72 1 20 HELIX 5 FA LEU A 81 ALA A 89 1 9 HELIX 6 GA ASP A 95 MET A 113 1 19 HELIX 7 HA THR A 119 GLU A 139 1 21 HELIX 8 AB THR B 4 MET B 18 1 15 HELIX 9 BB ASP B 19 VAL B 34 1 16 HELIX 10 EB ASN B 57 LYS B 76 1 20 HELIX 11 FB TYR B 85 SER B 93 1 9 HELIX 12 GB ASP B 99 LYS B 117 1 19 HELIX 13 HB THR B 123 LYS B 143 1 21 LINK FE HEM A 143 NE2 HIS A 88 LINK FE HEM A 143 C CMO A 144 LINK FE HEM B 147 NE2 HIS B 92 LINK FE HEM B 147 C CMO B 148 LINK C ACE A 0 N SER A 1 SITE 1 STA 2 HIS A 88 HEM A 143 SITE 1 STB 2 HIS B 92 HEM B 147 CRYST1 91.170 88.060 55.250 90.00 97.65 90.00 C 1 2 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 0.010968 0.000000 0.001473 0.00000 SCALE2 0.000000 0.011356 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018262 0.00000