[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER OXYGEN TRANSPORT 21-JUN-96 1OUT TITLE TROUT HEMOGLOBIN I COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN I; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: DEOXY; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HEMOGLOBIN I; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: YES; COMPND 12 OTHER_DETAILS: DEOXY SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ONCORHYNCHUS MYKISS; SOURCE 3 ORGANISM_COMMON: TROUT; SOURCE 4 TISSUE: BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: ONCORHYNCHUS MYKISS; SOURCE 7 ORGANISM_COMMON: TROUT KEYWDS HEME, OXYGEN TRANSPORT, RESPIRATORY PROTEIN, ERYTHROCYTE EXPDTA X-RAY DIFFRACTION AUTHOR J.TAME,J.WILSON REVDAT 1 11-JAN-97 1OUT 0 JRNL AUTH J.R.TAME,J.C.WILSON,R.E.WEBER JRNL TITL THE CRYSTAL STRUCTURES OF TROUT HB I IN THE DEOXY JRNL TITL 2 AND CARBONMONOXY FORMS. JRNL REF J.MOL.BIOL. V. 259 749 1996 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 14704 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.162 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 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) : 0.1620 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2187 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 173 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.30 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) : 0.25 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) : 0.014 ; 0.025 REMARK 3 ANGLE DISTANCE (A) : 0.030 ; 0.035 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.035 ; 0.050 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) : 0.096 ; 0.120 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.192 ; 0.300 REMARK 3 MULTIPLE TORSION (A) : 0.275 ; 0.300 REMARK 3 H-BOND (X...Y) (A) : 0.181 ; 0.300 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) : 2.700 ; 7.000 REMARK 3 STAGGERED (DEGREES) : 19.990; 20.000 REMARK 3 TRANSVERSE (DEGREES) : 31.785; 30.000 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.063 ; 4.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.547 ; 6.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 7.599 ; 8.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.641 ; 10.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OUT 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) : 293.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX9.6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.87 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MAR RESEARCH 300MM IMAGE PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17315 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : 0.04900 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 (%): 55.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,2/3+Z REMARK 290 3555 -X+Y,-X,1/3+Z REMARK 290 4555 -X,-Y,1/2+Z REMARK 290 5555 Y,-X+Y,1/6+Z REMARK 290 6555 X-Y,X,5/6+Z REMARK 290 7555 Y,X,2/3-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,1/3-Z REMARK 290 10555 -Y,-X,1/6-Z REMARK 290 11555 -X+Y,Y,1/2-Z REMARK 290 12555 X,X-Y,5/6-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 208.49333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 104.24667 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 156.37000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 52.12333 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 260.61667 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 208.49333 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 104.24667 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 52.12333 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 156.37000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 260.61667 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 94.92000 REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 54.80209 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 104.24667 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 CH2 TRP B 15 OD1 ASP B 72 1.84 DBREF 1OUT A 1 141 UNP P02019 HBA1_ONCMY 1 143 DBREF 1OUT B 1 146 UNP P02142 HBB1_ONCMY 1 146 SEQADV 1OUT A UNP P02019 ASP 32 DELETION SEQADV 1OUT A UNP P02019 LYS 33 DELETION SEQRES 1 A 142 SER LEU THR ALA LYS ASP LYS SER VAL VAL LYS ALA PHE SEQRES 2 A 142 TRP GLY LYS ILE SER GLY LYS ALA ASP VAL VAL GLY ALA SEQRES 3 A 142 GLU ALA LEU GLY ARG MET LEU THR ALA TYR PRO GLN THR SEQRES 4 A 142 LYS THR TYR PHE SER HIS TRP ALA ASP LEU SER PRO GLY SEQRES 5 A 142 SER GLY PRO VAL LYS LYS HIS GLY GLY ILE ILE MET GLY SEQRES 6 A 142 ALA ILE GLY LYS ALA VAL GLY LEU MET ASP ASP LEU VAL SEQRES 7 A 142 GLY GLY MET SER ALA LEU SER ASP LEU HIS ALA PHE LYS SEQRES 8 A 142 LEU ARG VAL ASP PRO GLY ASN PHE LYS ILE LEU SER HIS SEQRES 9 A 142 ASN ILE LEU VAL THR LEU ALA ILE HIS PHE PRO SER ASP SEQRES 10 A 142 PHE THR PRO GLU VAL HIS ILE ALA VAL ASP LYS PHE LEU SEQRES 11 A 142 ALA ALA VAL SER ALA ALA LEU ALA ASP LYS TYR ARG SEQRES 1 B 146 VAL GLU TRP THR ASP ALA GLU LYS SER THR ILE SER ALA SEQRES 2 B 146 VAL TRP GLY LYS VAL ASN ILE ASP GLU ILE GLY PRO LEU SEQRES 3 B 146 ALA LEU ALA ARG VAL LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE GLY SER PHE GLY ASN VAL SER THR PRO ALA SEQRES 5 B 146 ALA ILE MET GLY ASN PRO LYS VAL ALA ALA HIS GLY LYS SEQRES 6 B 146 VAL VAL CYS GLY ALA LEU ASP LYS ALA VAL LYS ASN MET SEQRES 7 B 146 GLY ASN ILE LEU ALA THR TYR LYS SER LEU SER GLU THR SEQRES 8 B 146 HIS ALA ASN LYS LEU PHE VAL ASP PRO ASP ASN PHE ARG SEQRES 9 B 146 VAL LEU ALA ASP VAL LEU THR ILE VAL ILE ALA ALA LYS SEQRES 10 B 146 PHE GLY ALA SER PHE THR PRO GLU ILE GLN ALA THR TRP SEQRES 11 B 146 GLN LYS PHE MET LYS VAL VAL VAL ALA ALA MET GLY SER SEQRES 12 B 146 ARG TYR PHE HET ACE A 0 3 HET HEM A 143 43 HET HEM B 148 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 ACE C2 H4 O FORMUL 4 HEM 2(C34 H32 FE N4 O4) FORMUL 6 HOH *173(H2 O) HELIX 1 1 ALA A 4 ALA A 35 1 32 HELIX 2 2 PRO A 37 PHE A 43 5 7 HELIX 3 3 GLY A 54 GLY A 72 1 19 HELIX 4 4 LEU A 77 GLY A 80 1 4 HELIX 5 5 SER A 82 PHE A 90 1 9 HELIX 6 6 PRO A 96 HIS A 113 5 18 HELIX 7 7 PRO A 120 ALA A 138 1 19 HELIX 8 8 ASP B 5 LYS B 17 1 13 HELIX 9 9 ILE B 20 VAL B 34 1 15 HELIX 10 10 PRO B 36 TYR B 41 5 6 HELIX 11 11 GLY B 43 PHE B 45 5 3 HELIX 12 12 PRO B 51 GLY B 56 1 6 HELIX 13 13 PRO B 58 ASN B 77 1 20 HELIX 14 14 ILE B 81 ASN B 94 1 14 HELIX 15 15 PRO B 100 SER B 121 5 22 HELIX 16 16 PRO B 124 MET B 141 1 18 LINK C ACE A 0 N SER A 1 LINK FE HEM A 143 NE2 HIS A 88 LINK FE HEM B 148 NE2 HIS B 92 CRYST1 63.280 63.280 312.740 90.00 90.00 120.00 P 65 2 2 12 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 0.015803 0.009124 0.000000 0.00000 SCALE2 0.000000 0.018247 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003198 0.00000