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HEADER OXYGEN TRANSPORT 22-MAR-94 1HLB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN (DEOXY); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAUDINA ARENICOLA KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR M.L.HACKERT,D.T.MITCHELL REVDAT 1 22-JUN-94 1HLB 0 JRNL AUTH D.T.MITCHELL,G.B.KITTO,M.L.HACKERT JRNL TITL STRUCTURAL ANALYSIS OF MONOMERIC HEMICHROME AND JRNL TITL 2 DIMERIC CYANOMET HEMOGLOBINS FROM CAUDINA JRNL TITL 3 ARENICOLA. JRNL REF J.MOL.BIOL. V. 251 421 1995 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.D.MCDONALD,L.DAVIDSON,G.B.KITTO REMARK 1 TITL AMINO ACID SEQUENCE OF THE COELOMIC C GLOBIN FROM REMARK 1 TITL 2 THE SEA CUCUMBER CAUDINA (MOLPADIA) ARENICOLA REMARK 1 REF J.PROTEIN CHEM. V. 11 29 1992 REMARK 1 REFN ASTM JPCHD2 UK ISSN 0277-8033 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.M.CARSON,T.R.BOWERS,G.B.KITTO,M.L.HACKERT REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC DATA ON MONOMERIC AND REMARK 1 TITL 2 DIMERIC HEMOGLOBINS FROM THE SEA CUCUMBER, REMARK 1 TITL 3 MOLPADIA ARENICOLA REMARK 1 REF J.BIOL.CHEM. V. 254 7400 1979 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REFERENCE 3 REMARK 1 AUTH C.BONAVENTURA,J.BONAVENTURA,B.KITTO,M.BRUNORI, REMARK 1 AUTH 2 E.ANTONINI REMARK 1 TITL FUNCTIONAL CONSEQUENCES OF LIGAND-LINKED REMARK 1 TITL 2 DISSOCIATION IN HEMOGLOBIN FROM THE SEA CUCUMBER REMARK 1 TITL 3 MOLPADIA ARENICOLA REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V. 428 779 1976 REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002 REMARK 1 REFERENCE 4 REMARK 1 AUTH G.B.KITTO,D.ERWIN,R.WEST,J.OMNAAS REMARK 1 TITL N-TERMINAL SUBSTITUTION OF SOME SEA CUCUMBER REMARK 1 TITL 2 HEMOGLOBINS REMARK 1 REF COMP.BIOCHEM.PHYSIOL. B: V. 55 105 1976 REMARK 1 REF 2 COMP.BIOCHEM. REMARK 1 REFN ASTM CBPBB8 UK ISSN 0305-0491 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 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 : 4916 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) : 0.150 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 : 1525 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 43 REMARK 3 SOLVENT ATOMS : 333 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) : 0.014 REMARK 3 BOND ANGLES (DEGREES) : 3.59 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 1HLB 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 (2007-03-23) 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: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 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,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 22.61500 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 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 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 NE2 HIS A 104 FE HEM 158 2.06 REMARK 500 NE2 HIS A 73 FE HEM 158 2.07 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 153 N - CA - C ANGL. DEV. = 22.5 DEGREES REMARK 500 VAL A 154 N - CA - C ANGL. DEV. = 22.3 DEGREES REMARK 500 VAL A 154 CA - C - N ANGL. DEV. =-26.9 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ALA A 5 -90.54 43.94 REMARK 500 ALA A 8 -33.82 60.09 REMARK 500 LEU A 153 121.37 51.17 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 159 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH 164 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH 166 DISTANCE = 8.21 ANGSTROMS REMARK 525 HOH 170 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH 173 DISTANCE = 9.54 ANGSTROMS REMARK 525 HOH 178 DISTANCE = 9.69 ANGSTROMS REMARK 525 HOH 181 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH 184 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH 191 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH 197 DISTANCE = 5.39 ANGSTROMS REMARK 525 HOH 198 DISTANCE = 7.48 ANGSTROMS REMARK 525 HOH 199 DISTANCE = 9.95 ANGSTROMS REMARK 525 HOH 205 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH 207 DISTANCE = 8.25 ANGSTROMS REMARK 525 HOH 215 DISTANCE = 7.55 ANGSTROMS REMARK 525 HOH 216 DISTANCE = 12.83 ANGSTROMS REMARK 525 HOH 218 DISTANCE = 6.74 ANGSTROMS REMARK 525 HOH 219 DISTANCE = 9.19 ANGSTROMS REMARK 525 HOH 222 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH 225 DISTANCE = 6.73 ANGSTROMS REMARK 525 HOH 257 DISTANCE = 6.47 ANGSTROMS DBREF 1HLB A 1 157 UNP P80018 GLBC_CAUAR 1 157 SEQRES 1 A 158 ACE GLY GLY THR LEU ALA ILE GLN ALA GLN GLY ASP LEU SEQRES 2 A 158 THR LEU ALA GLN LYS LYS ILE VAL ARG LYS THR TRP HIS SEQRES 3 A 158 GLN LEU MET ARG ASN LYS THR SER PHE VAL THR ASP VAL SEQRES 4 A 158 PHE ILE ARG ILE PHE ALA TYR ASP PRO SER ALA GLN ASN SEQRES 5 A 158 LYS PHE PRO GLN MET ALA GLY MET SER ALA SER GLN LEU SEQRES 6 A 158 ARG SER SER ARG GLN MET GLN ALA HIS ALA ILE ARG VAL SEQRES 7 A 158 SER SER ILE MET SER GLU TYR VAL GLU GLU LEU ASP SER SEQRES 8 A 158 ASP ILE LEU PRO GLU LEU LEU ALA THR LEU ALA ARG THR SEQRES 9 A 158 HIS ASP LEU ASN LYS VAL GLY ALA ASP HIS TYR ASN LEU SEQRES 10 A 158 PHE ALA LYS VAL LEU MET GLU ALA LEU GLN ALA GLU LEU SEQRES 11 A 158 GLY SER ASP PHE ASN GLU LYS THR ARG ASP ALA TRP ALA SEQRES 12 A 158 LYS ALA PHE SER VAL VAL GLN ALA VAL LEU LEU VAL LYS SEQRES 13 A 158 HIS GLY FTNOTE 1 HEMICHROME COORDINATION OF HEME IRON ATOM WITH BOTH THE FTNOTE 1 PROXIMAL AND DISTAL HISTIDINES COORDINATING TO THE HEME FTNOTE 1 IRON ATOM. HET ACE A 0 3 HET HEM 158 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 1 ACE C2 H4 O FORMUL 2 HEM C34 H32 FE N4 O4 FORMUL 3 HOH *111(H2 O) HELIX 1 A THR A 13 MET A 28 1 16 HELIX 2 B SER A 33 TYR A 45 1 13 HELIX 3 C ASP A 46 LYS A 52 1 7 HELIX 4 D SER A 60 SER A 66 1 7 HELIX 5 E SER A 67 GLU A 86 1DISTAL HIS 73 20 HELIX 6 F ASP A 91 LEU A 106 1KINK AT PRO 93, PROX. HIS 104 16 HELIX 7 G GLY A 110 GLU A 128 1 19 HELIX 8 H ASN A 134 ALA A 150 1 17 TURN 1 G/H ASN A 134 THR A 137 BETA BEND, I 3 CRYST1 45.740 45.230 40.920 90.00 104.40 90.00 P 1 21 1 2 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 0.021863 0.000000 0.005613 0.00000 SCALE2 0.000000 0.022109 0.000000 0.00000 SCALE3 0.000000 0.000000 0.025231 0.00000