Header list of 1buy.pdb file
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HEADER CYTOKINE 08-SEP-98 1BUY TITLE HUMAN ERYTHROPOIETIN, NMR MINIMIZED AVERAGE STRUCTURE CAVEAT 1BUY THERE ARE CHIRALITY ERRORS IN THE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (ERYTHROPOIETIN); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 OTHER_DETAILS: SYNTHETIC GENE KEYWDS CYTOKINE, GLYCOPROTEIN, GROWTH FACTOR EXPDTA SOLUTION NMR AUTHOR J.C.CHEETHAM,D.M.SMITH,K.H.AOKI,J.L.STEVENSON,T.J.HOEFFEL,R.S.SYED, AUTHOR 2 J.EGRIE,T.S.HARVEY REVDAT 3 03-NOV-21 1BUY 1 REMARK SEQADV REVDAT 2 24-FEB-09 1BUY 1 VERSN REVDAT 1 10-SEP-99 1BUY 0 JRNL AUTH J.C.CHEETHAM,D.M.SMITH,K.H.AOKI,J.L.STEVENSON,T.J.HOEFFEL, JRNL AUTH 2 R.S.SYED,J.EGRIE,T.S.HARVEY JRNL TITL NMR STRUCTURE OF HUMAN ERYTHROPOIETIN AND A COMPARISON WITH JRNL TITL 2 ITS RECEPTOR BOUND CONFORMATION. JRNL REF NAT.STRUCT.BIOL. V. 5 861 1998 JRNL REFN ISSN 1072-8368 JRNL PMID 9783743 JRNL DOI 10.1038/2302 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 1BUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1000007320. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2/3/4D NOESY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX500; DRX600; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING REMARK 210 PROTOCOL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 15N AND 15N, 13C PROTEIN REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. 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: MONOMERIC 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 REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 H ALA A 124 H ALA A 125 1.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ALA A 1 CA ALA A 1 CB 0.198 REMARK 500 REMARK 500 REMARK: NULL 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ALA A 1 N - CA - CB ANGL. DEV. = 16.1 DEGREES REMARK 500 TYR A 49 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 TRP A 51 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES REMARK 500 TRP A 51 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 TRP A 51 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES REMARK 500 TRP A 64 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 TRP A 64 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES REMARK 500 TRP A 64 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES REMARK 500 TRP A 64 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 TRP A 64 CG - CD2 - CE3 ANGL. DEV. = -6.1 DEGREES REMARK 500 TRP A 88 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 TRP A 88 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 TRP A 88 NE1 - CE2 - CZ2 ANGL. DEV. = 8.3 DEGREES REMARK 500 ILE A 133 CB - CA - C ANGL. DEV. = -14.5 DEGREES REMARK 500 ARG A 139 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 3 33.39 -72.59 REMARK 500 ARG A 4 -171.24 62.87 REMARK 500 LEU A 5 -129.13 -77.71 REMARK 500 CYS A 29 -170.97 -60.31 REMARK 500 GLU A 31 -52.67 -140.17 REMARK 500 HIS A 32 -173.63 -65.97 REMARK 500 CYS A 33 24.11 46.91 REMARK 500 SER A 34 45.73 -164.09 REMARK 500 LEU A 35 -149.62 -57.84 REMARK 500 GLU A 37 -152.95 -73.61 REMARK 500 LYS A 38 53.55 -163.93 REMARK 500 LYS A 45 -4.76 -57.26 REMARK 500 VAL A 46 160.13 -48.98 REMARK 500 ARG A 53 40.58 -84.94 REMARK 500 SER A 84 -154.16 -70.96 REMARK 500 SER A 85 -72.62 -95.60 REMARK 500 GLN A 86 83.75 46.81 REMARK 500 PRO A 87 -149.23 -63.59 REMARK 500 TRP A 88 164.74 70.54 REMARK 500 PRO A 90 100.55 -57.53 REMARK 500 ALA A 114 -156.28 -69.58 REMARK 500 LYS A 116 -44.44 -161.05 REMARK 500 GLU A 117 51.62 27.02 REMARK 500 PRO A 121 177.39 -59.34 REMARK 500 ALA A 124 -8.13 -173.46 REMARK 500 ALA A 125 -20.53 168.45 REMARK 500 SER A 126 25.46 -69.79 REMARK 500 ALA A 127 32.56 -167.07 REMARK 500 ALA A 128 -64.58 -171.02 REMARK 500 PRO A 129 -86.70 -50.10 REMARK 500 LEU A 130 40.85 34.22 REMARK 500 ARG A 131 23.46 -78.66 REMARK 500 ARG A 162 30.77 37.18 REMARK 500 THR A 163 -24.42 -152.93 REMARK 500 ASP A 165 52.27 -144.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 4 0.27 SIDE CHAIN REMARK 500 ARG A 10 0.29 SIDE CHAIN REMARK 500 ARG A 14 0.28 SIDE CHAIN REMARK 500 ARG A 53 0.32 SIDE CHAIN REMARK 500 ARG A 76 0.32 SIDE CHAIN REMARK 500 ARG A 110 0.22 SIDE CHAIN REMARK 500 ARG A 131 0.14 SIDE CHAIN REMARK 500 ARG A 143 0.15 SIDE CHAIN REMARK 500 ARG A 150 0.16 SIDE CHAIN REMARK 500 ARG A 162 0.18 SIDE CHAIN REMARK 500 ARG A 166 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1BUY A 1 166 UNP P01588 EPO_HUMAN 28 193 SEQADV 1BUY LYS A 24 UNP P01588 ASN 51 ENGINEERED MUTATION SEQADV 1BUY LYS A 38 UNP P01588 ASN 65 ENGINEERED MUTATION SEQADV 1BUY LYS A 83 UNP P01588 ASN 110 ENGINEERED MUTATION SEQRES 1 A 166 ALA PRO PRO ARG LEU ILE CYS ASP SER ARG VAL LEU GLU SEQRES 2 A 166 ARG TYR LEU LEU GLU ALA LYS GLU ALA GLU LYS ILE THR SEQRES 3 A 166 THR GLY CYS ALA GLU HIS CYS SER LEU ASN GLU LYS ILE SEQRES 4 A 166 THR VAL PRO ASP THR LYS VAL ASN PHE TYR ALA TRP LYS SEQRES 5 A 166 ARG MET GLU VAL GLY GLN GLN ALA VAL GLU VAL TRP GLN SEQRES 6 A 166 GLY LEU ALA LEU LEU SER GLU ALA VAL LEU ARG GLY GLN SEQRES 7 A 166 ALA LEU LEU VAL LYS SER SER GLN PRO TRP GLU PRO LEU SEQRES 8 A 166 GLN LEU HIS VAL ASP LYS ALA VAL SER GLY LEU ARG SER SEQRES 9 A 166 LEU THR THR LEU LEU ARG ALA LEU GLY ALA GLN LYS GLU SEQRES 10 A 166 ALA ILE SER PRO PRO ASP ALA ALA SER ALA ALA PRO LEU SEQRES 11 A 166 ARG THR ILE THR ALA ASP THR PHE ARG LYS LEU PHE ARG SEQRES 12 A 166 VAL TYR SER ASN PHE LEU ARG GLY LYS LEU LYS LEU TYR SEQRES 13 A 166 THR GLY GLU ALA CYS ARG THR GLY ASP ARG HELIX 1 1 SER A 9 THR A 27 1 19 HELIX 2 2 PHE A 48 TRP A 51 1 4 HELIX 3 3 VAL A 56 LYS A 83 1 28 HELIX 4 4 GLN A 92 ALA A 111 1 20 HELIX 5 5 PHE A 138 CYS A 161 1 24 SSBOND 1 CYS A 7 CYS A 161 1555 1555 2.02 SSBOND 2 CYS A 29 CYS A 33 1555 1555 2.02 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 3 20 Bytes