Header list of 1isk.pdb file
Complete list - b 23 2 Bytes
HEADER ISOMERASE 12-MAR-97 1ISK
TITLE 3-OXO-DELTA5-STEROID ISOMERASE, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-OXO-DELTA5-STEROID ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: KSI, 3-KETOSTEROID ISOMERASE;
COMPND 5 EC: 5.3.3.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COMAMONAS TESTOSTERONI;
SOURCE 3 ORGANISM_TAXID: 285;
SOURCE 4 ATCC: 11996;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NCM533;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKC2
KEYWDS ISOMERASE, KSI, 3-KETOSTEROID
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.R.WU,S.EBRAHIMIAN,M.E.ZAWROTNY,L.D.THORNBURG,G.C.PEREZ-ALVARADO,
AUTHOR 2 P.BROTHERS,R.M.POLLACK,M.F.SUMMERS
REVDAT 3 23-FEB-22 1ISK 1 REMARK
REVDAT 2 24-FEB-09 1ISK 1 VERSN
REVDAT 1 12-NOV-97 1ISK 0
JRNL AUTH Z.R.WU,S.EBRAHIMIAN,M.E.ZAWROTNY,L.D.THORNBURG,
JRNL AUTH 2 G.C.PEREZ-ALVARADO,P.BROTHERS,R.M.POLLACK,M.F.SUMMERS
JRNL TITL SOLUTION STRUCTURE OF 3-OXO-DELTA5-STEROID ISOMERASE.
JRNL REF SCIENCE V. 276 415 1997
JRNL REFN ISSN 0036-8075
JRNL PMID 9103200
JRNL DOI 10.1126/SCIENCE.276.5311.415
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ISK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174252.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
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
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 B 31 O VAL B 109 1.59
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 1 ASN A 2 130.18 62.44
REMARK 500 1 ALA A 31 178.78 -50.18
REMARK 500 1 PRO A 39 -84.30 -74.98
REMARK 500 1 GLU A 43 95.95 59.33
REMARK 500 1 THR A 48 -29.44 -39.41
REMARK 500 1 THR A 68 14.15 -141.16
REMARK 500 1 GLN A 69 -88.05 -148.16
REMARK 500 1 GLU A 70 -174.95 173.46
REMARK 500 1 ARG A 72 79.68 -112.99
REMARK 500 1 VAL A 74 -147.45 -148.62
REMARK 500 1 ALA A 75 100.63 -50.46
REMARK 500 1 ASN A 76 34.17 37.54
REMARK 500 1 ALA A 78 88.19 -153.08
REMARK 500 1 ALA A 106 -39.21 -174.88
REMARK 500 1 ASN B 2 124.45 167.25
REMARK 500 1 ALA B 31 172.68 -47.07
REMARK 500 1 SER B 42 72.36 62.05
REMARK 500 1 GLU B 43 64.00 -168.98
REMARK 500 1 THR B 68 22.67 -154.76
REMARK 500 1 GLN B 69 -86.73 -147.99
REMARK 500 1 GLU B 70 -177.46 -179.22
REMARK 500 1 ASN B 76 30.76 38.95
REMARK 500 1 TYR B 88 75.19 -110.28
REMARK 500 1 GLN B 89 80.95 35.33
REMARK 500 1 ALA B 106 -20.85 151.23
REMARK 500 2 ASN A 2 97.09 -65.15
REMARK 500 2 ALA A 31 173.92 -47.87
REMARK 500 2 ALA A 34 179.16 -57.44
REMARK 500 2 PRO A 39 -70.62 -74.94
REMARK 500 2 SER A 42 -177.98 149.69
REMARK 500 2 GLU A 43 79.21 64.36
REMARK 500 2 PRO A 44 -167.77 -75.01
REMARK 500 2 ALA A 56 -70.51 -68.02
REMARK 500 2 THR A 68 -51.10 -136.98
REMARK 500 2 GLN A 69 -160.66 -179.98
REMARK 500 2 VAL A 74 -139.30 -157.07
REMARK 500 2 ALA A 75 95.87 -31.48
REMARK 500 2 ASN A 76 58.08 20.93
REMARK 500 2 GLN A 89 72.80 -63.58
REMARK 500 2 ARG A 91 -179.89 165.72
REMARK 500 2 ALA A 106 -40.53 -172.89
REMARK 500 2 ALA A 123 175.34 -59.25
REMARK 500 2 ASN B 2 76.66 41.00
REMARK 500 2 LEU B 23 -72.55 -70.94
REMARK 500 2 ALA B 31 167.39 -45.10
REMARK 500 2 ALA B 34 179.10 -58.93
REMARK 500 2 PRO B 39 -77.33 -74.92
REMARK 500 2 SER B 42 -177.55 153.15
REMARK 500 2 GLU B 43 63.77 67.15
REMARK 500 2 PRO B 44 -169.23 -74.98
REMARK 500
REMARK 500 THIS ENTRY HAS 548 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: SIA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: TYR A14 AND ASP A99 BOTH STABILIZE THE
REMARK 800 INTERMEDIATE BY FORMING HYDROGEN-BOND TO IT. ASP A38 TRANSFERS
REMARK 800 PROTON FROM C-4B TO C-6B.
REMARK 800
REMARK 800 SITE_IDENTIFIER: SIB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: TYR B14 AND ASP B99 BOTH STABILIZE THE
REMARK 800 INTERMEDIATE BY FORMING HYDROGEN-BOND TO IT. ASP B38 TRANSFERS
REMARK 800 PROTON FROM C-4B TO C-6B.
DBREF 1ISK A 1 125 UNP P00947 SDIS_COMTE 1 125
DBREF 1ISK B 1 125 UNP P00947 SDIS_COMTE 1 125
SEQRES 1 A 125 MET ASN THR PRO GLU HIS MET THR ALA VAL VAL GLN ARG
SEQRES 2 A 125 TYR VAL ALA ALA LEU ASN ALA GLY ASP LEU ASP GLY ILE
SEQRES 3 A 125 VAL ALA LEU PHE ALA ASP ASP ALA THR VAL GLU ASP PRO
SEQRES 4 A 125 VAL GLY SER GLU PRO ARG SER GLY THR ALA ALA ILE ARG
SEQRES 5 A 125 GLU PHE TYR ALA ASN SER LEU LYS LEU PRO LEU ALA VAL
SEQRES 6 A 125 GLU LEU THR GLN GLU VAL ARG ALA VAL ALA ASN GLU ALA
SEQRES 7 A 125 ALA PHE ALA PHE THR VAL SER PHE GLU TYR GLN GLY ARG
SEQRES 8 A 125 LYS THR VAL VAL ALA PRO ILE ASP HIS PHE ARG PHE ASN
SEQRES 9 A 125 GLY ALA GLY LYS VAL VAL SER MET ARG ALA LEU PHE GLY
SEQRES 10 A 125 GLU LYS ASN ILE HIS ALA GLY ALA
SEQRES 1 B 125 MET ASN THR PRO GLU HIS MET THR ALA VAL VAL GLN ARG
SEQRES 2 B 125 TYR VAL ALA ALA LEU ASN ALA GLY ASP LEU ASP GLY ILE
SEQRES 3 B 125 VAL ALA LEU PHE ALA ASP ASP ALA THR VAL GLU ASP PRO
SEQRES 4 B 125 VAL GLY SER GLU PRO ARG SER GLY THR ALA ALA ILE ARG
SEQRES 5 B 125 GLU PHE TYR ALA ASN SER LEU LYS LEU PRO LEU ALA VAL
SEQRES 6 B 125 GLU LEU THR GLN GLU VAL ARG ALA VAL ALA ASN GLU ALA
SEQRES 7 B 125 ALA PHE ALA PHE THR VAL SER PHE GLU TYR GLN GLY ARG
SEQRES 8 B 125 LYS THR VAL VAL ALA PRO ILE ASP HIS PHE ARG PHE ASN
SEQRES 9 B 125 GLY ALA GLY LYS VAL VAL SER MET ARG ALA LEU PHE GLY
SEQRES 10 B 125 GLU LYS ASN ILE HIS ALA GLY ALA
HELIX 1 1 THR A 3 ALA A 20 1 18
HELIX 2 2 ASP A 22 PHE A 30 1 9
HELIX 3 3 THR A 48 LEU A 61 1 14
HELIX 4 4 THR B 3 ALA B 20 1 18
HELIX 5 5 ASP B 22 PHE B 30 1 9
HELIX 6 6 THR B 48 LEU B 61 1 14
SHEET 1 A 6 GLU A 43 GLY A 47 0
SHEET 2 A 6 ALA A 34 ASP A 38 -1
SHEET 3 A 6 SER A 111 GLY A 124 1
SHEET 4 A 6 ARG A 91 PHE A 103 -1
SHEET 5 A 6 GLU A 77 TYR A 88 -1
SHEET 6 A 6 LEU A 63 VAL A 74 -1
SHEET 1 B 6 GLU B 43 GLY B 47 0
SHEET 2 B 6 ALA B 34 ASP B 38 -1
SHEET 3 B 6 SER B 111 GLY B 124 1
SHEET 4 B 6 ARG B 91 PHE B 103 -1
SHEET 5 B 6 GLU B 77 TYR B 88 -1
SHEET 6 B 6 LEU B 63 VAL B 74 -1
CISPEP 1 ASP A 38 PRO A 39 1 -0.03
CISPEP 2 ASP B 38 PRO B 39 1 0.14
CISPEP 3 ASP A 38 PRO A 39 2 -0.09
CISPEP 4 ASP B 38 PRO B 39 2 -0.11
CISPEP 5 ASP A 38 PRO A 39 3 -0.02
CISPEP 6 ASP B 38 PRO B 39 3 0.05
CISPEP 7 ASP A 38 PRO A 39 4 0.00
CISPEP 8 ASP B 38 PRO B 39 4 -0.05
CISPEP 9 ASP A 38 PRO A 39 5 0.00
CISPEP 10 ASP B 38 PRO B 39 5 -0.04
CISPEP 11 ASP A 38 PRO A 39 6 0.12
CISPEP 12 ASP B 38 PRO B 39 6 0.03
CISPEP 13 ASP A 38 PRO A 39 7 0.00
CISPEP 14 ASP B 38 PRO B 39 7 0.04
CISPEP 15 ASP A 38 PRO A 39 8 0.09
CISPEP 16 ASP B 38 PRO B 39 8 0.04
CISPEP 17 ASP A 38 PRO A 39 9 0.07
CISPEP 18 ASP B 38 PRO B 39 9 0.01
CISPEP 19 ASP A 38 PRO A 39 10 -0.02
CISPEP 20 ASP B 38 PRO B 39 10 0.00
CISPEP 21 ASP A 38 PRO A 39 11 0.07
CISPEP 22 ASP B 38 PRO B 39 11 0.09
CISPEP 23 ASP A 38 PRO A 39 12 -0.08
CISPEP 24 ASP B 38 PRO B 39 12 -0.01
CISPEP 25 ASP A 38 PRO A 39 13 0.03
CISPEP 26 ASP B 38 PRO B 39 13 -0.05
CISPEP 27 ASP A 38 PRO A 39 14 0.03
CISPEP 28 ASP B 38 PRO B 39 14 0.00
CISPEP 29 ASP A 38 PRO A 39 15 0.07
CISPEP 30 ASP B 38 PRO B 39 15 -0.06
CISPEP 31 ASP A 38 PRO A 39 16 0.05
CISPEP 32 ASP B 38 PRO B 39 16 -0.07
CISPEP 33 ASP A 38 PRO A 39 17 -0.03
CISPEP 34 ASP B 38 PRO B 39 17 0.03
CISPEP 35 ASP A 38 PRO A 39 18 -0.03
CISPEP 36 ASP B 38 PRO B 39 18 0.06
CISPEP 37 ASP A 38 PRO A 39 19 0.08
CISPEP 38 ASP B 38 PRO B 39 19 -0.04
CISPEP 39 ASP A 38 PRO A 39 20 0.03
CISPEP 40 ASP B 38 PRO B 39 20 -0.03
SITE 1 SIA 4 TYR A 14 ASP A 38 ASP A 99 PHE A 101
SITE 1 SIB 4 TYR B 14 ASP B 38 ASP B 99 PHE B 101
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
MODEL 1
Complete list - b 23 2 Bytes