Header list of 1o5p.pdb file
Complete list - b 23 2 Bytes
HEADER ANTIBIOTIC 04-OCT-03 1O5P
TITLE SOLUTION STRUCTURE OF HOLO-NEOCARZINOSTATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEOCARZINOSTATIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NCS, MITOMALCIN, MMC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CARZINOSTATICUS;
SOURCE 3 ORGANISM_TAXID: 1897;
SOURCE 4 OTHER_DETAILS: PROTEIN WAS ISOTOPE LABELED BY PRE-ENRICHED CHLORELLA
SOURCE 5 AS AMINO ACIDE SOURCE.
KEYWDS PROTEIN-LIGAND COMPLEX, 7 STRANDED BETA BARREL, CROMOPROTEIN,
KEYWDS 2 ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 60
AUTHOR H.TAKASHIMA,T.ISHINO,T.YOSHIDA,K.HASUDA,T.OHKUBO,Y.KOBAYASHI
REVDAT 5 23-FEB-22 1O5P 1 REMARK
REVDAT 4 24-FEB-09 1O5P 1 VERSN
REVDAT 3 29-MAR-05 1O5P 1 JRNL
REVDAT 2 20-APR-04 1O5P 1 REMARK
REVDAT 1 14-OCT-03 1O5P 0
JRNL AUTH H.TAKASHIMA,T.YOSHIDA,T.ISHINO,K.HASUDA,T.OHKUBO,Y.KOBAYASHI
JRNL TITL SOLUTION NMR STRUCTURE INVESTIGATION FOR RELEASING MECHANISM
JRNL TITL 2 OF NEOCARZINOSTATIN CHROMOPHORE FROM THE HOLOPROTEIN
JRNL REF J.BIOL.CHEM. V. 280 11340 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15640161
JRNL DOI 10.1074/JBC.M411579200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.TAKASHIMA,N.MIMURA,T.OHKUBO,T.YOSHIDA,H.TAMAOKI,
REMARK 1 AUTH 2 Y.KOBAYASHI
REMARK 1 TITL DISTRIBUTED COMPUTING AND NMR CONSTRAINT-BASED
REMARK 1 TITL 2 HIGH-RESOLUTION STRUCTURE DETERMINATION: APPLIED FOR
REMARK 1 TITL 3 BIOACTIVE PEPTIDE ENDOTHELIN-1 TO DETERMINE C-TERMINAL
REMARK 1 TITL 4 FOLDING.
REMARK 1 REF J.AM.CHEM.SOC. V. 126 4504 2004
REMARK 1 REFN ISSN 0002-7863
REMARK 1 PMID 15070353
REMARK 1 DOI 10.1021/JA031637W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH 2.0.6
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O5P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000005995.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5MM HOLO-NEOCARZINOSTATIN U
REMARK 210 -15N, 13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING WITH RANDOM ARRAY
REMARK 210 INITIAL STRUCTURES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 60
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 60
REMARK 210
REMARK 210 REMARK: BASED ON DISTRIBUTED COMPUTING (SUN GRID ENGINE), THE
REMARK 210 STRUCTURE CALCULATION EXPLORED CONFORMATIONAL SPACE
REMARK 210 COMPREHENSIVELY BY USING A HUGE NUMBER OF INITIAL STRUCTURES TO
REMARK 210 INCREASE STRUCTURE PRECISION AND CONVERGENCE.
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 O GLY A 102 HD21 ASN A 103 1.46
REMARK 500 O LEU A 77 H ASP A 79 1.52
REMARK 500 H GLN A 36 OD2 ASP A 51 1.53
REMARK 500 H ASP A 33 O SER A 98 1.53
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 THR A 4 -169.77 -179.62
REMARK 500 1 THR A 8 149.78 -175.72
REMARK 500 1 SER A 14 145.47 67.05
REMARK 500 1 ASP A 15 106.84 -51.16
REMARK 500 1 GLN A 27 99.58 -47.79
REMARK 500 1 ALA A 28 78.01 -56.20
REMARK 500 1 ALA A 31 109.96 -49.72
REMARK 500 1 ASP A 41 -175.06 174.78
REMARK 500 1 PRO A 49 21.05 -71.56
REMARK 500 1 SER A 53 -165.82 -104.20
REMARK 500 1 SER A 54 137.13 178.89
REMARK 500 1 ASP A 58 -139.56 -60.40
REMARK 500 1 ARG A 71 -78.02 -71.66
REMARK 500 1 GLU A 74 121.92 -30.10
REMARK 500 1 PHE A 76 113.55 -38.99
REMARK 500 1 PHE A 78 58.10 -64.48
REMARK 500 1 ASP A 79 18.95 -160.02
REMARK 500 1 ASP A 99 -157.21 -123.35
REMARK 500 1 PRO A 105 177.17 -46.88
REMARK 500 2 THR A 4 -169.78 -179.46
REMARK 500 2 THR A 8 149.84 -177.70
REMARK 500 2 SER A 14 144.99 66.93
REMARK 500 2 ASP A 15 108.77 -51.17
REMARK 500 2 GLN A 27 98.04 -47.09
REMARK 500 2 ALA A 28 77.31 -55.82
REMARK 500 2 ASP A 41 -175.89 173.98
REMARK 500 2 PRO A 49 24.29 -75.38
REMARK 500 2 SER A 53 -169.24 -111.65
REMARK 500 2 SER A 54 135.34 179.10
REMARK 500 2 ASP A 58 -139.46 -60.73
REMARK 500 2 ARG A 71 -101.66 -55.80
REMARK 500 2 GLU A 74 121.02 -32.09
REMARK 500 2 PHE A 76 113.03 -39.37
REMARK 500 2 PHE A 78 58.36 -63.57
REMARK 500 2 ASP A 79 19.74 -161.53
REMARK 500 2 ASP A 99 -159.04 -117.36
REMARK 500 2 PRO A 105 178.30 -46.93
REMARK 500 3 SER A 14 144.36 67.55
REMARK 500 3 ASP A 15 106.34 -50.87
REMARK 500 3 GLN A 27 100.10 -47.28
REMARK 500 3 ALA A 28 77.75 -56.86
REMARK 500 3 ALA A 31 109.81 -47.52
REMARK 500 3 ASP A 41 -175.38 174.33
REMARK 500 3 PRO A 49 23.90 -74.39
REMARK 500 3 SER A 53 -168.79 -112.63
REMARK 500 3 SER A 54 136.83 178.79
REMARK 500 3 ASP A 58 -139.12 -60.14
REMARK 500 3 ARG A 71 -101.45 -53.12
REMARK 500 3 GLU A 74 121.92 -33.42
REMARK 500 3 PHE A 78 58.06 -65.25
REMARK 500
REMARK 500 THIS ENTRY HAS 1037 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHR A 114
DBREF 1O5P A 1 113 UNP P0A3R9 NCZS_STRCZ 35 147
SEQRES 1 A 113 ALA ALA PRO THR ALA THR VAL THR PRO SER SER GLY LEU
SEQRES 2 A 113 SER ASP GLY THR VAL VAL LYS VAL ALA GLY ALA GLY LEU
SEQRES 3 A 113 GLN ALA GLY THR ALA TYR ASP VAL GLY GLN CYS ALA TRP
SEQRES 4 A 113 VAL ASP THR GLY VAL LEU ALA CYS ASN PRO ALA ASP PHE
SEQRES 5 A 113 SER SER VAL THR ALA ASP ALA ASN GLY SER ALA SER THR
SEQRES 6 A 113 SER LEU THR VAL ARG ARG SER PHE GLU GLY PHE LEU PHE
SEQRES 7 A 113 ASP GLY THR ARG TRP GLY THR VAL ASP CYS THR THR ALA
SEQRES 8 A 113 ALA CYS GLN VAL GLY LEU SER ASP ALA ALA GLY ASN GLY
SEQRES 9 A 113 PRO GLU GLY VAL ALA ILE SER PHE ASN
HET CHR A 114 80
HETNAM CHR NEOCARZINOSTATIN-CHROMOPHORE
HETSYN CHR NCS-CHROMOPHORE
FORMUL 2 CHR C35 H33 N O12
SHEET 1 A 2 THR A 17 GLY A 23 0
SHEET 2 A 2 ALA A 63 VAL A 69 -1 O LEU A 67 N VAL A 19
SHEET 1 B 5 SER A 53 THR A 56 0
SHEET 2 B 5 ALA A 31 TRP A 39 -1 N VAL A 34 O SER A 53
SHEET 3 B 5 LEU A 45 CYS A 47 -1 O ALA A 46 N ALA A 38
SHEET 4 B 5 SER A 72 LEU A 77 -1 O PHE A 76 N CYS A 47
SHEET 5 B 5 ARG A 82 ASP A 87 -1 O VAL A 86 N PHE A 73
SHEET 1 C 4 SER A 53 THR A 56 0
SHEET 2 C 4 ALA A 31 TRP A 39 -1 N VAL A 34 O SER A 53
SHEET 3 C 4 CYS A 93 SER A 98 -1 O SER A 98 N ASP A 33
SHEET 4 C 4 GLY A 107 ALA A 109 -1 O VAL A 108 N VAL A 95
SSBOND 1 CYS A 37 CYS A 47 1555 1555 2.03
SSBOND 2 CYS A 88 CYS A 93 1555 1555 2.02
CISPEP 1 THR A 8 PRO A 9 1 -0.85
CISPEP 2 THR A 8 PRO A 9 2 -0.98
CISPEP 3 THR A 8 PRO A 9 3 -0.42
CISPEP 4 THR A 8 PRO A 9 4 -0.79
CISPEP 5 THR A 8 PRO A 9 5 -0.92
CISPEP 6 THR A 8 PRO A 9 6 -0.41
CISPEP 7 THR A 8 PRO A 9 7 -1.05
CISPEP 8 THR A 8 PRO A 9 8 -0.30
CISPEP 9 THR A 8 PRO A 9 9 -0.87
CISPEP 10 THR A 8 PRO A 9 10 -0.84
CISPEP 11 THR A 8 PRO A 9 11 -0.40
CISPEP 12 THR A 8 PRO A 9 12 -0.94
CISPEP 13 THR A 8 PRO A 9 13 -0.22
CISPEP 14 THR A 8 PRO A 9 14 -0.73
CISPEP 15 THR A 8 PRO A 9 15 -0.23
CISPEP 16 THR A 8 PRO A 9 16 -0.66
CISPEP 17 THR A 8 PRO A 9 17 -0.45
CISPEP 18 THR A 8 PRO A 9 18 -1.01
CISPEP 19 THR A 8 PRO A 9 19 -0.33
CISPEP 20 THR A 8 PRO A 9 20 -0.51
CISPEP 21 THR A 8 PRO A 9 21 -0.91
CISPEP 22 THR A 8 PRO A 9 22 -0.68
CISPEP 23 THR A 8 PRO A 9 23 -0.68
CISPEP 24 THR A 8 PRO A 9 24 -0.76
CISPEP 25 THR A 8 PRO A 9 25 -0.34
CISPEP 26 THR A 8 PRO A 9 26 -0.92
CISPEP 27 THR A 8 PRO A 9 27 -0.82
CISPEP 28 THR A 8 PRO A 9 28 -0.84
CISPEP 29 THR A 8 PRO A 9 29 -0.85
CISPEP 30 THR A 8 PRO A 9 30 -0.64
CISPEP 31 THR A 8 PRO A 9 31 -0.53
CISPEP 32 THR A 8 PRO A 9 32 -0.62
CISPEP 33 THR A 8 PRO A 9 33 -0.67
CISPEP 34 THR A 8 PRO A 9 34 -0.45
CISPEP 35 THR A 8 PRO A 9 35 -0.80
CISPEP 36 THR A 8 PRO A 9 36 -0.70
CISPEP 37 THR A 8 PRO A 9 37 -0.81
CISPEP 38 THR A 8 PRO A 9 38 -0.91
CISPEP 39 THR A 8 PRO A 9 39 -0.87
CISPEP 40 THR A 8 PRO A 9 40 -0.61
CISPEP 41 THR A 8 PRO A 9 41 -0.43
CISPEP 42 THR A 8 PRO A 9 42 -0.48
CISPEP 43 THR A 8 PRO A 9 43 -0.86
CISPEP 44 THR A 8 PRO A 9 44 -0.81
CISPEP 45 THR A 8 PRO A 9 45 -0.57
CISPEP 46 THR A 8 PRO A 9 46 -0.48
CISPEP 47 THR A 8 PRO A 9 47 -0.62
CISPEP 48 THR A 8 PRO A 9 48 -0.64
CISPEP 49 THR A 8 PRO A 9 49 -0.93
CISPEP 50 THR A 8 PRO A 9 50 -0.58
CISPEP 51 THR A 8 PRO A 9 51 -0.43
CISPEP 52 THR A 8 PRO A 9 52 -0.90
CISPEP 53 THR A 8 PRO A 9 53 -0.72
CISPEP 54 THR A 8 PRO A 9 54 -0.96
CISPEP 55 THR A 8 PRO A 9 55 -0.83
CISPEP 56 THR A 8 PRO A 9 56 -0.58
CISPEP 57 THR A 8 PRO A 9 57 -0.79
CISPEP 58 THR A 8 PRO A 9 58 -0.46
CISPEP 59 THR A 8 PRO A 9 59 -0.52
CISPEP 60 THR A 8 PRO A 9 60 -0.97
SITE 1 AC1 11 GLY A 35 CYS A 37 TRP A 39 LEU A 45
SITE 2 AC1 11 PHE A 76 PHE A 78 GLN A 94 GLY A 96
SITE 3 AC1 11 SER A 98 GLY A 102 ASN A 103
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