Header list of 1j5h.pdb file
Complete list - b 23 2 Bytes
HEADER ANTIBIOTIC 02-MAY-02 1J5H
TITLE SOLUTION STRUCTURE OF APO-NEOCARZINOSTATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APO-NEOCARZINOSTATIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NCS, MITOMALCIN, MMC;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CARZINOSTATICUS;
SOURCE 3 ORGANISM_TAXID: 1897;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCANTABB5
KEYWDS BETA SANDWICH, IGG FOLD, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 44
AUTHOR M.D.URBANIAK,F.W.MUSKETT,M.D.FINUCANE,S.CADDICK,D.N.WOOLFSON
REVDAT 4 23-FEB-22 1J5H 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1J5H 1 VERSN
REVDAT 2 11-DEC-02 1J5H 1 JRNL
REVDAT 1 11-SEP-02 1J5H 0
JRNL AUTH M.D.URBANIAK,F.W.MUSKETT,M.D.FINUCANE,S.CADDICK,D.N.WOOLFSON
JRNL TITL SOLUTION STRUCTURE OF A NOVEL CHROMOPROTEIN DERIVED FROM
JRNL TITL 2 APO-NEOCARZINOSTATIN AND A SYNTHETIC CHROMOPHORE
JRNL REF BIOCHEMISTRY V. 41 11731 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12269815
JRNL DOI 10.1021/BI0262146
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, DYANA
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, MUMENTHALER, WURTHRICH
REMARK 3 (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESTRAINTS FOR STRUCTURE CALCULATION: INTRARESIDUE NOES 194,
REMARK 3 SEQUENTIAL NOES (I, I +1) 206,
REMARK 3 MEDIUM-RANGE NOES (I, I+2 - I+4) 129, LONG-RANGE NOES (I, I> 5)
REMARK 3 303, PSI ANGLE RESTRAINTS 56, HYDROGEN BONDS 52, DISULPHIDE BONDS
REMARK 3 12.
REMARK 4
REMARK 4 1J5H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000001636.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 25 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.2 MM U-15N 1, 25 MM PHOSPHATE
REMARK 210 PH 5.0, 0.1 MM TSP, 0.005%
REMARK 210 SODIUM AZIDE W/V
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-1H-15N TOCSY; 3D 1H-1H-15N
REMARK 210 NOESY; 3D HNHA; 3D HNHB; 2D 1H-
REMARK 210 15N HSQC; 2D 1H-1H NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE SGI6X, XEASY 1.3.13
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 44
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-44
REMARK 465 RES C SSSEQI
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 LEU A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
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 THR A 68 HE ARG A 70 1.44
REMARK 500 O ASP A 51 H SER A 53 1.56
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 4 147.65 -178.55
REMARK 500 1 SER A 10 16.74 -159.09
REMARK 500 1 SER A 11 159.12 167.56
REMARK 500 1 LEU A 13 -149.98 -93.80
REMARK 500 1 ASP A 15 94.80 -63.59
REMARK 500 1 THR A 17 80.89 -66.32
REMARK 500 1 ALA A 24 -163.71 153.49
REMARK 500 1 GLN A 27 -98.59 -86.80
REMARK 500 1 ALA A 28 93.17 176.17
REMARK 500 1 VAL A 40 -106.41 -100.54
REMARK 500 1 ASP A 41 39.43 -89.16
REMARK 500 1 THR A 42 -66.02 65.79
REMARK 500 1 PRO A 49 41.26 -74.99
REMARK 500 1 PHE A 52 -55.41 67.95
REMARK 500 1 SER A 53 149.83 -31.89
REMARK 500 1 ALA A 59 -89.81 31.06
REMARK 500 1 SER A 64 106.21 -162.31
REMARK 500 1 THR A 65 -177.92 178.10
REMARK 500 1 ARG A 70 154.98 -37.18
REMARK 500 1 PHE A 73 -165.42 -178.89
REMARK 500 1 LEU A 77 -70.35 -49.80
REMARK 500 1 PHE A 78 -28.47 170.09
REMARK 500 1 ASP A 79 52.08 173.18
REMARK 500 1 TRP A 83 -78.91 -65.88
REMARK 500 1 THR A 85 68.02 -65.54
REMARK 500 1 ALA A 92 69.08 35.42
REMARK 500 1 CYS A 93 -179.65 -51.63
REMARK 500 1 ASN A 103 -179.45 -48.30
REMARK 500 1 GLU A 106 -156.81 -80.64
REMARK 500 1 VAL A 108 78.06 -105.03
REMARK 500 2 ALA A 2 -55.55 167.26
REMARK 500 2 THR A 8 -60.34 -27.79
REMARK 500 2 PRO A 9 -91.69 -75.07
REMARK 500 2 SER A 10 24.06 89.83
REMARK 500 2 LEU A 13 -145.39 -99.74
REMARK 500 2 ASP A 15 98.68 -57.32
REMARK 500 2 ALA A 24 -160.88 150.61
REMARK 500 2 GLN A 27 -99.56 -89.97
REMARK 500 2 ALA A 28 91.71 178.22
REMARK 500 2 THR A 42 90.91 -54.71
REMARK 500 2 VAL A 44 39.95 -98.42
REMARK 500 2 PRO A 49 26.47 -74.99
REMARK 500 2 PHE A 52 -49.22 70.12
REMARK 500 2 SER A 53 151.09 -35.13
REMARK 500 2 ALA A 59 -89.69 30.35
REMARK 500 2 ARG A 71 -72.54 -89.46
REMARK 500 2 ASP A 79 21.90 -153.93
REMARK 500 2 THR A 81 -147.85 -157.08
REMARK 500 2 THR A 85 81.74 23.86
REMARK 500 2 ALA A 92 56.30 30.11
REMARK 500
REMARK 500 THIS ENTRY HAS 1320 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5343 RELATED DB: BMRB
REMARK 900 1H AND 15N ASSIGNMENTS
DBREF 1J5H A 1 113 UNP P0A3R9 NCZS_STRCZ 35 147
SEQADV 1J5H HIS A -8 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H HIS A -7 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H HIS A -6 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H HIS A -5 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H HIS A -4 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H HIS A -3 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H LEU A -2 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H GLN A -1 UNP P0A3R9 EXPRESSION TAG
SEQADV 1J5H GLY A 0 UNP P0A3R9 EXPRESSION TAG
SEQRES 1 A 122 HIS HIS HIS HIS HIS HIS LEU GLN GLY ALA ALA PRO THR
SEQRES 2 A 122 ALA THR VAL THR PRO SER SER GLY LEU SER ASP GLY THR
SEQRES 3 A 122 VAL VAL LYS VAL ALA GLY ALA GLY LEU GLN ALA GLY THR
SEQRES 4 A 122 ALA TYR ASP VAL GLY GLN CYS ALA TRP VAL ASP THR GLY
SEQRES 5 A 122 VAL LEU ALA CYS ASN PRO ALA ASP PHE SER SER VAL THR
SEQRES 6 A 122 ALA ASP ALA ASN GLY SER ALA SER THR SER LEU THR VAL
SEQRES 7 A 122 ARG ARG SER PHE GLU GLY PHE LEU PHE ASP GLY THR ARG
SEQRES 8 A 122 TRP GLY THR VAL ASP CYS THR THR ALA ALA CYS GLN VAL
SEQRES 9 A 122 GLY LEU SER ASP ALA ALA GLY ASN GLY PRO GLU GLY VAL
SEQRES 10 A 122 ALA ILE SER PHE ASN
SHEET 1 A 3 THR A 4 VAL A 7 0
SHEET 2 A 3 THR A 17 ALA A 24 -1 O ALA A 22 N THR A 6
SHEET 3 A 3 SER A 62 VAL A 69 -1 O THR A 65 N VAL A 21
SHEET 1 B 4 SER A 53 THR A 56 0
SHEET 2 B 4 ALA A 31 GLN A 36 -1 N TYR A 32 O VAL A 55
SHEET 3 B 4 GLN A 94 SER A 98 -1 O GLY A 96 N GLY A 35
SHEET 4 B 4 VAL A 108 ALA A 109 -1 O VAL A 108 N VAL A 95
SHEET 1 C 2 CYS A 37 TRP A 39 0
SHEET 2 C 2 LEU A 45 CYS A 47 -1 O ALA A 46 N ALA A 38
SHEET 1 D 2 SER A 72 LEU A 77 0
SHEET 2 D 2 ARG A 82 ASP A 87 -1 N TRP A 83 O GLY A 75
SSBOND 1 CYS A 37 CYS A 47 1555 1555 2.00
SSBOND 2 CYS A 88 CYS A 93 1555 1555 1.85
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