Header list of 1nq4.pdb file
Complete list - b 23 2 Bytes
HEADER BIOSYNTHETIC PROTEIN 21-JAN-03 1NQ4
TITLE SOLUTION STRUCTURE OF OXYTETRACYCLINE ACYL CARRIER PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYTETRACYCLINE POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES RIMOSUS;
SOURCE 3 ORGANISM_TAXID: 1927;
SOURCE 4 GENE: OTCY1-3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT-7
KEYWDS SOLUTION STRUCTURE, OXYTETRACYCLINE, POLYKETIDE SYNTHASE, DYNAMICS,
KEYWDS 2 ACP, BIOSYNTHETIC PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 28
AUTHOR S.C.FINDLOW,C.WINSOR,T.J.SIMPSON,J.CROSBY,M.P.CRUMP
REVDAT 3 23-FEB-22 1NQ4 1 REMARK
REVDAT 2 24-FEB-09 1NQ4 1 VERSN
REVDAT 1 04-NOV-03 1NQ4 0
JRNL AUTH S.C.FINDLOW,C.WINSOR,T.J.SIMPSON,J.CROSBY,M.P.CRUMP
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF OXYTETRACYCLINE
JRNL TITL 2 POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES
JRNL TITL 3 RIMOSUS
JRNL REF BIOCHEMISTRY V. 42 8423 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12859187
JRNL DOI 10.1021/BI0342259
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), ALEX T BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES ARE BASED ON A TOTAL OF 1131 RESTRAINTS, 1054 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 77 DIHEDRAL ANGLE RESTRAINTS,76 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1NQ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018099.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM OTC ACP U-15N; 20MM ACETATE
REMARK 210 BUFFER; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY; HNHA;
REMARK 210 1H-15N HSQC; 3D_15N-SEPARATED_
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGY CONFORMERS WITH NO
REMARK 210 NOE VIOLATIONS EXCEEDING 0.3A
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 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
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 LEU A 3 -164.03 -59.29
REMARK 500 1 GLU A 21 117.68 -178.63
REMARK 500 1 VAL A 29 28.85 -144.97
REMARK 500 1 ASP A 40 -73.57 -99.08
REMARK 500 1 SER A 41 -40.45 176.64
REMARK 500 1 GLN A 58 57.50 -173.04
REMARK 500 1 ALA A 67 98.71 -58.90
REMARK 500 1 SER A 85 155.34 61.61
REMARK 500 1 SER A 87 33.78 -166.40
REMARK 500 1 ALA A 88 -79.26 63.43
REMARK 500 1 ARG A 93 32.42 -153.00
REMARK 500 1 ASP A 94 -156.78 -138.12
REMARK 500 2 GLU A 21 -167.25 -160.26
REMARK 500 2 SER A 22 -72.22 -107.40
REMARK 500 2 ASP A 28 100.92 -178.11
REMARK 500 2 ASP A 40 -72.29 -90.81
REMARK 500 2 SER A 41 -40.93 174.92
REMARK 500 2 GLN A 58 101.47 177.90
REMARK 500 2 ALA A 67 95.88 -58.25
REMARK 500 2 SER A 87 80.69 60.82
REMARK 500 2 ALA A 92 -47.46 -154.10
REMARK 500 2 ARG A 93 -66.97 69.29
REMARK 500 2 ASP A 94 -67.64 69.32
REMARK 500 3 THR A 2 -171.98 44.72
REMARK 500 3 GLU A 19 28.86 42.48
REMARK 500 3 GLU A 20 32.69 34.30
REMARK 500 3 GLU A 21 157.83 153.21
REMARK 500 3 LEU A 25 40.55 -94.20
REMARK 500 3 ASP A 40 -73.34 -102.07
REMARK 500 3 SER A 41 -43.85 171.84
REMARK 500 3 GLN A 58 49.30 -166.97
REMARK 500 3 ALA A 67 94.08 -57.30
REMARK 500 3 SER A 85 163.56 58.32
REMARK 500 3 ALA A 91 -41.04 -176.65
REMARK 500 3 ARG A 93 129.00 63.06
REMARK 500 3 ASP A 94 110.34 61.18
REMARK 500 4 THR A 2 169.05 171.61
REMARK 500 4 LEU A 3 -164.87 -112.39
REMARK 500 4 GLU A 19 111.13 74.51
REMARK 500 4 GLU A 20 46.97 -169.38
REMARK 500 4 GLU A 21 173.56 62.84
REMARK 500 4 SER A 22 -78.53 -58.00
REMARK 500 4 ASP A 28 96.41 -173.11
REMARK 500 4 VAL A 29 52.37 -140.35
REMARK 500 4 ASP A 40 -70.32 -83.34
REMARK 500 4 SER A 41 -37.96 174.44
REMARK 500 4 GLN A 58 66.53 -176.72
REMARK 500 4 ALA A 67 97.10 -58.57
REMARK 500 4 ALA A 84 -76.57 -59.63
REMARK 500 4 SER A 85 -53.93 173.30
REMARK 500
REMARK 500 THIS ENTRY HAS 329 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7154 RELATED DB: BMRB
REMARK 900 1H AND 15N CHEMICAL SHIFT DATA ENTRY
DBREF 1NQ4 A 1 95 UNP P43677 ACPX_STRRM 1 95
SEQRES 1 A 95 MET THR LEU LEU THR LEU SER ASP LEU LEU THR LEU LEU
SEQRES 2 A 95 ARG GLU CYS ALA GLY GLU GLU GLU SER ILE ASP LEU GLY
SEQRES 3 A 95 GLY ASP VAL GLU ASP VAL ALA PHE ASP ALA LEU GLY TYR
SEQRES 4 A 95 ASP SER LEU ALA LEU LEU ASN THR VAL GLY ARG ILE GLU
SEQRES 5 A 95 ARG ASP TYR GLY VAL GLN LEU GLY ASP ASP ALA VAL GLU
SEQRES 6 A 95 LYS ALA THR THR PRO ARG ALA LEU ILE GLU MET THR ASN
SEQRES 7 A 95 ALA SER LEU THR GLY ALA SER PRO SER ALA GLY GLY ALA
SEQRES 8 A 95 ALA ARG ASP LYS
HELIX 1 1 THR A 5 GLY A 18 1 14
HELIX 2 2 ALA A 33 GLY A 38 1 6
HELIX 3 3 SER A 41 TYR A 55 1 15
HELIX 4 4 ASP A 62 ALA A 67 1 6
HELIX 5 5 THR A 69 ALA A 84 1 16
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