Header list of 1klp.pdb file
Complete list - r 25 2 Bytes
HEADER LIGAND TRANSPORT 12-DEC-01 1KLP
TITLE THE SOLUTION STRUCTURE OF ACYL CARRIER PROTEIN FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEROMYCOLATE EXTENSION ACYL CARRIER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACP, ACPM;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 VARIANT: H37RV;
SOURCE 6 GENE: ACPM;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 CODONPLUS (DE3)-RP;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS FOUR-HELIX BUNDLE, LIGAND TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.C.WONG,G.LIU,Y.-M.ZHANG,C.O.ROCK,J.ZHENG
REVDAT 4 13-JUL-11 1KLP 1 VERSN
REVDAT 3 24-FEB-09 1KLP 1 VERSN
REVDAT 2 01-APR-03 1KLP 1 JRNL
REVDAT 1 07-JUN-02 1KLP 0
JRNL AUTH H.C.WONG,G.LIU,Y.M.ZHANG,C.O.ROCK,J.ZHENG
JRNL TITL THE SOLUTION STRUCTURE OF ACYL CARRIER PROTEIN FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF J.BIOL.CHEM. V. 277 15874 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11825906
JRNL DOI 10.1074/JBC.M112300200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB015084.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM 15N,13C; 40 MM POTASSIUM
REMARK 210 PHOSPHATE PH 6.5; 0.1 MM DTT;
REMARK 210 0.1% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCA(CO)NH; HNCO; HNHA;
REMARK 210 HCCH-TOCSY; 13C-HSQC-NOESY
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 : NMRPIPE, XEASY 1.3.13
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 320
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 GLN A 50 H LYS A 54 1.55
REMARK 500 O ALA A 48 H GLU A 52 1.55
REMARK 500 O PRO A 60 H LEU A 64 1.56
REMARK 500 O GLN A 50 H ASP A 53 1.57
REMARK 500 O PRO A 60 H ASP A 63 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 PHE A 33 -36.85 79.91
REMARK 500 1 VAL A 34 -56.59 -136.89
REMARK 500 1 ASP A 35 -31.34 -38.30
REMARK 500 1 ASP A 36 -67.98 -105.69
REMARK 500 1 ASP A 40 -170.45 88.00
REMARK 500 1 LEU A 67 115.41 -39.75
REMARK 500 1 ILE A 77 -75.92 -85.29
REMARK 500 1 GLU A 81 -88.34 -83.35
REMARK 500 1 GLU A 82 92.22 163.94
REMARK 500 1 GLU A 83 -75.74 -130.59
REMARK 500 1 GLU A 86 -59.58 -122.37
REMARK 500 1 ALA A 87 -51.66 -171.00
REMARK 500 1 ALA A 88 -171.46 162.56
REMARK 500 1 ALA A 90 -47.71 162.87
REMARK 500 1 LEU A 91 137.33 -39.98
REMARK 500 1 ARG A 92 56.85 -164.15
REMARK 500 1 ALA A 93 73.43 163.80
REMARK 500 1 LYS A 94 140.98 67.45
REMARK 500 1 ILE A 95 -82.74 -58.01
REMARK 500 1 ASN A 99 84.90 -168.96
REMARK 500 1 ASP A 101 -58.29 -157.74
REMARK 500 1 ALA A 102 42.51 80.39
REMARK 500 1 VAL A 103 165.73 -44.59
REMARK 500 1 ALA A 104 56.33 -177.19
REMARK 500 1 ASN A 105 -156.62 175.60
REMARK 500 1 GLN A 107 -154.95 -131.73
REMARK 500 1 GLU A 111 -148.19 -128.17
REMARK 500 1 SER A 114 146.27 65.51
REMARK 500 2 PRO A 29 40.35 -75.05
REMARK 500 2 PHE A 33 -36.26 79.62
REMARK 500 2 VAL A 34 -56.86 -136.51
REMARK 500 2 ASP A 35 -30.75 -39.09
REMARK 500 2 ASP A 36 -67.31 -105.41
REMARK 500 2 ASP A 40 -171.42 88.38
REMARK 500 2 LEU A 67 119.60 -39.45
REMARK 500 2 ILE A 77 -76.24 -80.40
REMARK 500 2 GLU A 82 90.42 82.92
REMARK 500 2 GLU A 83 -69.98 -129.60
REMARK 500 2 GLU A 86 -64.83 -127.91
REMARK 500 2 ALA A 87 -63.48 -169.59
REMARK 500 2 ALA A 88 -167.54 -177.25
REMARK 500 2 ARG A 92 46.93 -177.91
REMARK 500 2 ALA A 93 -71.58 -141.27
REMARK 500 2 SER A 97 -152.58 -137.15
REMARK 500 2 ASN A 99 102.72 -178.58
REMARK 500 2 ALA A 102 38.71 -151.08
REMARK 500 2 ALA A 104 46.85 -166.35
REMARK 500 2 ASN A 105 165.41 -44.37
REMARK 500 2 GLN A 107 90.73 -179.55
REMARK 500 2 ALA A 108 45.18 -175.96
REMARK 500
REMARK 500 THIS ENTRY HAS 620 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KLP A 1 115 UNP P0A4W6 ACPM_MYCTU 1 115
SEQRES 1 A 115 MET PRO VAL THR GLN GLU GLU ILE ILE ALA GLY ILE ALA
SEQRES 2 A 115 GLU ILE ILE GLU GLU VAL THR GLY ILE GLU PRO SER GLU
SEQRES 3 A 115 ILE THR PRO GLU LYS SER PHE VAL ASP ASP LEU ASP ILE
SEQRES 4 A 115 ASP SER LEU SER MET VAL GLU ILE ALA VAL GLN THR GLU
SEQRES 5 A 115 ASP LYS TYR GLY VAL LYS ILE PRO ASP GLU ASP LEU ALA
SEQRES 6 A 115 GLY LEU ARG THR VAL GLY ASP VAL VAL ALA TYR ILE GLN
SEQRES 7 A 115 LYS LEU GLU GLU GLU ASN PRO GLU ALA ALA GLN ALA LEU
SEQRES 8 A 115 ARG ALA LYS ILE GLU SER GLU ASN PRO ASP ALA VAL ALA
SEQRES 9 A 115 ASN VAL GLN ALA ARG LEU GLU ALA GLU SER LYS
HELIX 1 1 THR A 4 GLU A 17 1 14
HELIX 2 2 ILE A 39 TYR A 55 1 17
HELIX 3 3 PRO A 60 ALA A 65 1 6
HELIX 4 4 THR A 69 GLU A 82 1 14
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 - r 25 2 Bytes