Header list of 1nmr.pdb file
Complete list - b 23 2 Bytes
HEADER PEPTIDE BINDING PROTEIN 10-JAN-03 1NMR
TITLE SOLUTION STRUCTURE OF C-TERMINAL DOMAIN FROM TRYPANOSOMA CRUZI
TITLE 2 POLY(A)-BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(A)-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD (DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ALL HELICAL DOMAIN, PEPTIDE BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.SIDDIQUI,G.KOZLOV,I.D'ORSO,J.F.TREMPE,A.C.C.FRASCH,K.GEHRING
REVDAT 4 23-FEB-22 1NMR 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1NMR 1 VERSN
REVDAT 2 04-NOV-03 1NMR 1 JRNL
REVDAT 1 09-SEP-03 1NMR 0
JRNL AUTH N.SIDDIQUI,G.KOZLOV,I.D'ORSO,J.F.TREMPE,K.GEHRING
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN FROM
JRNL TITL 2 POLY(A)-BINDING PROTEIN IN TRYPANOSOMA CRUZI: A VEGETAL PABC
JRNL TITL 3 DOMAIN
JRNL REF PROTEIN SCI. V. 12 1925 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 12930992
JRNL DOI 10.1110/PS.0390103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1170 RESTRAINTS: 974 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 78 DIHEDRAL ANGLE RESTRAINTS,49 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS AND 69 15N-1H RESIDUAL DIPOLAR COUPLINGS
REMARK 4
REMARK 4 1NMR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018013.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE, 150MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM TCPABC, UNLABELLED, 50MM
REMARK 210 PHOSPHATE BUFFER, 150MM NACL,
REMARK 210 1MM NAN3, PH 6.3, 90% H2O, 10%
REMARK 210 D2O; 2MM TCPABC U-15N, 50MM
REMARK 210 PHOSPHATE BUFFER, 150MM NACL,
REMARK 210 1MM NAN3, PH 6.3, 90% H2O, 10%
REMARK 210 D2O; 2MM TCPABC U-15N,13C, 50MM
REMARK 210 PHOSPHATE BUFFER, 150MM NACL,
REMARK 210 1MM NAN3, PH 6.3, 100% D20; 2MM
REMARK 210 TCPABC U-15N, 50MM PHOSPHATE
REMARK 210 BUFFER, 150MM NACL, 1MM NAN3,
REMARK 210 18MG/ML PF1 PHAGE, PH 6.3, 90%
REMARK 210 H2O, 10% D2O; 2MM TCPABC,
REMARK 210 UNLABELLED, 50MM PHOSPHATE
REMARK 210 BUFFER, 150MM NACL, 1MM NAN3, PH
REMARK 210 6.3, 100% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY; IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, XEASY 1.3.13, ARIA
REMARK 210 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES.
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 OD1 ASN A 55 HZ2 LYS A 71 1.56
REMARK 500 O ALA A 43 H THR A 47 1.60
REMARK 500 O MET A 49 N LEU A 51 2.14
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 SER A 2 31.44 -96.96
REMARK 500 1 GLN A 9 79.31 -105.14
REMARK 500 1 LEU A 18 53.18 -115.04
REMARK 500 1 ALA A 41 43.78 -78.96
REMARK 500 1 ALA A 42 -39.47 -159.76
REMARK 500 1 LEU A 50 -66.80 23.75
REMARK 500 1 ASP A 54 -70.60 -89.52
REMARK 500 1 LEU A 59 -32.53 -38.17
REMARK 500 1 LEU A 61 52.00 -114.64
REMARK 500 1 LEU A 62 90.34 -29.80
REMARK 500 1 PRO A 65 -72.28 -71.96
REMARK 500 1 LEU A 67 -70.23 -50.75
REMARK 500 1 LEU A 79 -166.49 60.69
REMARK 500 1 ARG A 81 23.31 -68.96
REMARK 500 1 MET A 83 -69.62 -161.95
REMARK 500 2 SER A 3 -68.31 -154.44
REMARK 500 2 THR A 13 -72.12 -66.50
REMARK 500 2 LEU A 15 18.66 -69.67
REMARK 500 2 ALA A 16 88.65 -68.49
REMARK 500 2 ASN A 17 -75.13 -121.92
REMARK 500 2 ILE A 38 -65.19 -92.81
REMARK 500 2 ALA A 41 44.58 -93.90
REMARK 500 2 ALA A 42 -39.08 -159.55
REMARK 500 2 LEU A 50 -66.68 23.02
REMARK 500 2 ASP A 54 -74.78 -87.23
REMARK 500 2 LEU A 59 -36.44 -36.97
REMARK 500 2 LEU A 61 53.95 -116.35
REMARK 500 2 LEU A 62 89.49 -29.28
REMARK 500 2 LEU A 67 -71.13 -55.94
REMARK 500 2 LEU A 79 -171.87 53.99
REMARK 500 2 ARG A 81 17.12 -65.59
REMARK 500 3 ALA A 5 96.60 -56.75
REMARK 500 3 SER A 6 -62.08 -108.57
REMARK 500 3 ASN A 10 -84.42 -68.50
REMARK 500 3 ASN A 17 -67.97 -125.46
REMARK 500 3 ALA A 41 45.53 -77.27
REMARK 500 3 ALA A 42 -44.82 -159.69
REMARK 500 3 LEU A 50 -66.82 24.83
REMARK 500 3 ASP A 54 -63.96 -91.03
REMARK 500 3 LEU A 59 -34.46 -36.94
REMARK 500 3 LEU A 62 88.87 -31.77
REMARK 500 3 LEU A 67 -70.07 -55.26
REMARK 500 3 LEU A 79 -71.11 -54.83
REMARK 500 3 ARG A 81 23.33 -76.01
REMARK 500 3 MET A 83 178.48 -49.41
REMARK 500 4 ALA A 16 46.95 -76.13
REMARK 500 4 ASN A 17 -62.44 -126.45
REMARK 500 4 ILE A 38 -65.05 -91.11
REMARK 500 4 ALA A 41 47.00 -92.82
REMARK 500 4 ALA A 42 -39.63 -159.51
REMARK 500
REMARK 500 THIS ENTRY HAS 277 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NMR A 3 85 UNP Q27335 Q27335_TRYCR 468 550
SEQADV 1NMR GLY A 1 UNP Q27335 CLONING ARTIFACT
SEQADV 1NMR SER A 2 UNP Q27335 CLONING ARTIFACT
SEQRES 1 A 85 GLY SER SER LEU ALA SER GLN GLY GLN ASN LEU SER THR
SEQRES 2 A 85 VAL LEU ALA ASN LEU THR PRO GLU GLN GLN LYS ASN VAL
SEQRES 3 A 85 LEU GLY GLU ARG LEU TYR ASN HIS ILE VAL ALA ILE ASN
SEQRES 4 A 85 PRO ALA ALA ALA ALA LYS VAL THR GLY MET LEU LEU GLU
SEQRES 5 A 85 MET ASP ASN GLY GLU ILE LEU ASN LEU LEU ASP THR PRO
SEQRES 6 A 85 GLY LEU LEU ASP ALA LYS VAL GLN GLU ALA LEU GLU VAL
SEQRES 7 A 85 LEU ASN ARG HIS MET ASN VAL
HELIX 1 1 LEU A 11 ALA A 16 1 6
HELIX 2 2 LEU A 18 ALA A 37 1 20
HELIX 3 3 ASN A 39 LEU A 50 1 12
HELIX 4 4 MET A 53 ASN A 60 1 8
HELIX 5 5 THR A 64 LEU A 79 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