Header list of 1g9l.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 24-NOV-00 1G9L
TITLE SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYADENYLATE-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 498-636);
COMPND 5 SYNONYM: POLY(A) BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS ALL-HELICAL DOMAIN, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.KOZLOV,J.-F.TREMPE,K.KHALEGHPOUR,A.KAHVEJIAN,I.EKIEL,K.GEHRING
REVDAT 5 23-FEB-22 1G9L 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1G9L 1 VERSN
REVDAT 3 01-APR-03 1G9L 1 JRNL
REVDAT 2 11-APR-01 1G9L 1 JRNL
REVDAT 1 14-MAR-01 1G9L 0
JRNL AUTH G.KOZLOV,J.F.TREMPE,K.KHALEGHPOUR,A.KAHVEJIAN,I.EKIEL,
JRNL AUTH 2 K.GEHRING
JRNL TITL STRUCTURE AND FUNCTION OF THE C-TERMINAL PABC DOMAIN OF
JRNL TITL 2 HUMAN POLY(A)-BINDING PROTEIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 4409 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11287632
JRNL DOI 10.1073/PNAS.071024998
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, ARIA 0.9
REMARK 3 AUTHORS : BRUKER SPECTROSPIN (XWINNMR), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1862 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 102 DIHEDRAL ANGLES RESTRAINTS
REMARK 3 AND 33 HYDROGEN BONDS.
REMARK 4
REMARK 4 1G9L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012404.
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 : 0.2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM 15N-LABELED PABC; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.1M NACL; 1MM
REMARK 210 NAN3; PH 6.3; 3MM 15N,13C-
REMARK 210 LABELED PABC; 50MM PHOSPHATE
REMARK 210 BUFFER; 0.1M NACL; 1MM NAN3; PH
REMARK 210 6.3; 3MM UNLABELED PABC; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.1M NACL; 1MM
REMARK 210 NAN3; PH 6.3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, XEASY 1.3.13, CNS
REMARK 210 0.9, ARIA 0.9
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 190
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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
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 5 -61.53 -104.12
REMARK 500 1 ALA A 9 72.63 55.37
REMARK 500 1 GLN A 30 -98.49 -74.83
REMARK 500 1 LEU A 32 41.70 -87.55
REMARK 500 1 PRO A 36 -174.00 -63.59
REMARK 500 1 PRO A 43 171.64 -58.25
REMARK 500 1 THR A 54 -163.76 -173.98
REMARK 500 1 GLN A 64 -98.84 -124.70
REMARK 500 1 GLU A 65 47.39 -107.07
REMARK 500 1 GLN A 68 -61.97 -130.42
REMARK 500 1 MET A 69 -9.38 -58.82
REMARK 500 1 PRO A 83 81.57 -55.75
REMARK 500 1 ALA A 86 -138.87 -66.67
REMARK 500 1 LYS A 88 -25.60 -161.30
REMARK 500 1 ILE A 89 -80.08 -49.20
REMARK 500 1 LEU A 93 -7.97 -58.76
REMARK 500 1 GLU A 95 3.24 -171.59
REMARK 500 1 ILE A 96 -152.55 -62.96
REMARK 500 1 ASP A 97 -2.46 -59.42
REMARK 500 1 ASN A 98 -30.12 78.27
REMARK 500 1 PRO A 108 1.62 -69.88
REMARK 500 1 GLN A 126 -95.41 -81.69
REMARK 500 1 LYS A 128 -154.41 -88.47
REMARK 500 2 SER A 5 52.55 -93.26
REMARK 500 2 ALA A 6 158.00 64.57
REMARK 500 2 ALA A 7 25.55 -165.15
REMARK 500 2 ALA A 8 -92.49 59.22
REMARK 500 2 ALA A 9 -95.24 -117.27
REMARK 500 2 THR A 10 79.59 -170.41
REMARK 500 2 PRO A 11 39.50 -82.07
REMARK 500 2 LYS A 20 41.39 -96.89
REMARK 500 2 ALA A 22 -169.78 -75.67
REMARK 500 2 GLN A 29 -79.19 -93.54
REMARK 500 2 LEU A 32 -74.56 -97.69
REMARK 500 2 ASN A 33 53.85 -105.41
REMARK 500 2 ALA A 34 -168.07 -74.08
REMARK 500 2 GLN A 41 -158.79 -75.59
REMARK 500 2 PRO A 43 86.42 -69.87
REMARK 500 2 ALA A 44 43.17 -86.34
REMARK 500 2 THR A 54 -167.44 -168.58
REMARK 500 2 GLN A 64 -94.88 -129.35
REMARK 500 2 GLN A 68 -54.98 -132.37
REMARK 500 2 PRO A 83 78.19 -57.18
REMARK 500 2 ALA A 86 -138.43 -69.88
REMARK 500 2 LYS A 88 -23.79 -159.96
REMARK 500 2 ILE A 89 -81.93 -49.68
REMARK 500 2 GLU A 95 1.48 -168.04
REMARK 500 2 ILE A 96 -153.64 -63.21
REMARK 500 2 ASP A 97 -2.62 -59.82
REMARK 500 2 ASN A 98 -36.53 79.49
REMARK 500
REMARK 500 THIS ENTRY HAS 735 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1G9L A 6 144 UNP P11940 PABP1_HUMAN 498 636
SEQADV 1G9L GLY A 1 UNP P11940 CLONING ARTIFACT
SEQADV 1G9L PRO A 2 UNP P11940 CLONING ARTIFACT
SEQADV 1G9L LEU A 3 UNP P11940 CLONING ARTIFACT
SEQADV 1G9L GLY A 4 UNP P11940 CLONING ARTIFACT
SEQADV 1G9L SER A 5 UNP P11940 CLONING ARTIFACT
SEQRES 1 A 144 GLY PRO LEU GLY SER ALA ALA ALA ALA THR PRO ALA VAL
SEQRES 2 A 144 ARG THR VAL PRO GLN TYR LYS TYR ALA ALA GLY VAL ARG
SEQRES 3 A 144 ASN PRO GLN GLN HIS LEU ASN ALA GLN PRO GLN VAL THR
SEQRES 4 A 144 MET GLN GLN PRO ALA VAL HIS VAL GLN GLY GLN GLU PRO
SEQRES 5 A 144 LEU THR ALA SER MET LEU ALA SER ALA PRO PRO GLN GLU
SEQRES 6 A 144 GLN LYS GLN MET LEU GLY GLU ARG LEU PHE PRO LEU ILE
SEQRES 7 A 144 GLN ALA MET HIS PRO THR LEU ALA GLY LYS ILE THR GLY
SEQRES 8 A 144 MET LEU LEU GLU ILE ASP ASN SER GLU LEU LEU HIS MET
SEQRES 9 A 144 LEU GLU SER PRO GLU SER LEU ARG SER LYS VAL ASP GLU
SEQRES 10 A 144 ALA VAL ALA VAL LEU GLN ALA HIS GLN ALA LYS GLU ALA
SEQRES 11 A 144 ALA GLN LYS ALA VAL ASN SER ALA THR GLY VAL PRO THR
SEQRES 12 A 144 VAL
HELIX 1 1 THR A 54 ALA A 59 1 6
HELIX 2 2 LEU A 74 HIS A 82 1 9
HELIX 3 3 LYS A 88 LEU A 93 1 6
HELIX 4 4 ASN A 98 SER A 107 1 10
HELIX 5 5 GLU A 109 ALA A 124 1 16
CISPEP 1 GLY A 1 PRO A 2 2 0.60
CISPEP 2 ASN A 27 PRO A 28 2 0.32
CISPEP 3 GLN A 35 PRO A 36 4 0.48
CISPEP 4 GLY A 1 PRO A 2 5 0.25
CISPEP 5 VAL A 16 PRO A 17 5 0.33
CISPEP 6 ASN A 27 PRO A 28 5 0.34
CISPEP 7 GLU A 51 PRO A 52 5 1.55
CISPEP 8 PRO A 62 PRO A 63 5 -0.01
CISPEP 9 VAL A 141 PRO A 142 5 0.42
CISPEP 10 GLN A 35 PRO A 36 8 0.42
CISPEP 11 GLN A 35 PRO A 36 9 0.66
CISPEP 12 VAL A 141 PRO A 142 9 0.10
CISPEP 13 THR A 10 PRO A 11 10 0.56
CISPEP 14 VAL A 141 PRO A 142 11 1.15
CISPEP 15 THR A 10 PRO A 11 12 0.47
CISPEP 16 ASN A 27 PRO A 28 12 0.54
CISPEP 17 THR A 10 PRO A 11 13 -0.03
CISPEP 18 PRO A 62 PRO A 63 13 -0.72
CISPEP 19 PRO A 62 PRO A 63 14 -0.24
CISPEP 20 THR A 10 PRO A 11 15 0.39
CISPEP 21 PRO A 62 PRO A 63 15 -0.33
CISPEP 22 HIS A 82 PRO A 83 16 2.40
CISPEP 23 GLN A 42 PRO A 43 17 0.18
CISPEP 24 GLU A 51 PRO A 52 17 0.46
CISPEP 25 PRO A 62 PRO A 63 17 0.00
CISPEP 26 GLN A 42 PRO A 43 20 -0.03
CISPEP 27 VAL A 141 PRO A 142 20 0.38
CISPEP 28 GLU A 51 PRO A 52 22 0.72
CISPEP 29 THR A 10 PRO A 11 23 0.31
CISPEP 30 VAL A 16 PRO A 17 23 0.97
CISPEP 31 GLN A 35 PRO A 36 23 0.92
CISPEP 32 THR A 10 PRO A 11 24 0.83
CISPEP 33 GLN A 42 PRO A 43 24 0.32
CISPEP 34 ASN A 27 PRO A 28 25 0.66
CISPEP 35 GLN A 35 PRO A 36 25 0.66
CISPEP 36 VAL A 141 PRO A 142 25 0.13
CISPEP 37 VAL A 16 PRO A 17 27 0.53
CISPEP 38 GLN A 42 PRO A 43 27 0.64
CISPEP 39 VAL A 141 PRO A 142 28 0.23
CISPEP 40 THR A 10 PRO A 11 29 -0.04
CISPEP 41 PRO A 62 PRO A 63 29 -0.21
CISPEP 42 THR A 10 PRO A 11 30 0.48
CISPEP 43 PRO A 62 PRO A 63 30 -0.61
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