Header list of 1pul.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 25-JUN-03 1PUL
TITLE SOLUTION STRUCTURE FOR THE 21KDA CAENORHABDITIS ELEGANS PROTEIN
TITLE 2 CE32E8.3. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET WR33
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN C32E8.3 IN CHROMOSOME I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: C32E8.3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B-WR33
KEYWDS ALPHA HELICAL, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NESG, STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR R.TEJERO,J.M.ARAMINI,G.V.T.SWAPNA,D.MONLEON,Y.CHIANG,D.MACAPAGAL,
AUTHOR 2 K.C.GUNSALUS,S.KIM,T.SZYPERSKI,G.T.MONTELIONE,NORTHEAST STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (NESG)
REVDAT 4 02-MAR-22 1PUL 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1PUL 1 VERSN
REVDAT 2 18-APR-06 1PUL 1 AUTHOR
REVDAT 1 21-JUN-05 1PUL 0
JRNL AUTH D.MONLEON,Y.CHIANG,J.M.ARAMINI,G.V.SWAPNA,D.MACAPAGAL,
JRNL AUTH 2 K.C.GUNSALUS,S.KIM,T.SZYPERSKI,G.T.MONTELIONE
JRNL TITL BACKBONE 1H, 15N AND 13C ASSIGNMENTS FOR THE 21 KDA
JRNL TITL 2 CAENORHABDITIS ELEGANS HOMOLOGUE OF "BRAIN-SPECIFIC"
JRNL TITL 3 PROTEIN.
JRNL REF J.BIOMOL.NMR V. 28 91 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 14739645
JRNL DOI 10.1023/B:JNMR.0000012832.71049.BF
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DYANA 1.5, AUTOSTRUCTURE 2.1.0, CNS 1.1
REMARK 3 AUTHORS : GUNTERT (DYANA), HUANG, MONTELIONE
REMARK 3 (AUTOSTRUCTURE), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL 729 CONFORMATIONALLY-
REMARK 3 RESTRICTING
REMARK 3 NOE-DERIVED DISTANCE CONSTRAINTS, 260 DIHEDRAL ANGLE CONSTRAINTS,
REMARK 3 AND 50 HYDROGEN BOND CONSTRAINTS (9.3 CONSTRAINTS PER RESIDUE; 1.2
REMARK 3 LONG-RANGE CONSTRAINTS PER RESIDUE). STRUCTURE DETERMINATION WAS
REMARK 3 PERFORMED ITERATIVELY USING AUTOSTRUCTURE (DYANA). THE 10
REMARK 3 STRUCTURES WITH THE LOWEST TARGET FUNCTION WERE FURTHER REFINED BY
REMARK 3 RESTRAINED MOLECULAR DYNAMICS/ENERGY MINIMIZATION IN EXPLICIT
REMARK 3 WATER (CNS). THE UNSTRUCTURED N- (1 TO 17) AND C- (121 TO 125)
REMARK 3 TERMINAL REGIONS OF THE MOLECULE ARE OMITTED FROM THIS DEPOSITION.
REMARK 4
REMARK 4 1PUL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019579.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM WR33 U-15N,13C; 20MM
REMARK 210 NAH2PO4, 50MM NACL, 10MM DTT,
REMARK 210 0.02% AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY; 3D 13C-NOESY; 2D
REMARK 210 15N,1H HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.106,
REMARK 210 AUTOASSIGN 1.11.0, TALOS 2.1,
REMARK 210 PSVS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. AUTOMATIC BACKBONE ASSIGNMENTS WERE MADE USING
REMARK 210 AUTOASSIGN. MANUAL SIDE CHAIN ASSIGNMENTS. AUTOMATIC NOESY
REMARK 210 ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN BOND CONSTRAINTS
REMARK 210 WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL ANGLE CONSTRAINTS
REMARK 210 WERE DETERMINED USING HYPER AND TALOS. FINAL STRUCTURE QUALITY
REMARK 210 FACTORS FOR THE ENSEMBLE (RESIDUES 18 TO 120), WHERE ORDERED
REMARK 210 RESIDUES [S(PHI) + S(PSI) > 1.8] COMPRISE 19-33,42-56,61-62,64-
REMARK 210 74,77-79,83-119: (A) RMSD FOR ORDERED RESIDUES: BB, 1.2; HEAVY
REMARK 210 ATOM, 1.7 (B) RAMACHANDRAN STATISTICS FOR ORDERED RESIDUES: MOST
REMARK 210 FAVORED: 93.0%; ADDITIONALLY ALLOWED: 5.7%; GENEROUSLY ALLOWED,
REMARK 210 0.8%; DISALLOWED, 0.5% (C) PROCHECK SCORES FOR ORDERED RESIDUES
REMARK 210 (RAW/Z-): BB, 0.20/1.10; ALL, -0.02/-0.12. (D) MAGE MOLPROBITY
REMARK 210 CLASH SCORE (RAW/Z-): 33.54/-4.23. (E) RPF SCORES FOR GOODNESS
REMARK 210 OF FIT TO NOESY DATA: F-MEASURE, 0.834; RECALL, 0.900; PRECISION,
REMARK 210 0.776; DP-SCORE, 0.606.
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 SER A 9
REMARK 465 HIS A 10
REMARK 465 MET A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 GLY A 16
REMARK 465 PHE A 17
REMARK 465 ALA A 121
REMARK 465 PRO A 122
REMARK 465 SER A 123
REMARK 465 VAL A 124
REMARK 465 GLY A 125
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 H MET A 42 HD3 LYS A 80 1.28
REMARK 500 HG2 LYS A 80 H ALA A 81 1.29
REMARK 500 OD2 ASP A 29 HZ3 LYS A 33 1.57
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 38 74.85 -107.30
REMARK 500 1 ALA A 39 93.65 -161.05
REMARK 500 1 THR A 40 61.39 61.66
REMARK 500 1 PRO A 77 -168.48 -69.49
REMARK 500 1 LYS A 79 -75.25 -67.39
REMARK 500 1 LYS A 80 -167.39 179.54
REMARK 500 1 ALA A 81 -118.09 -149.51
REMARK 500 1 THR A 82 -167.30 -168.12
REMARK 500 1 LYS A 103 -52.27 105.28
REMARK 500 2 PHE A 34 -152.34 -89.36
REMARK 500 2 ALA A 39 42.45 -85.45
REMARK 500 2 GLU A 41 148.45 -172.01
REMARK 500 2 THR A 75 -86.38 -130.02
REMARK 500 2 LYS A 80 -152.11 56.97
REMARK 500 2 ALA A 81 -94.91 -117.45
REMARK 500 2 THR A 82 -139.70 163.99
REMARK 500 2 SER A 101 -76.19 -80.94
REMARK 500 2 LYS A 102 -76.03 -100.99
REMARK 500 2 LYS A 103 -54.18 173.04
REMARK 500 3 ALA A 36 129.82 172.67
REMARK 500 3 THR A 38 21.15 -159.19
REMARK 500 3 ASN A 59 -6.28 70.55
REMARK 500 3 THR A 75 110.69 174.24
REMARK 500 3 ALA A 81 -92.74 -146.34
REMARK 500 3 THR A 82 -175.85 172.32
REMARK 500 3 SER A 101 -60.08 -93.49
REMARK 500 3 LYS A 103 -64.31 103.07
REMARK 500 4 ALA A 36 153.74 179.39
REMARK 500 4 THR A 38 -88.32 -139.55
REMARK 500 4 ASP A 58 69.87 -165.16
REMARK 500 4 ASN A 59 -69.02 -103.23
REMARK 500 4 LYS A 60 -48.73 177.54
REMARK 500 4 LYS A 80 173.45 77.44
REMARK 500 4 THR A 82 -157.11 -100.39
REMARK 500 4 SER A 101 -65.03 -100.45
REMARK 500 4 LYS A 102 -76.74 -101.70
REMARK 500 4 LYS A 103 -54.89 163.16
REMARK 500 5 ALA A 36 68.39 61.73
REMARK 500 5 LEU A 57 -165.93 -79.38
REMARK 500 5 ASP A 58 82.15 -63.66
REMARK 500 5 LYS A 60 -78.71 -134.47
REMARK 500 5 THR A 75 115.55 177.02
REMARK 500 5 ALA A 81 -84.75 -108.45
REMARK 500 5 THR A 82 -164.60 177.95
REMARK 500 5 GLU A 85 -72.84 -41.75
REMARK 500 5 SER A 101 -75.66 -100.58
REMARK 500 5 LYS A 103 -59.10 101.90
REMARK 500 5 LEU A 119 32.05 -69.10
REMARK 500 6 LYS A 33 -79.45 -93.56
REMARK 500 6 ASP A 58 76.11 51.95
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: WR33 RELATED DB: TARGETDB
DBREF 1PUL A 11 125 UNP P91127 YBYK_CAEEL 1 115
SEQADV 1PUL MET A 1 UNP P91127 EXPRESSION TAG
SEQADV 1PUL GLY A 2 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 3 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 4 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 5 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 6 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 7 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 8 UNP P91127 EXPRESSION TAG
SEQADV 1PUL SER A 9 UNP P91127 EXPRESSION TAG
SEQADV 1PUL HIS A 10 UNP P91127 EXPRESSION TAG
SEQRES 1 A 125 MET GLY HIS HIS HIS HIS HIS HIS SER HIS MET ALA ALA
SEQRES 2 A 125 ALA ALA GLY PHE ASN TRP ASP ASP ALA ASP VAL LYS LYS
SEQRES 3 A 125 ARG TRP ASP ALA PHE THR LYS PHE GLY ALA ALA THR ALA
SEQRES 4 A 125 THR GLU MET THR GLY LYS ASN PHE ASP LYS TRP LEU LYS
SEQRES 5 A 125 ASP ALA GLY VAL LEU ASP ASN LYS ALA ILE THR GLY THR
SEQRES 6 A 125 MET THR GLY ILE ALA PHE SER LYS VAL THR GLY PRO LYS
SEQRES 7 A 125 LYS LYS ALA THR PHE ASP GLU THR LYS LYS VAL LEU ALA
SEQRES 8 A 125 PHE VAL ALA GLU ASP ARG ALA ARG GLN SER LYS LYS PRO
SEQRES 9 A 125 ILE GLN ASP GLU LEU ASP ALA ILE THR GLU LYS LEU ALA
SEQRES 10 A 125 LYS LEU GLU ALA PRO SER VAL GLY
HELIX 1 1 ASP A 20 GLY A 35 1 16
HELIX 2 2 THR A 43 GLY A 55 1 13
HELIX 3 3 THR A 63 THR A 75 1 13
HELIX 4 4 THR A 82 LYS A 102 1 21
HELIX 5 5 PRO A 104 LEU A 119 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 - r 2 2 Bytes