Header list of 1fwq.pdb file
Complete list - 23 20 Bytes
HEADER METAL BINDING PROTEIN 24-SEP-00 1FWQ
TITLE SOLUTION STRUCTURE OF HUMAN MSS4, A GUANINE NUCLEOTIDE EXCHANGE FACTOR
TITLE 2 FOR RAB PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE EXCHANGE FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ZINC-BINDING, BETA STRUCTURE, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR H.YU,S.L.SCHREIBER
REVDAT 3 23-FEB-22 1FWQ 1 REMARK
REVDAT 2 24-FEB-09 1FWQ 1 VERSN
REVDAT 1 04-OCT-00 1FWQ 0
JRNL AUTH H.YU,S.L.SCHREIBER
JRNL TITL STRUCTURE OF GUANINE-NUCLEOTIDE-EXCHANGE FACTOR HUMAN MSS4
JRNL TITL 2 AND IDENTIFICATION OF ITS RAB-INTERACTING SURFACE.
JRNL REF NATURE V. 376 788 1995
JRNL REFN ISSN 0028-0836
JRNL PMID 7651540
JRNL DOI 10.1038/376788A0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1,289 NOE-DERIVED DISTANCE CONSTRAINTS AND 117 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1FWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011963.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MM MSS4, U-15N; 40MM TRIS (PH
REMARK 210 6.5), 100MM KCL, 2MM DTT; 3MM
REMARK 210 MSS4, U-15N,13C; 40MM TRIS (PH
REMARK 210 6.5), 100MM KCL, 2MM DTT; 3MM
REMARK 210 MSS4, U-15N,13C; 40MM TRIS (PH
REMARK 210 6.5), 100MM KCL, 2MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_TOCSY; HNCA,
REMARK 210 HNCOCA, HNCO; HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 GLU A 6
REMARK 465 PRO A 7
REMARK 465 SER A 8
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 SER A 12 -170.13 -58.80
REMARK 500 CYS A 23 95.40 -48.91
REMARK 500 VAL A 30 -76.40 -71.44
REMARK 500 ARG A 40 47.62 -85.83
REMARK 500 GLN A 42 98.72 -61.92
REMARK 500 LYS A 50 -95.03 41.75
REMARK 500 LYS A 51 177.24 51.74
REMARK 500 PRO A 52 -81.03 -77.45
REMARK 500 ALA A 53 -38.92 81.93
REMARK 500 LEU A 54 110.99 67.47
REMARK 500 SER A 55 -43.50 83.60
REMARK 500 ASP A 56 -168.16 68.46
REMARK 500 ASN A 59 64.05 -164.64
REMARK 500 GLN A 66 -36.92 -147.92
REMARK 500 ASP A 73 115.00 -160.49
REMARK 500 PHE A 77 -167.28 -53.64
REMARK 500 GLU A 78 -93.38 -132.98
REMARK 500 ASN A 79 44.69 -91.17
REMARK 500 LYS A 84 162.99 -41.21
REMARK 500 VAL A 86 49.21 -89.00
REMARK 500 ASN A 88 15.46 -155.26
REMARK 500 CYS A 97 57.35 -153.84
REMARK 500 GLU A 98 97.83 -37.24
REMARK 500 ILE A 99 -69.10 -150.22
REMARK 500 ALA A 116 112.60 -33.49
REMARK 500 LEU A 117 -74.66 -51.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 16 0.27 SIDE CHAIN
REMARK 500 ARG A 18 0.14 SIDE CHAIN
REMARK 500 ARG A 25 0.21 SIDE CHAIN
REMARK 500 ARG A 40 0.31 SIDE CHAIN
REMARK 500 ARG A 41 0.28 SIDE CHAIN
REMARK 500 ARG A 49 0.31 SIDE CHAIN
REMARK 500 ARG A 119 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 124 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 23 SG
REMARK 620 2 CYS A 26 SG 109.4
REMARK 620 3 CYS A 94 SG 109.2 109.7
REMARK 620 4 CYS A 97 SG 109.6 109.3 109.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 124
DBREF 1FWQ A 1 123 UNP P47224 MSS4_HUMAN 1 123
SEQRES 1 A 123 MET GLU PRO ALA ASP GLU PRO SER GLU LEU VAL SER ALA
SEQRES 2 A 123 GLU GLY ARG ASN ARG LYS ALA VAL LEU CYS GLN ARG CYS
SEQRES 3 A 123 GLY SER ARG VAL LEU GLN PRO GLY THR ALA LEU PHE SER
SEQRES 4 A 123 ARG ARG GLN LEU PHE LEU PRO SER MET ARG LYS LYS PRO
SEQRES 5 A 123 ALA LEU SER ASP GLY SER ASN PRO ASP GLY ASP LEU LEU
SEQRES 6 A 123 GLN GLU HIS TRP LEU VAL GLU ASP MET PHE ILE PHE GLU
SEQRES 7 A 123 ASN VAL GLY PHE THR LYS ASP VAL GLY ASN ILE LYS PHE
SEQRES 8 A 123 LEU VAL CYS ALA ASP CYS GLU ILE GLY PRO ILE GLY TRP
SEQRES 9 A 123 HIS CYS LEU ASP ASP LYS ASN SER PHE TYR VAL ALA LEU
SEQRES 10 A 123 GLU ARG VAL SER HIS GLU
HET ZN A 124 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ASP A 73 PHE A 77 5 5
SHEET 1 A 3 SER A 28 LEU A 31 0
SHEET 2 A 3 ALA A 20 CYS A 23 -1 O VAL A 21 N VAL A 30
SHEET 3 A 3 SER A 121 GLU A 123 -1 N SER A 121 O LEU A 22
SHEET 1 B 2 LEU A 37 PHE A 38 0
SHEET 2 B 2 TRP A 69 LEU A 70 -1 O LEU A 70 N LEU A 37
SHEET 1 C 2 LEU A 43 LEU A 45 0
SHEET 2 C 2 ASP A 63 LEU A 65 -1 O ASP A 63 N LEU A 45
SHEET 1 D 3 ILE A 89 LEU A 92 0
SHEET 2 D 3 GLY A 103 CYS A 106 -1 O GLY A 103 N LEU A 92
SHEET 3 D 3 TYR A 114 VAL A 115 -1 O TYR A 114 N TRP A 104
LINK SG CYS A 23 ZN ZN A 124 1555 1555 2.30
LINK SG CYS A 26 ZN ZN A 124 1555 1555 2.30
LINK SG CYS A 94 ZN ZN A 124 1555 1555 2.30
LINK SG CYS A 97 ZN ZN A 124 1555 1555 2.30
CISPEP 1 GLY A 100 PRO A 101 0 0.53
SITE 1 AC1 4 CYS A 23 CYS A 26 CYS A 94 CYS A 97
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
Complete list - 23 20 Bytes