Header list of 1rfh.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 09-NOV-03 1RFH
TITLE SOLUTION STRUCTURE OF THE C1 DOMAIN OF NORE1, A NOVEL RAS EFFECTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS ASSOCIATION (RALGDS/AF-6) DOMAIN FAMILY 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYSTEINE-RICH DOMAIN;
COMPND 5 SYNONYM: NOVEL RAS EFFECTOR 1, RAP1-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RASSF5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T1
KEYWDS ZINC, SIGNAL TRANSDUCTION, APOPTOSIS, CYSTEINE RICH DOMAIN, METAL
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR E.GUIBERMAN,S.WOHLGEMUTH,C.HERRMANN,S.HARJES,K.H.MUELLER,P.BAYER
REVDAT 3 02-MAR-22 1RFH 1 REMARK LINK
REVDAT 2 24-FEB-09 1RFH 1 VERSN
REVDAT 1 14-JUN-05 1RFH 0
JRNL AUTH E.GUIBERMAN,S.WOHLGEMUTH,C.HERRMANN,S.HARJES,K.H.MUELLER,
JRNL AUTH 2 P.BAYER
JRNL TITL THE SOLUTION STRUCTURE OF C1 DOMAIN OF NORE1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AURELIA 2.8.11, CNS 1.1
REMARK 3 AUTHORS : BRUKER (AURELIA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 557 RESTRAINTS, 475 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 48 DIHEDRAL ANGLE RESTRAINTS, 34 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1RFH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020700.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300
REMARK 210 PH : 6.9; 6.9; 6.9
REMARK 210 IONIC STRENGTH : 0.5 MM NAN3; 0.5 MM NAN3; 0.5 MM
REMARK 210 NAN3
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.6MM C1 DOMAIN UNLABELED, 20MM
REMARK 210 PHOSPHATE BUFFER K; 2MM C1
REMARK 210 DOMAIN U-15N, 20MM PHOSPHATE
REMARK 210 BUFFER K; 2MM C1 DOMAIN U-15N/
REMARK 210 13C, 20MM PHOSPHATE BUFFER K
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
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 : XWINNMR 2.5, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
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 : 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 GLY A 130 H VAL A 139 1.56
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 GLU A 113 90.52 -60.08
REMARK 500 1 PHE A 120 100.64 53.96
REMARK 500 1 ALA A 124 92.69 -58.99
REMARK 500 1 CYS A 132 83.20 -59.87
REMARK 500 1 ARG A 137 -167.38 -105.39
REMARK 500 1 GLN A 142 88.13 -58.81
REMARK 500 1 CYS A 149 -47.84 -169.79
REMARK 500 1 LYS A 150 -140.24 -82.52
REMARK 500 2 GLU A 113 90.52 -60.08
REMARK 500 2 PHE A 120 100.64 53.96
REMARK 500 2 ALA A 124 92.69 -58.99
REMARK 500 2 CYS A 132 83.20 -59.87
REMARK 500 2 ARG A 137 -167.38 -105.39
REMARK 500 2 GLN A 142 88.13 -58.81
REMARK 500 2 CYS A 149 -47.84 -169.79
REMARK 500 2 LYS A 150 -140.24 -82.52
REMARK 500 3 ARG A 114 94.75 -62.34
REMARK 500 3 PHE A 120 99.57 53.60
REMARK 500 3 PRO A 129 -178.16 -50.92
REMARK 500 3 CYS A 132 87.60 -57.17
REMARK 500 3 CYS A 135 -68.02 -91.40
REMARK 500 3 GLN A 142 92.05 -58.53
REMARK 500 3 ALA A 147 -9.02 -57.18
REMARK 500 3 CYS A 149 -48.40 -178.55
REMARK 500 3 LYS A 150 -141.76 -70.53
REMARK 500 3 SER A 155 -72.04 -48.23
REMARK 500 3 GLN A 162 69.24 -103.57
REMARK 500 3 CYS A 165 107.20 -59.54
REMARK 500 4 GLU A 113 82.30 -64.11
REMARK 500 4 PHE A 120 124.43 60.53
REMARK 500 4 ALA A 124 94.54 -64.31
REMARK 500 4 LEU A 125 -164.56 -78.91
REMARK 500 4 ARG A 126 36.74 71.74
REMARK 500 4 PRO A 129 171.64 -46.18
REMARK 500 4 CYS A 132 89.26 -50.10
REMARK 500 4 CYS A 135 -67.25 -91.73
REMARK 500 4 GLN A 142 89.79 -59.91
REMARK 500 4 ALA A 147 -9.47 -59.11
REMARK 500 4 CYS A 149 -45.54 -174.03
REMARK 500 4 LYS A 150 -141.82 -83.68
REMARK 500 5 PHE A 120 107.03 55.28
REMARK 500 5 LEU A 125 -73.16 -86.78
REMARK 500 5 ARG A 126 -72.79 65.77
REMARK 500 5 PRO A 129 179.42 -49.80
REMARK 500 5 CYS A 132 85.91 -57.94
REMARK 500 5 CYS A 135 -65.23 -92.16
REMARK 500 5 GLN A 142 98.00 -62.15
REMARK 500 5 ALA A 147 -8.54 -59.36
REMARK 500 5 CYS A 149 -46.55 -175.76
REMARK 500 5 LYS A 150 -141.83 -77.22
REMARK 500
REMARK 500 THIS ENTRY HAS 207 RAMACHANDRAN OUTLIERS.
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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 132 SG
REMARK 620 2 CYS A 135 SG 83.6
REMARK 620 3 HIS A 154 ND1 79.0 120.9
REMARK 620 4 CYS A 157 SG 132.9 105.0 127.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 118 ND1
REMARK 620 2 CYS A 146 SG 92.1
REMARK 620 3 CYS A 149 SG 80.8 84.9
REMARK 620 4 CYS A 165 SG 113.8 154.0 100.6
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
DBREF 1RFH A 108 166 UNP O70407 O70407_MOUSE 108 166
SEQRES 1 A 59 PRO ARG VAL LEU ALA GLU ARG GLY GLU GLY HIS ARG PHE
SEQRES 2 A 59 VAL GLU LEU ALA LEU ARG GLY GLY PRO GLY TRP CYS ASP
SEQRES 3 A 59 LEU CYS GLY ARG GLU VAL LEU ARG GLN ALA LEU ARG CYS
SEQRES 4 A 59 ALA ASN CYS LYS PHE THR CYS HIS SER GLU CYS ARG SER
SEQRES 5 A 59 LEU ILE GLN LEU ASP CYS ARG
HET ZN A 1 1
HET ZN A 2 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 HIS A 154 SER A 159 1 6
SHEET 1 A 3 VAL A 121 GLU A 122 0
SHEET 2 A 3 LEU A 144 ARG A 145 -1 O ARG A 145 N VAL A 121
SHEET 3 A 3 THR A 152 CYS A 153 -1 O CYS A 153 N LEU A 144
SHEET 1 B 2 GLY A 130 TRP A 131 0
SHEET 2 B 2 GLU A 138 VAL A 139 -1 O VAL A 139 N GLY A 130
LINK ZN ZN A 1 SG CYS A 132 1555 1555 2.51
LINK ZN ZN A 1 SG CYS A 135 1555 1555 2.52
LINK ZN ZN A 1 ND1 HIS A 154 1555 1555 2.23
LINK ZN ZN A 1 SG CYS A 157 1555 1555 2.30
LINK ZN ZN A 2 ND1 HIS A 118 1555 1555 2.20
LINK ZN ZN A 2 SG CYS A 146 1555 1555 2.50
LINK ZN ZN A 2 SG CYS A 149 1555 1555 2.50
LINK ZN ZN A 2 SG CYS A 165 1555 1555 2.30
SITE 1 AC1 5 CYS A 132 LEU A 134 CYS A 135 HIS A 154
SITE 2 AC1 5 CYS A 157
SITE 1 AC2 5 HIS A 118 CYS A 146 ASN A 148 CYS A 149
SITE 2 AC2 5 CYS A 165
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