Header list of 1nfa.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION REGULATION 18-JAN-97 1NFA
TITLE HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN TRANSCRIPTION FACTOR NFATC1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN, RESIDUES 416 - 591;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM UNTIL DEPHOSPHORYLATED;
SOURCE 7 GENE: NFATC1;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE 13 EXPRESSION_SYSTEM_GENE: NFATC1
KEYWDS NFAT, TRANSCRIPTION REGULATION, REL-HOMOLOGY FOLD, ACTIVATES CYTOKINE
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.A.WOLFE,P.ZHOU,V.DOTSCH,L.CHEN,A.YOU,S.N.HO,G.R.CRABTREE,G.WAGNER,
AUTHOR 2 G.L.VERDINE
REVDAT 3 23-FEB-22 1NFA 1 REMARK
REVDAT 2 24-FEB-09 1NFA 1 VERSN
REVDAT 1 01-APR-97 1NFA 0
JRNL AUTH S.A.WOLFE,P.ZHOU,V.DOTSCH,L.CHEN,A.YOU,S.N.HO,G.R.CRABTREE,
JRNL AUTH 2 G.WAGNER,G.L.VERDINE
JRNL TITL UNUSUAL REL-LIKE ARCHITECTURE IN THE DNA-BINDING DOMAIN OF
JRNL TITL 2 THE TRANSCRIPTION FACTOR NFATC.
JRNL REF NATURE V. 385 172 1997
JRNL REFN ISSN 0028-0836
JRNL PMID 8990122
JRNL DOI 10.1038/385172A0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CALCULATIONS WERE PERFORMED BASED ON
REMARK 3 1087 EFFECTIVE NON-HYDROGEN-BOND CONSTRAINTS WITH 3 REDAC
REMARK 3 CYCLES. STRUCTURES WITH TARGET FUNCTIONS BELOW 10 WERE FURTHER
REMARK 3 REFINED BY SIMULATED ANNEALING USING X-PLOR.
REMARK 4
REMARK 4 1NFA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175265.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N NOESY-HSQC; 2D 1H-1H
REMARK 210 NOESY; 3D 13C NOESY-HSQC; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX-500; UNITY PLUS 750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, XPLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST BACKBONE RMSD TO THE
REMARK 210 MEAN
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 USING 13C, 15N-LABELED NFATC. IONIC_STRENGTH: 100
REMARK 210 MM KCL PRESSURE: NULL SOLVENT SYSTEM: H2O
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: 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 LYS A 2 -153.77 -154.44
REMARK 500 1 GLN A 5 77.88 174.42
REMARK 500 1 SER A 8 41.35 -155.68
REMARK 500 1 SER A 10 55.10 -166.23
REMARK 500 1 PRO A 12 -163.03 -77.18
REMARK 500 1 GLU A 14 126.80 -172.31
REMARK 500 1 LYS A 22 162.60 -43.18
REMARK 500 1 SER A 23 50.02 -119.48
REMARK 500 1 HIS A 25 118.60 -170.40
REMARK 500 1 HIS A 28 55.93 -162.75
REMARK 500 1 TYR A 29 115.03 -179.93
REMARK 500 1 GLU A 30 74.23 173.42
REMARK 500 1 THR A 31 32.64 -145.69
REMARK 500 1 GLU A 32 -72.62 -102.72
REMARK 500 1 SER A 34 -38.99 -154.75
REMARK 500 1 ARG A 35 42.50 -161.57
REMARK 500 1 ALA A 40 -152.94 -74.24
REMARK 500 1 PRO A 46 -167.93 -79.43
REMARK 500 1 LEU A 54 35.61 -99.96
REMARK 500 1 ASN A 56 34.60 -87.72
REMARK 500 1 ASP A 70 -55.26 -142.50
REMARK 500 1 ARG A 71 -34.66 -174.66
REMARK 500 1 LEU A 72 86.80 -66.34
REMARK 500 1 ALA A 77 -76.29 -67.12
REMARK 500 1 HIS A 82 59.38 -175.93
REMARK 500 1 THR A 85 -147.39 -145.52
REMARK 500 1 SER A 99 103.68 77.03
REMARK 500 1 THR A 101 87.96 -159.58
REMARK 500 1 ASN A 112 -67.52 -165.39
REMARK 500 1 SER A 113 108.05 164.63
REMARK 500 1 MET A 114 49.83 -154.67
REMARK 500 1 ASP A 119 39.48 -149.50
REMARK 500 1 CYS A 120 59.03 -145.05
REMARK 500 1 LEU A 126 24.13 -141.77
REMARK 500 1 ASN A 128 27.60 -168.66
REMARK 500 1 ASP A 130 68.23 163.93
REMARK 500 1 ARG A 134 -61.01 -167.06
REMARK 500 1 LYS A 135 142.48 164.73
REMARK 500 1 THR A 138 -49.06 -152.16
REMARK 500 1 ASP A 139 -70.91 166.13
REMARK 500 1 ILE A 140 -42.30 -145.22
REMARK 500 1 ARG A 142 52.20 -140.95
REMARK 500 1 ASN A 144 164.11 -47.11
REMARK 500 1 THR A 145 51.48 -154.43
REMARK 500 1 THR A 162 -79.77 -136.39
REMARK 500 1 SER A 164 106.34 -163.83
REMARK 500 1 ASN A 170 92.49 171.74
REMARK 500 1 ILE A 172 78.74 -115.21
REMARK 500 2 GLN A 5 79.32 170.47
REMARK 500 2 SER A 10 -175.05 64.82
REMARK 500
REMARK 500 THIS ENTRY HAS 437 RAMACHANDRAN OUTLIERS.
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 1 ARG A 16 0.21 SIDE CHAIN
REMARK 500 1 ARG A 26 0.28 SIDE CHAIN
REMARK 500 1 ARG A 35 0.31 SIDE CHAIN
REMARK 500 1 ARG A 71 0.24 SIDE CHAIN
REMARK 500 1 ARG A 74 0.31 SIDE CHAIN
REMARK 500 1 ARG A 83 0.22 SIDE CHAIN
REMARK 500 1 ARG A 115 0.32 SIDE CHAIN
REMARK 500 1 ARG A 127 0.11 SIDE CHAIN
REMARK 500 1 ARG A 134 0.32 SIDE CHAIN
REMARK 500 1 ARG A 142 0.23 SIDE CHAIN
REMARK 500 1 ARG A 146 0.17 SIDE CHAIN
REMARK 500 1 ARG A 148 0.30 SIDE CHAIN
REMARK 500 1 ARG A 152 0.31 SIDE CHAIN
REMARK 500 1 ARG A 161 0.16 SIDE CHAIN
REMARK 500 1 ARG A 177 0.32 SIDE CHAIN
REMARK 500 2 ARG A 16 0.31 SIDE CHAIN
REMARK 500 2 ARG A 26 0.32 SIDE CHAIN
REMARK 500 2 ARG A 35 0.13 SIDE CHAIN
REMARK 500 2 ARG A 71 0.23 SIDE CHAIN
REMARK 500 2 ARG A 74 0.16 SIDE CHAIN
REMARK 500 2 ARG A 83 0.12 SIDE CHAIN
REMARK 500 2 ARG A 115 0.32 SIDE CHAIN
REMARK 500 2 ARG A 127 0.15 SIDE CHAIN
REMARK 500 2 ARG A 134 0.25 SIDE CHAIN
REMARK 500 2 ARG A 142 0.15 SIDE CHAIN
REMARK 500 2 ARG A 146 0.11 SIDE CHAIN
REMARK 500 2 ARG A 148 0.10 SIDE CHAIN
REMARK 500 2 ARG A 152 0.32 SIDE CHAIN
REMARK 500 2 ARG A 161 0.32 SIDE CHAIN
REMARK 500 2 ARG A 177 0.24 SIDE CHAIN
REMARK 500 3 ARG A 16 0.31 SIDE CHAIN
REMARK 500 3 ARG A 26 0.21 SIDE CHAIN
REMARK 500 3 ARG A 35 0.24 SIDE CHAIN
REMARK 500 3 ARG A 71 0.24 SIDE CHAIN
REMARK 500 3 ARG A 74 0.18 SIDE CHAIN
REMARK 500 3 ARG A 115 0.32 SIDE CHAIN
REMARK 500 3 ARG A 127 0.30 SIDE CHAIN
REMARK 500 3 ARG A 134 0.29 SIDE CHAIN
REMARK 500 3 ARG A 142 0.18 SIDE CHAIN
REMARK 500 3 ARG A 146 0.26 SIDE CHAIN
REMARK 500 3 ARG A 148 0.31 SIDE CHAIN
REMARK 500 3 ARG A 152 0.31 SIDE CHAIN
REMARK 500 3 ARG A 161 0.31 SIDE CHAIN
REMARK 500 3 ARG A 177 0.20 SIDE CHAIN
REMARK 500 4 ARG A 16 0.13 SIDE CHAIN
REMARK 500 4 ARG A 26 0.13 SIDE CHAIN
REMARK 500 4 ARG A 35 0.26 SIDE CHAIN
REMARK 500 4 ARG A 71 0.23 SIDE CHAIN
REMARK 500 4 ARG A 74 0.16 SIDE CHAIN
REMARK 500 4 ARG A 83 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 147 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NFA A 3 178 UNP O95644 NFAC1_HUMAN 416 591
SEQRES 1 A 178 MET LYS ASP TRP GLN LEU PRO SER HIS SER GLY PRO TYR
SEQRES 2 A 178 GLU LEU ARG ILE GLU VAL GLN PRO LYS SER HIS HIS ARG
SEQRES 3 A 178 ALA HIS TYR GLU THR GLU GLY SER ARG GLY ALA VAL LYS
SEQRES 4 A 178 ALA SER ALA GLY GLY HIS PRO ILE VAL GLN LEU HIS GLY
SEQRES 5 A 178 TYR LEU GLU ASN GLU PRO LEU MET LEU GLN LEU PHE ILE
SEQRES 6 A 178 GLY THR ALA ASP ASP ARG LEU LEU ARG PRO HIS ALA PHE
SEQRES 7 A 178 TYR GLN VAL HIS ARG ILE THR GLY LYS THR VAL SER THR
SEQRES 8 A 178 THR SER HIS GLU ALA ILE LEU SER ASN THR LYS VAL LEU
SEQRES 9 A 178 GLU ILE PRO LEU LEU PRO GLU ASN SER MET ARG ALA VAL
SEQRES 10 A 178 ILE ASP CYS ALA GLY ILE LEU LYS LEU ARG ASN SER ASP
SEQRES 11 A 178 ILE GLU LEU ARG LYS GLY GLU THR ASP ILE GLY ARG LYS
SEQRES 12 A 178 ASN THR ARG VAL ARG LEU VAL PHE ARG VAL HIS VAL PRO
SEQRES 13 A 178 GLN PRO SER GLY ARG THR LEU SER LEU GLN VAL ALA SER
SEQRES 14 A 178 ASN PRO ILE GLU CYS SER GLN ARG SER
HELIX 1 1 ALA A 40 GLY A 44 5 5
SHEET 1 A 4 ARG A 148 ARG A 152 0
SHEET 2 A 4 PRO A 58 GLY A 66 -1 N GLY A 66 O ARG A 148
SHEET 3 A 4 LYS A 102 LEU A 109 -1 N LEU A 108 O LEU A 59
SHEET 4 A 4 GLU A 95 ILE A 97 -1 N ALA A 96 O VAL A 103
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