Header list of 2ezi.pdb file
Complete list - r 9 2 Bytes
HEADER DNA BINDING PROTEIN 25-JUL-97 2EZI
TITLE SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA
TITLE 2 BINDING DOMAIN OF MU PHAGE TRANSPOSASE, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSPOSASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IGAMMA SUBDOMAIN, RESIDUES 174 - 247;
COMPND 5 OTHER_DETAILS: MUA OF PHAGE MU TRANSPOSASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE MU;
SOURCE 3 ORGANISM_TAXID: 10677
KEYWDS DNA-BINDING PROTEIN, TRANSPOSITION, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.M.CLORE,R.T.CLUBB,S.SCHUMAKER,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2EZI 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 2EZI 1 VERSN
REVDAT 1 03-DEC-97 2EZI 0
JRNL AUTH R.T.CLUBB,S.SCHUMACHER,K.MIZUUCHI,A.M.GRONENBORN,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE I GAMMA SUBDOMAIN OF THE MU END
JRNL TITL 2 DNA-BINDING DOMAIN OF PHAGE MU TRANSPOSASE.
JRNL REF J.MOL.BIOL. V. 273 19 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9367742
JRNL DOI 10.1006/JMBI.1997.1312
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR (SEE ABOVE)), BRUNGER (X-PLOR (SEE
REMARK 3 ABOVE))
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A
REMARK 3 TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR
REMARK 3 NMR AND IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS:
REMARK 3 264 SEQUENTIAL (|I- J|=1), 282 MEDIUM RANGE (1 < |I-J| <=5)
REMARK 3 AND 178 LONG RANGE (|I-J| >5) INTERRESIDUES AND 245
REMARK 3 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS;
REMARK 3 40 DISTANCE RESTRAINTS FOR 20 BACKBONE H-BONDS;
REMARK 3 108 TORSION ANGLE RESTRAINTS; 47 THREE-BOND HN-HA COUPLING
REMARK 3 CONSTANT RESTRAINTS; AND 129 (66 CALPHA AND 63 CBETA) 13C
REMARK 3 SHIFT RESTRAINTS.
REMARK 3
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229,
REMARK 3 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO
REMARK 3 INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J.
REMARK 3 MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL
REMARK 3 SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B
REMARK 3 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE
REMARK 3 POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI. 5,
REMARK 3 1067-1080; KUSZEWSKI ET AL. (1997) J. MAGN. RESON 125,
REMARK 3 171-177).
REMARK 3
REMARK 3 THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN
REMARK 3 ENTRY 2EZH AND 30 STRUCTURES ARE PRESENTED IN ENTRY 2EZI,
REMARK 3 AND THE EXPERIMENTAL RESTRAINTS IN 2EZHMR. IN THE
REMARK 3 RESTRAINED REGULARIZED MEAN COORDINATES (2EZH) THE LAST
REMARK 3 COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE
REMARK 3 INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN
REMARK 3 COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO GENERATE
REMARK 3 THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 180 -
REMARK 3 240. NOTE THAT THE OCCUPANCY FIELD HAS NO MEANING.
REMARK 4
REMARK 4 2EZI 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_1000178060.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600
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 : 30
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 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 ALA A 199 H CYS A 203 1.55
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 179 10.98 -149.41
REMARK 500 1 ASP A 232 159.84 101.86
REMARK 500 1 GLU A 241 -4.40 -57.13
REMARK 500 1 LEU A 246 -43.96 -155.46
REMARK 500 2 PRO A 195 0.09 -65.45
REMARK 500 2 LYS A 197 66.67 64.26
REMARK 500 2 ASP A 232 153.48 110.07
REMARK 500 2 HIS A 244 -11.04 -153.68
REMARK 500 3 LEU A 231 -84.67 -67.48
REMARK 500 3 ASP A 232 147.58 -175.81
REMARK 500 3 ARG A 240 58.47 -91.96
REMARK 500 3 GLU A 243 -53.28 -160.76
REMARK 500 4 LYS A 197 59.39 39.75
REMARK 500 4 PRO A 198 -172.91 -54.17
REMARK 500 4 LEU A 231 -86.07 -68.59
REMARK 500 5 GLU A 179 83.48 -168.56
REMARK 500 5 PRO A 195 12.78 -60.19
REMARK 500 5 LEU A 231 -86.42 -70.67
REMARK 500 5 ASP A 232 147.62 -174.93
REMARK 500 6 LYS A 197 74.47 42.54
REMARK 500 6 PRO A 198 -175.28 -50.06
REMARK 500 6 ASP A 232 153.31 113.47
REMARK 500 7 HIS A 176 -110.28 -140.05
REMARK 500 7 GLU A 179 52.87 -100.19
REMARK 500 7 PRO A 198 -179.12 -56.60
REMARK 500 7 ASP A 232 150.49 174.33
REMARK 500 8 GLU A 179 38.43 -158.29
REMARK 500 8 PHE A 180 -79.74 -90.75
REMARK 500 8 PRO A 195 -6.08 -47.26
REMARK 500 8 LYS A 197 59.25 38.44
REMARK 500 8 LEU A 231 -75.60 -72.31
REMARK 500 8 ASP A 232 148.76 174.71
REMARK 500 8 GLU A 243 118.90 -160.46
REMARK 500 8 ALA A 245 63.75 -162.97
REMARK 500 9 PHE A 180 7.06 -156.35
REMARK 500 9 ASP A 181 4.50 -53.75
REMARK 500 9 PRO A 195 -35.68 -39.53
REMARK 500 9 PRO A 198 174.63 -52.73
REMARK 500 9 ASP A 232 156.35 102.90
REMARK 500 10 LYS A 197 65.29 65.97
REMARK 500 10 LEU A 231 -78.34 -70.94
REMARK 500 10 ASP A 232 144.07 -177.72
REMARK 500 10 HIS A 244 28.44 -147.77
REMARK 500 10 ALA A 245 -71.43 -79.99
REMARK 500 11 ASP A 181 108.44 -49.33
REMARK 500 11 LYS A 197 62.43 66.07
REMARK 500 11 LEU A 231 -90.17 -66.33
REMARK 500 11 CYS A 239 -111.35 -74.46
REMARK 500 11 GLU A 243 -37.76 -159.53
REMARK 500 12 PRO A 195 -5.93 -58.38
REMARK 500
REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EZH RELATED DB: PDB
DBREF 2EZI A 174 247 UNP P07636 TRA_BPMU 174 247
SEQRES 1 A 75 MET ASN VAL HIS LYS SER GLU PHE ASP GLU ASP ALA TRP
SEQRES 2 A 75 GLN PHE LEU ILE ALA ASP TYR LEU ARG PRO GLU LYS PRO
SEQRES 3 A 75 ALA PHE ARG LYS CYS TYR GLU ARG LEU GLU LEU ALA ALA
SEQRES 4 A 75 ARG GLU HIS GLY TRP SER ILE PRO SER ARG ALA THR ALA
SEQRES 5 A 75 PHE ARG ARG ILE GLN GLN LEU ASP GLU ALA MET VAL VAL
SEQRES 6 A 75 ALA CYS ARG GLU GLY GLU HIS ALA LEU MET
HELIX 1 1 GLU A 182 TYR A 192 1 11
HELIX 2 2 PHE A 200 HIS A 214 1 15
HELIX 3 3 ARG A 221 LEU A 231 1 11
HELIX 4 4 GLU A 233 ARG A 240 5 8
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 9 2 Bytes