Header list of 1ehx.pdb file
Complete list - b 16 2 Bytes
HEADER UNKNOWN FUNCTION 23-FEB-00 1EHX
TITLE NMR SOLUTION STRUCTURE OF THE LAST UNKNOWN MODULE OF THE CELLULOSOMAL
TITLE 2 SCAFFOLDIN PROTEIN CIPC OF CLOSTRIDUM CELLULOLYTICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCAFFOLDIN PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNKNOW DOMAIN;
COMPND 5 SYNONYM: CIPC;
COMPND 6 OTHER_DETAILS: HOMOLOGOUS MODULE WITH UNKNOW FUNCTION X2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM CELLULOLYTICUM;
SOURCE 3 ORGANISM_TAXID: 1521
KEYWDS BETA-BETA-BARRELS, 3.10 HELIX, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.MOSBAH,A.BELAICH,O.BORNET,J.P.BELAICH,B.HENRISSAT,H.DARBON
REVDAT 4 16-FEB-22 1EHX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1EHX 1 VERSN
REVDAT 2 01-APR-03 1EHX 1 JRNL
REVDAT 1 17-NOV-00 1EHX 0
JRNL AUTH A.MOSBAH,A.BELAICH,O.BORNET,J.P.BELAICH,B.HENRISSAT,H.DARBON
JRNL TITL SOLUTION STRUCTURE OF THE MODULE X2 1 OF UNKNOWN FUNCTION OF
JRNL TITL 2 THE CELLULOSOMAL SCAFFOLDING PROTEIN CIPC OF CLOSTRIDIUM
JRNL TITL 3 CELLULOLYTICUM.
JRNL REF J.MOL.BIOL. V. 304 201 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11080456
JRNL DOI 10.1006/JMBI.2000.4192
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1828 RESTRAINTS, 1647 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 66
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 105 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS
REMARK 4
REMARK 4 1EHX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010590.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 MM X2 UNIFORM LABELLING 15N;
REMARK 210 20 MM ACETATE BUFFER NA; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY; 2D_
REMARK 210 15N_HSQC; 2D_15N_HSQC_NOESY; 2D_
REMARK 210 15N_HSQC_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.2, DIANA 2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING AND TORSION ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 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 : 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 GLN A 39 H SER A 41 1.53
REMARK 500 O GLN A 39 N SER A 41 1.96
REMARK 500 O GLU A 62 N THR A 64 2.15
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 ASN A 7 168.77 -39.87
REMARK 500 1 PRO A 8 -157.89 -51.14
REMARK 500 1 SER A 10 140.46 -170.21
REMARK 500 1 SER A 17 9.68 -69.40
REMARK 500 1 ASP A 20 114.79 -34.44
REMARK 500 1 ASN A 28 -13.77 -37.16
REMARK 500 1 GLN A 39 89.15 -31.81
REMARK 500 1 SER A 40 -41.89 8.27
REMARK 500 1 THR A 47 107.13 10.02
REMARK 500 1 ASN A 48 -14.17 91.81
REMARK 500 1 ALA A 54 -11.69 -45.60
REMARK 500 1 PRO A 61 -161.24 -56.97
REMARK 500 1 GLU A 62 -168.87 -51.80
REMARK 500 1 ASN A 63 67.83 -39.09
REMARK 500 1 THR A 65 78.62 -101.67
REMARK 500 1 LEU A 68 81.49 -68.76
REMARK 500 1 LYS A 77 17.50 -142.58
REMARK 500 1 ASN A 78 151.53 -45.15
REMARK 500 1 PRO A 79 98.47 -60.63
REMARK 500 1 THR A 82 89.77 -69.73
REMARK 500 1 ILE A 90 -62.96 -161.10
REMARK 500 2 ASN A 7 -98.79 -54.65
REMARK 500 2 SER A 10 148.50 -170.77
REMARK 500 2 ALA A 13 149.59 -170.09
REMARK 500 2 ASP A 20 137.94 -34.89
REMARK 500 2 ASN A 28 67.75 -37.19
REMARK 500 2 GLN A 39 89.23 -31.29
REMARK 500 2 SER A 40 -41.29 -4.17
REMARK 500 2 TYR A 43 -169.32 -121.36
REMARK 500 2 THR A 47 106.67 12.74
REMARK 500 2 ASN A 48 -11.84 85.22
REMARK 500 2 ALA A 54 -9.40 -46.53
REMARK 500 2 LEU A 60 127.41 -34.70
REMARK 500 2 PRO A 61 -173.75 -53.44
REMARK 500 2 GLU A 62 -166.92 -53.76
REMARK 500 2 ASN A 63 71.60 -38.57
REMARK 500 2 LYS A 66 161.86 -42.70
REMARK 500 2 ASP A 71 94.69 -68.15
REMARK 500 2 LEU A 93 -157.51 -132.94
REMARK 500 3 ASP A 3 73.16 -113.90
REMARK 500 3 ASN A 7 -80.11 -49.94
REMARK 500 3 THR A 9 8.00 -150.00
REMARK 500 3 SER A 10 145.92 -170.31
REMARK 500 3 SER A 17 10.04 -69.53
REMARK 500 3 ASP A 20 140.94 -35.50
REMARK 500 3 ASN A 28 67.31 -36.94
REMARK 500 3 GLN A 39 90.07 -30.45
REMARK 500 3 SER A 40 -43.70 5.33
REMARK 500 3 THR A 47 97.22 24.50
REMARK 500 3 ASN A 48 -1.68 73.63
REMARK 500
REMARK 500 THIS ENTRY HAS 387 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EHX A 1 94 UNP Q45996 Q45996_CLOCE 194 287
SEQADV 1EHX MET A 1 UNP Q45996 PRO 194 CONFLICT
SEQADV 1EHX LEU A 93 UNP Q45996 ASP 286 CONFLICT
SEQADV 1EHX GLU A 94 UNP Q45996 SER 287 CONFLICT
SEQRES 1 A 94 MET GLN ASP PRO THR ILE ASN PRO THR SER ILE SER ALA
SEQRES 2 A 94 LYS ALA GLY SER PHE ALA ASP THR LYS ILE THR LEU THR
SEQRES 3 A 94 PRO ASN GLY ASN THR PHE ASN GLY ILE SER GLU LEU GLN
SEQRES 4 A 94 SER SER GLN TYR THR LYS GLY THR ASN GLU VAL THR LEU
SEQRES 5 A 94 LEU ALA SER TYR LEU ASN THR LEU PRO GLU ASN THR THR
SEQRES 6 A 94 LYS THR LEU THR PHE ASP PHE GLY VAL GLY THR LYS ASN
SEQRES 7 A 94 PRO LYS LEU THR ILE THR VAL LEU PRO LYS ASP ILE PRO
SEQRES 8 A 94 GLY LEU GLU
HELIX 1 1 SER A 36 SER A 41 5 6
HELIX 2 2 LEU A 53 LEU A 60 1 8
SHEET 1 A 4 THR A 5 ILE A 6 0
SHEET 2 A 4 THR A 21 THR A 26 -1 N THR A 26 O THR A 5
SHEET 3 A 4 GLU A 49 LEU A 52 -1 O VAL A 50 N ILE A 23
SHEET 4 A 4 TYR A 43 GLY A 46 -1 N THR A 44 O THR A 51
SHEET 1 B 3 SER A 10 ALA A 13 0
SHEET 2 B 3 LYS A 80 VAL A 85 1 O THR A 82 N ILE A 11
SHEET 3 B 3 THR A 64 THR A 69 -1 O THR A 64 N VAL A 85
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 16 2 Bytes