Header list of 1ymz.pdb file
Complete list - 2 20 Bytes
HEADER UNKNOWN FUNCTION 22-JAN-05 1YMZ
TITLE CC45, AN ARTIFICIAL WW DOMAIN DESIGNED USING STATISTICAL COUPLING
TITLE 2 ANALYSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CC45;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: COMPUTATIONAL DESIGN
KEYWDS ARTIFICIAL PROTEIN, COMPUTATIONAL DESIGN, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.SOCOLICH,S.W.LOCKLESS,W.P.RUSS,H.LEE,K.H.GARDNER,R.RANGANATHAN
REVDAT 3 02-MAR-22 1YMZ 1 REMARK
REVDAT 2 24-FEB-09 1YMZ 1 VERSN
REVDAT 1 27-SEP-05 1YMZ 0
JRNL AUTH M.SOCOLICH,S.W.LOCKLESS,W.P.RUSS,H.LEE,K.H.GARDNER,
JRNL AUTH 2 R.RANGANATHAN
JRNL TITL EVOLUTIONARY INFORMATION FOR SPECIFYING A PROTEIN FOLD.
JRNL REF NATURE V. 437 512 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 16177782
JRNL DOI 10.1038/NATURE03991
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, ARIA 1.2
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YMZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031700.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 600UM CC45 PROTEIN, 100MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 100MM NACL, 90%
REMARK 210 H2O:10% D2O; 1MM CC45 PROTEIN,
REMARK 210 100MM SODIUM PHOSPHATE BUFFER,
REMARK 210 100MM NACL, 99% D2O; 850UM CC45
REMARK 210 PROTEIN, U-15N, 100MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 100MM NACL, 90%
REMARK 210 H2O:10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.2.2, CNS 1.1, ARIA 1.2
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED BY A COMBINATION OF 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR-EDITED METHODS.
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 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 SER A 0
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 TRP A 30 45.29 -95.95
REMARK 500 1 ILE A 35 86.78 -67.93
REMARK 500 1 ILE A 36 132.00 74.00
REMARK 500 2 PRO A 33 109.60 -52.03
REMARK 500 2 ILE A 36 96.44 74.65
REMARK 500 3 PRO A 33 103.81 -56.34
REMARK 500 3 ILE A 36 90.48 65.55
REMARK 500 4 TRP A 30 41.46 -96.89
REMARK 500 5 THR A 34 -35.95 -161.20
REMARK 500 6 ASP A 12 -143.46 -81.63
REMARK 500 6 VAL A 13 90.48 -58.24
REMARK 500 6 GLU A 14 -29.29 76.95
REMARK 500 6 TRP A 30 32.56 -94.68
REMARK 500 6 PRO A 33 99.23 -59.19
REMARK 500 8 TRP A 30 52.39 -102.47
REMARK 500 9 ASP A 12 -83.90 -96.03
REMARK 500 9 GLU A 14 79.75 -161.13
REMARK 500 9 PRO A 33 105.11 -43.21
REMARK 500 9 ILE A 35 81.26 68.85
REMARK 500 10 ASP A 12 -79.10 -100.09
REMARK 500 10 PRO A 33 103.23 -30.22
REMARK 500 10 ILE A 36 103.38 69.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE SEQUENCE NUMBERING IS BASED ON AN ALIGNMENT OF WW
REMARK 999 DOMAINS PRESENTED IN FIGURE 1 OF PRIMARY REFERENCE, LEADING TO A
REMARK 999 GAP IN NUMBERING BETWEEN GLU 14 AND GLY 16
DBREF 1YMZ A -5 38 PDB 1YMZ 1YMZ -5 38
SEQRES 1 A 43 GLY SER HIS GLY ARG SER MET PRO LEU PRO PRO GLY TRP
SEQRES 2 A 43 GLU ARG ARG THR ASP VAL GLU GLY LYS VAL TYR TYR PHE
SEQRES 3 A 43 ASN VAL ARG THR LEU THR THR THR TRP GLU ARG PRO THR
SEQRES 4 A 43 ILE ILE LEU GLU
SHEET 1 A 3 TRP A 7 THR A 11 0
SHEET 2 A 3 VAL A 18 ASN A 22 -1 O PHE A 21 N GLU A 8
SHEET 3 A 3 THR A 27 THR A 29 -1 O THR A 29 N TYR A 20
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 - 2 20 Bytes