Header list of 1egs.pdb file
Complete list - 16 20 Bytes
HEADER CHAPERONIN 30-JUN-97 1EGS
TITLE NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC
TITLE 2 PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROES;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOBILE LOOP;
COMPND 5 SYNONYM: 10 KD CHAPERONIN, PROTEIN CPN10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS CHAPERONIN, PROTEIN FOLDING, HEAT SHOCK
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.J.LANDRY
REVDAT 4 16-FEB-22 1EGS 1 REMARK LINK
REVDAT 3 24-FEB-09 1EGS 1 VERSN
REVDAT 2 01-APR-03 1EGS 1 JRNL
REVDAT 1 17-SEP-97 1EGS 0
JRNL AUTH S.J.LANDRY,A.TAHER,C.GEORGOPOULOS,S.M.VAN DER VIES
JRNL TITL INTERPLAY OF STRUCTURE AND DISORDER IN COCHAPERONIN MOBILE
JRNL TITL 2 LOOPS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 93 11622 1996
JRNL REFN ISSN 0027-8424
JRNL PMID 8876186
JRNL DOI 10.1073/PNAS.93.21.11622
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.LANDRY,J.ZEILSTRA-RYALLS,O.FAYET,C.GEORGOPOULOS,
REMARK 1 AUTH 2 L.M.GIERASCH
REMARK 1 TITL CHARACTERIZATION OF A FUNCTIONALLY IMPORTANT MOBILE DOMAIN
REMARK 1 TITL 2 OF GROES
REMARK 1 REF NATURE V. 364 255 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1EGS 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_1000173049.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
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 : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : VXR500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER
REMARK 210 METHOD USED : MOLECULAR DYNAMICS AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 2 LYS A 3 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 5 LYS A 3 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 5 VAL A 9 CB - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 5 LEU A 10 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 5 LEU A 10 CB - CG - CD1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 6 LEU A 10 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 6 LEU A 10 CB - CG - CD1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 10 LEU A 10 N - CA - CB ANGL. DEV. = -14.7 DEGREES
REMARK 500 10 LEU A 10 CB - CG - CD1 ANGL. DEV. = 15.2 DEGREES
REMARK 500 11 LEU A 10 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 11 LEU A 10 CB - CG - CD1 ANGL. DEV. = 14.5 DEGREES
REMARK 500 12 LYS A 3 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 12 LEU A 10 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 12 LEU A 10 CB - CG - CD1 ANGL. DEV. = 16.0 DEGREES
REMARK 500 15 LEU A 10 N - CA - CB ANGL. DEV. = -13.5 DEGREES
REMARK 500 15 LEU A 10 CB - CG - CD1 ANGL. DEV. = 15.9 DEGREES
REMARK 500 16 GLY A 6 CA - C - N ANGL. DEV. = 13.2 DEGREES
REMARK 500 18 LEU A 10 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 18 LEU A 10 CB - CG - CD1 ANGL. DEV. = 16.0 DEGREES
REMARK 500 19 LYS A 3 N - CA - CB ANGL. DEV. = -10.9 DEGREES
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 ALA A 5 90.30 -68.15
REMARK 500 1 ILE A 8 59.79 -101.15
REMARK 500 1 VAL A 9 81.44 -28.89
REMARK 500 2 ALA A 5 92.12 -68.12
REMARK 500 2 ILE A 8 67.77 -101.79
REMARK 500 2 VAL A 9 82.64 -31.03
REMARK 500 5 VAL A 9 77.00 46.21
REMARK 500 6 ILE A 8 55.12 -96.35
REMARK 500 6 VAL A 9 79.40 -26.23
REMARK 500 8 VAL A 9 88.73 -42.92
REMARK 500 9 LYS A 3 -166.28 -72.06
REMARK 500 9 SER A 4 144.66 42.40
REMARK 500 10 ILE A 8 53.83 -101.85
REMARK 500 10 VAL A 9 81.47 -31.65
REMARK 500 11 VAL A 9 78.98 -27.48
REMARK 500 12 VAL A 9 55.40 -118.66
REMARK 500 13 ALA A 5 92.14 -69.07
REMARK 500 13 VAL A 9 82.91 -32.82
REMARK 500 14 VAL A 9 86.72 -42.64
REMARK 500 15 ILE A 8 77.68 -108.17
REMARK 500 15 VAL A 9 52.07 -119.72
REMARK 500 16 ILE A 8 54.30 -98.13
REMARK 500 16 VAL A 9 81.39 -32.16
REMARK 500 17 ILE A 8 78.49 -111.51
REMARK 500 17 VAL A 9 78.85 -102.41
REMARK 500 18 VAL A 9 52.34 -119.11
REMARK 500 20 ILE A 8 70.56 38.71
REMARK 500 20 VAL A 9 74.60 -107.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 8 VAL A 9 6 -149.67
REMARK 500 ALA A 5 GLY A 6 8 -148.60
REMARK 500 ILE A 8 VAL A 9 8 -146.72
REMARK 500 LYS A 3 SER A 4 9 129.54
REMARK 500 SER A 4 ALA A 5 9 137.99
REMARK 500 ALA A 5 GLY A 6 10 -149.17
REMARK 500 ILE A 8 VAL A 9 10 -148.39
REMARK 500 ALA A 5 GLY A 6 11 -148.88
REMARK 500 ILE A 8 VAL A 9 11 -147.95
REMARK 500 VAL A 9 LEU A 10 12 129.30
REMARK 500 ALA A 5 GLY A 6 14 -147.99
REMARK 500 ILE A 8 VAL A 9 14 -145.15
REMARK 500 ILE A 8 VAL A 9 15 -146.50
REMARK 500 VAL A 9 LEU A 10 15 132.32
REMARK 500 GLY A 7 ILE A 8 16 -138.82
REMARK 500 ILE A 8 VAL A 9 16 -141.88
REMARK 500 ILE A 8 VAL A 9 18 -140.75
REMARK 500 VAL A 9 LEU A 10 18 133.11
REMARK 500 ILE A 8 VAL A 9 20 -149.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 11
DBREF 1EGS A 2 10 UNP P0A6F9 CH10_ECOLI 19 27
SEQRES 1 A 11 ACE THR LYS SER ALA GLY GLY ILE VAL LEU NH2
HET ACE A 1 6
HET NH2 A 11 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
LINK C ACE A 1 N THR A 2 1555 1555 1.34
LINK C LEU A 10 N NH2 A 11 1555 1555 1.33
CISPEP 1 GLY A 7 ILE A 8 9 -21.43
CISPEP 2 GLY A 6 GLY A 7 16 -5.79
SITE 1 AC2 1 LEU A 10
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 - 16 20 Bytes