Header list of 1fuv.pdb file
Complete list - 23 20 Bytes
HEADER CELL ADHESION 15-SEP-00 1FUV
TITLE SOLUTION STRUCTURE OF AN RGD PEPTIDE ISOMER-A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RGD PEPTIDE ISOMER-A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: PEPTIDE WAS CHEMICALLY SYNTHESIZED
KEYWDS DOUBLE S-S BONDS, TYPE I BETA-TURN, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR N.ASSA-MUNT,X.JIA,P.LAAKKONEN,E.RUOSLAHTI
REVDAT 3 23-FEB-22 1FUV 1 REMARK
REVDAT 2 24-FEB-09 1FUV 1 VERSN
REVDAT 1 16-MAY-01 1FUV 0
JRNL AUTH N.ASSA-MUNT,X.JIA,P.LAAKKONEN,E.RUOSLAHTI
JRNL TITL SOLUTION STRUCTURES AND INTEGRIN BINDING ACTIVITIES OF AN
JRNL TITL 2 RGD PEPTIDE WITH TWO ISOMERS.
JRNL REF BIOCHEMISTRY V. 40 2373 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11327857
JRNL DOI 10.1021/BI002101F
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.RUOSLAHTI
REMARK 1 TITL RGD AND OTHER RECOGNITION SEQUENCES FOR INTEGRINS.
REMARK 1 REF ANNU.REV.CELL DEV.BIOL. V. 12 697 1996
REMARK 1 REFN ISSN 1081-0706
REMARK 1 DOI 10.1146/ANNUREV.CELLBIO.12.1.697
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : ALEX.T. BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FUV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011917.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.5 MG
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
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 : 8
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
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 ASP A 3 -57.32 -137.45
REMARK 500 1 CYS A 4 -116.02 -54.79
REMARK 500 1 ARG A 5 -47.25 -155.19
REMARK 500 1 CYS A 8 56.07 -90.83
REMARK 500 2 ASP A 3 -64.70 -136.70
REMARK 500 2 CYS A 4 -112.75 -55.52
REMARK 500 2 ARG A 5 -74.90 -152.99
REMARK 500 2 CYS A 8 32.17 -99.71
REMARK 500 2 PHE A 9 170.48 -49.00
REMARK 500 3 ASP A 3 -62.35 -128.08
REMARK 500 3 CYS A 4 -109.56 -54.64
REMARK 500 3 ARG A 5 -78.08 -153.51
REMARK 500 3 PHE A 9 172.65 -46.61
REMARK 500 4 CYS A 4 -106.47 -49.16
REMARK 500 4 ARG A 5 -87.70 -154.85
REMARK 500 4 ASP A 7 -50.72 -134.23
REMARK 500 4 PHE A 9 178.43 -54.99
REMARK 500 5 ASP A 3 -64.63 -133.17
REMARK 500 5 CYS A 4 -108.81 -52.76
REMARK 500 5 ARG A 5 -77.24 -152.75
REMARK 500 5 CYS A 8 49.50 -90.47
REMARK 500 6 ASP A 3 -62.61 -136.01
REMARK 500 6 CYS A 4 -115.14 -52.65
REMARK 500 6 ARG A 5 -45.36 -154.72
REMARK 500 6 CYS A 8 40.04 -96.24
REMARK 500 7 ASP A 3 -66.19 -134.51
REMARK 500 7 CYS A 4 -110.11 -50.61
REMARK 500 7 ARG A 5 -83.17 -153.55
REMARK 500 7 CYS A 8 41.75 -85.76
REMARK 500 8 ASP A 3 -62.90 -133.83
REMARK 500 8 CYS A 4 -112.84 -54.41
REMARK 500 8 ARG A 5 -89.60 -154.19
REMARK 500 8 ASP A 7 -49.79 -139.55
REMARK 500 8 CYS A 8 33.51 -90.31
REMARK 500 9 ASP A 3 -70.49 -136.16
REMARK 500 9 CYS A 4 -111.15 -49.93
REMARK 500 9 ARG A 5 -85.28 -153.37
REMARK 500 9 ASP A 7 -56.24 -121.50
REMARK 500 9 CYS A 8 37.32 -82.84
REMARK 500 10 ASP A 3 -63.41 -131.30
REMARK 500 10 CYS A 4 -110.73 -53.63
REMARK 500 10 ARG A 5 -85.26 -153.78
REMARK 500 10 ASP A 7 -52.29 -127.82
REMARK 500 10 CYS A 8 34.35 -88.86
REMARK 500 11 ASP A 3 -64.15 -126.36
REMARK 500 11 CYS A 4 -110.13 -51.51
REMARK 500 11 ARG A 5 -82.56 -153.72
REMARK 500 11 CYS A 8 32.15 -90.21
REMARK 500 12 ASP A 3 -65.60 -134.96
REMARK 500 12 CYS A 4 -111.15 -51.34
REMARK 500
REMARK 500 THIS ENTRY HAS 81 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 5 0.31 SIDE CHAIN
REMARK 500 2 ARG A 5 0.28 SIDE CHAIN
REMARK 500 3 ARG A 5 0.32 SIDE CHAIN
REMARK 500 4 ARG A 5 0.23 SIDE CHAIN
REMARK 500 5 ARG A 5 0.31 SIDE CHAIN
REMARK 500 6 ARG A 5 0.25 SIDE CHAIN
REMARK 500 7 ARG A 5 0.32 SIDE CHAIN
REMARK 500 8 ARG A 5 0.26 SIDE CHAIN
REMARK 500 9 ARG A 5 0.30 SIDE CHAIN
REMARK 500 10 ARG A 5 0.29 SIDE CHAIN
REMARK 500 11 ARG A 5 0.28 SIDE CHAIN
REMARK 500 12 ARG A 5 0.30 SIDE CHAIN
REMARK 500 13 ARG A 5 0.27 SIDE CHAIN
REMARK 500 14 ARG A 5 0.27 SIDE CHAIN
REMARK 500 15 ARG A 5 0.28 SIDE CHAIN
REMARK 500 16 ARG A 5 0.32 SIDE CHAIN
REMARK 500 17 ARG A 5 0.30 SIDE CHAIN
REMARK 500 18 ARG A 5 0.31 SIDE CHAIN
REMARK 500 19 ARG A 5 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FUL RELATED DB: PDB
REMARK 900 1FUL IS THE SOLUTION STRUCTURE OF AN RGD PEPTIDE ISOMER-B
DBREF 1FUV A 1 11 PDB 1FUV 1FUV 1 11
SEQRES 1 A 11 ALA CYS ASP CYS ARG GLY ASP CYS PHE CYS GLY
SSBOND 1 CYS A 2 CYS A 10 1555 1555 2.03
SSBOND 2 CYS A 4 CYS A 8 1555 1555 2.02
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 - 23 20 Bytes