Header list of 1vex.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 06-APR-04 1VEX
TITLE F-SPONDIN TSR DOMAIN 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F-SPONDIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: F-SPONDIN TSR DOMAIN 4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS F-SPONDIN, TSR, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.PAAKKONEN,H.TOSSAVAINEN,P.PERMI,I.KILPELAINEN,P.GUNTERT
REVDAT 4 02-MAR-22 1VEX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1VEX 1 VERSN
REVDAT 2 19-SEP-06 1VEX 1 JRNL
REVDAT 1 19-APR-05 1VEX 0
JRNL AUTH K.PAAKKONEN,H.TOSSAVAINEN,P.PERMI,H.RAKKOLAINEN,H.RAUVALA,
JRNL AUTH 2 E.RAULO,I.KILPELAINEN,P.GUNTERT
JRNL TITL SOLUTION STRUCTURES OF THE FIRST AND FOURTH TSR DOMAINS OF
JRNL TITL 2 F-SPONDIN
JRNL REF PROTEINS V. 64 665 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16736493
JRNL DOI 10.1002/PROT.21030
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.30, OPALP 1.3
REMARK 3 AUTHORS : GUNTERT, P. ET AL. (CYANA), KORADI, R. ET AL.
REMARK 3 (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 848 RESTRAINTS, 825 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 23 PHI
REMARK 3 ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1VEX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000006542.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283.15
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-13C, U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; SCT-HMSQC-HA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE FIRST TWO AMINOACIDS (GS) OF THE SEQUENCE COME FROM
REMARK 210 THE EXPRESSION SYSTEM AND ARE NOT PART OF THE NATIVE DOMAIN
REMARK 210 SEQUENCE
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: 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 ARG A 639 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ARG A 635 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 7 ARG A 637 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 7 ARG A 637 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 12 VAL A 628 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 13 ARG A 637 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 13 ARG A 637 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 16 ARG A 637 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 16 ARG A 637 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 17 ARG A 637 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 18 ARG A 639 NE - CZ - NH2 ANGL. DEV. = -3.7 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 ASP A 649 111.13 -167.58
REMARK 500 1 PRO A 663 -176.29 -68.27
REMARK 500 2 LEU A 616 85.68 -64.64
REMARK 500 2 ALA A 645 -80.26 -132.95
REMARK 500 2 ASN A 651 15.42 53.63
REMARK 500 3 LEU A 641 156.57 -48.22
REMARK 500 3 ALA A 645 -73.58 -135.76
REMARK 500 4 ASP A 625 -89.54 -53.32
REMARK 500 4 ASN A 651 41.21 -89.61
REMARK 500 4 PRO A 663 -178.94 -69.77
REMARK 500 5 CYS A 626 -168.46 172.60
REMARK 500 5 ALA A 645 -91.14 -78.23
REMARK 500 6 PRO A 614 -84.33 -67.99
REMARK 500 6 CYS A 615 78.92 -69.80
REMARK 500 6 ASP A 625 -73.72 -45.51
REMARK 500 6 CYS A 626 -167.04 -172.37
REMARK 500 6 ASP A 649 -43.12 -149.98
REMARK 500 7 ALA A 645 -63.24 -120.08
REMARK 500 7 ASP A 649 -76.11 -29.23
REMARK 500 7 LEU A 654 -48.66 -133.30
REMARK 500 8 ASP A 625 -78.50 -23.83
REMARK 500 8 SER A 627 33.36 -99.18
REMARK 500 8 MET A 634 137.86 -172.47
REMARK 500 8 ARG A 639 -165.38 -125.53
REMARK 500 8 MET A 661 104.71 -164.89
REMARK 500 9 ALA A 645 -87.83 -143.20
REMARK 500 9 LEU A 647 -84.21 -134.78
REMARK 500 10 ALA A 645 -75.37 -87.95
REMARK 500 11 SER A 612 17.42 59.67
REMARK 500 11 MET A 634 130.55 177.50
REMARK 500 11 LEU A 644 -19.19 -140.08
REMARK 500 11 GLU A 646 78.11 41.14
REMARK 500 11 LEU A 647 -7.90 -59.28
REMARK 500 11 ASP A 649 107.51 155.70
REMARK 500 12 PRO A 614 -158.42 -83.82
REMARK 500 12 SER A 627 -78.85 -67.99
REMARK 500 12 ALA A 645 -89.30 -125.41
REMARK 500 12 LEU A 647 94.02 -162.58
REMARK 500 12 ASP A 649 -39.36 -146.70
REMARK 500 12 GLU A 652 -158.25 -74.61
REMARK 500 12 PRO A 663 -178.55 -64.05
REMARK 500 13 SER A 612 103.58 -59.09
REMARK 500 13 LEU A 616 95.75 -69.82
REMARK 500 13 SER A 627 1.88 -69.46
REMARK 500 13 CYS A 660 -32.24 -134.45
REMARK 500 13 MET A 661 82.84 15.54
REMARK 500 14 SER A 621 -178.46 -67.02
REMARK 500 14 LYS A 642 31.54 -86.66
REMARK 500 14 ALA A 645 -75.36 -140.65
REMARK 500 14 LEU A 647 -159.29 -137.72
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 3 ARG A 639 0.07 SIDE CHAIN
REMARK 500 4 ARG A 635 0.08 SIDE CHAIN
REMARK 500 4 ARG A 637 0.09 SIDE CHAIN
REMARK 500 7 ARG A 635 0.11 SIDE CHAIN
REMARK 500 9 ARG A 637 0.10 SIDE CHAIN
REMARK 500 10 ARG A 637 0.08 SIDE CHAIN
REMARK 500 20 ARG A 635 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VEX A 613 666 UNP P35446 SPON1_RAT 613 666
SEQADV 1VEX GLY A 611 UNP P35446 CLONING ARTIFACT
SEQADV 1VEX SER A 612 UNP P35446 CLONING ARTIFACT
SEQRES 1 A 56 GLY SER ILE PRO CYS LEU LEU SER PRO TRP SER GLU TRP
SEQRES 2 A 56 SER ASP CYS SER VAL THR CYS GLY LYS GLY MET ARG THR
SEQRES 3 A 56 ARG GLN ARG MET LEU LYS SER LEU ALA GLU LEU GLY ASP
SEQRES 4 A 56 CYS ASN GLU ASP LEU GLU GLN ALA GLU LYS CYS MET LEU
SEQRES 5 A 56 PRO GLU CYS PRO
SHEET 1 A 2 MET A 634 GLN A 638 0
SHEET 2 A 2 GLU A 655 LYS A 659 -1 O GLU A 658 N ARG A 635
SSBOND 1 CYS A 615 CYS A 650 1555 1555 2.01
SSBOND 2 CYS A 626 CYS A 660 1555 1555 2.04
SSBOND 3 CYS A 630 CYS A 665 1555 1555 2.03
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 2 2 Bytes