Header list of 1ksq.pdb file
Complete list - v 3 2 Bytes
HEADER PROTEIN BINDING 14-JAN-02 1KSQ TITLE NMR STUDY OF THE THIRD TB DOMAIN FROM LATENT TRANSFORMING GROWTH TITLE 2 FACTOR-BETA BINDING PROTEIN-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LATENT TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THIRD TB DOMAIN; COMPND 5 SYNONYM: TRANSFORMING GROWTH FACTOR BETA-1 BINDING PROTEIN 1,TGF- COMPND 6 BETA1-BP-1; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: LTBP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30; SOURCE 11 EXPRESSION_SYSTEM_GENE: LTBP1 KEYWDS LATENT TRANSFORMING GROWTH FACTOR-BETA BINDING PROTEIN-1, LTBP-1, KEYWDS 2 TGF-BETA, TB DOMAIN, LATENCY ASSOCIATED PROPEPTIDE, LAP, PROTEIN KEYWDS 3 BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.LACK,J.M.O'LEARY,V.KNOTT,X.YUAN,D.B.RIFKIN,P.A.HANDFORD,A.K.DOWNING REVDAT 4 03-NOV-21 1KSQ 1 REMARK SEQADV REVDAT 3 24-FEB-09 1KSQ 1 VERSN REVDAT 2 25-NOV-03 1KSQ 1 AUTHOR JRNL REVDAT 1 26-AUG-03 1KSQ 0 JRNL AUTH J.LACK,J.M.O'LEARY,V.KNOTT,X.YUAN,D.B.RIFKIN,P.A.HANDFORD, JRNL AUTH 2 A.K.DOWNING JRNL TITL SOLUTION STRUCTURE OF THE THIRD TB DOMAIN FROM LTBP1 JRNL TITL 2 PROVIDES INSIGHT INTO ASSEMBLY OF THE LARGE LATENT COMPLEX JRNL TITL 3 THAT SEQUESTERS LATENT TGF-BETA. JRNL REF J.MOL.BIOL. V. 334 281 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 14607119 JRNL DOI 10.1016/J.JMB.2003.09.053 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.10 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1676 RESTRAINTS, 1610 NOE-DERIVED DISTANCE CONSTRAINTS, 36 REMARK 3 DISTANCE RESTRAINTS FOR 18 HYDROGEN BONDS, AND 30 DIHEDRAL ANGLE REMARK 3 PHI RESTRAINTS. REMARK 4 REMARK 4 1KSQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015303. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7 MM [U-15N] TB3-LTBP-1, 90% REMARK 210 H2O/10% D2O; 1.2 MM [U-15N] TB3- REMARK 210 LTBP-1, 99.9% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D REMARK 210 NOESY; HMQC-J REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : OMEGA REMARK 210 SPECTROMETER MANUFACTURER : GE REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851, NMRVIEW 3.1.2, REMARK 210 FELIX 2.30 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: 3D NOESY MIXING TIME 150MS REMARK 210 2D NOESY MIXING TIME 90MS 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 CYS A 36 H SER A 39 1.57 REMARK 500 O VAL A 30 HE1 TRP A 43 1.60 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 47.60 -91.77 REMARK 500 1 GLN A 4 141.06 172.11 REMARK 500 1 PRO A 5 97.76 -55.04 REMARK 500 1 GLU A 7 71.24 33.03 REMARK 500 1 GLU A 8 95.36 -168.24 REMARK 500 1 ASN A 15 -109.64 -67.89 REMARK 500 1 ASN A 17 -35.17 -169.12 REMARK 500 1 ASP A 18 19.10 56.27 REMARK 500 1 SER A 20 -25.85 173.31 REMARK 500 1 CYS A 22 109.33 48.87 REMARK 500 1 ASN A 24 -94.24 -79.73 REMARK 500 1 VAL A 25 75.87 70.13 REMARK 500 1 LEU A 26 83.26 87.66 REMARK 500 1 LYS A 32 -37.59 -31.10 REMARK 500 1 SER A 39 58.23 94.39 REMARK 500 1 ALA A 41 -33.01 -151.88 REMARK 500 1 ASN A 46 104.42 25.37 REMARK 500 1 CYS A 47 -20.37 86.65 REMARK 500 1 GLU A 48 58.79 -112.95 REMARK 500 1 PRO A 51 98.05 -45.11 REMARK 500 1 LEU A 55 138.39 58.78 REMARK 500 1 GLU A 59 -87.61 -39.72 REMARK 500 1 THR A 61 -30.88 -34.80 REMARK 500 1 LYS A 66 -71.71 -90.04 REMARK 500 1 ALA A 73 -74.85 81.36 REMARK 500 2 PRO A 5 93.44 -52.77 REMARK 500 2 GLU A 7 36.30 35.53 REMARK 500 2 GLU A 8 76.93 -101.62 REMARK 500 2 ASN A 15 -116.73 -62.13 REMARK 500 2 LEU A 16 -150.21 -151.45 REMARK 500 2 ASN A 17 -28.75 172.93 REMARK 500 2 SER A 20 -81.52 176.50 REMARK 500 2 LEU A 21 -33.70 -33.20 REMARK 500 2 CYS A 22 100.98 71.13 REMARK 500 2 ASN A 24 -96.74 -79.58 REMARK 500 2 VAL A 25 52.77 83.81 REMARK 500 2 LEU A 26 133.15 87.10 REMARK 500 2 ALA A 27 122.54 161.20 REMARK 500 2 LYS A 32 -30.99 -37.18 REMARK 500 2 SER A 39 120.95 153.91 REMARK 500 2 ALA A 41 -32.12 -152.16 REMARK 500 2 ASN A 46 106.93 24.81 REMARK 500 2 CYS A 47 -42.15 81.16 REMARK 500 2 PRO A 51 93.74 -51.23 REMARK 500 2 LEU A 55 133.27 68.67 REMARK 500 2 GLU A 59 -81.30 -38.07 REMARK 500 2 PHE A 60 -81.06 -33.19 REMARK 500 2 LYS A 66 -81.67 -88.98 REMARK 500 2 PRO A 72 -79.30 -88.93 REMARK 500 2 ALA A 73 37.06 168.60 REMARK 500 REMARK 500 THIS ENTRY HAS 530 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1APJ RELATED DB: PDB REMARK 900 NMR STUDY OF THE TRANSFORMING GROWTH FACTOR-BETA BINDING PROTEIN- REMARK 900 LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR STRUCTURE, 21 STRUCTURES DBREF 1KSQ A 3 75 UNP P22064 LTB1S_HUMAN 1013 1085 SEQADV 1KSQ SER A 1 UNP P22064 EXPRESSION TAG SEQADV 1KSQ ALA A 2 UNP P22064 EXPRESSION TAG SEQRES 1 A 75 SER ALA ASP GLN PRO LYS GLU GLU LYS LYS GLU CYS TYR SEQRES 2 A 75 TYR ASN LEU ASN ASP ALA SER LEU CYS ASP ASN VAL LEU SEQRES 3 A 75 ALA PRO ASN VAL THR LYS GLN GLU CYS CYS CYS THR SER SEQRES 4 A 75 GLY ALA GLY TRP GLY ASP ASN CYS GLU ILE PHE PRO CYS SEQRES 5 A 75 PRO VAL LEU GLY THR ALA GLU PHE THR GLU MET CYS PRO SEQRES 6 A 75 LYS GLY LYS GLY PHE VAL PRO ALA GLY GLU HELIX 1 1 LYS A 32 THR A 38 1 7 HELIX 2 2 THR A 57 CYS A 64 1 8 SHEET 1 A 4 ASN A 29 THR A 31 0 SHEET 2 A 4 LYS A 9 TYR A 13 -1 N LYS A 10 O VAL A 30 SHEET 3 A 4 GLY A 42 ASP A 45 -1 O GLY A 42 N TYR A 13 SHEET 4 A 4 GLU A 48 PRO A 51 -1 O GLU A 48 N ASP A 45 SSBOND 1 CYS A 12 CYS A 35 1555 1555 2.03 SSBOND 2 CYS A 22 CYS A 47 1555 1555 2.03 SSBOND 3 CYS A 36 CYS A 52 1555 1555 2.03 SSBOND 4 CYS A 37 CYS A 64 1555 1555 2.04 CISPEP 1 CYS A 52 PRO A 53 1 -0.44 CISPEP 2 CYS A 52 PRO A 53 2 -0.46 CISPEP 3 CYS A 52 PRO A 53 3 -0.70 CISPEP 4 CYS A 52 PRO A 53 4 -0.85 CISPEP 5 CYS A 52 PRO A 53 5 -0.62 CISPEP 6 CYS A 52 PRO A 53 6 -0.98 CISPEP 7 CYS A 52 PRO A 53 7 -1.24 CISPEP 8 CYS A 52 PRO A 53 8 -0.99 CISPEP 9 CYS A 52 PRO A 53 9 -0.45 CISPEP 10 CYS A 52 PRO A 53 10 -0.65 CISPEP 11 CYS A 52 PRO A 53 11 -0.94 CISPEP 12 CYS A 52 PRO A 53 12 -0.56 CISPEP 13 CYS A 52 PRO A 53 13 -0.14 CISPEP 14 CYS A 52 PRO A 53 14 -0.30 CISPEP 15 CYS A 52 PRO A 53 15 -0.63 CISPEP 16 CYS A 52 PRO A 53 16 -0.29 CISPEP 17 CYS A 52 PRO A 53 17 -0.20 CISPEP 18 CYS A 52 PRO A 53 18 0.12 CISPEP 19 CYS A 52 PRO A 53 19 -0.89 CISPEP 20 CYS A 52 PRO A 53 20 0.21 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 - v 3 2 Bytes