Header list of 1lum.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 22-MAY-02 1LUM TITLE NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287TRANS, 20 LOW ENERGY TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE ITK/TSK; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SRC HOMOLOGY 2 (SH2) DOMAIN (RESIDUES 238-344); COMPND 5 SYNONYM: INTERLEUKIN-2 TYROSINE KINASE, T-CELL-SPECIFIC KINASE, IL-2- COMPND 6 INDUCIBLE T-CELL KINASE, KINASE EMT, KINASE TLK; COMPND 7 EC: 2.7.1.112; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX KEYWDS CIS/TRANS ISOMERIZATION, INTERLEUKIN-2 TYROSINE KINASE, ITK, T-CELL KEYWDS 2 SPECIFIC KINASE, TSK, SRC HOMOLOGY 2, SH2, PROLINE, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR R.J.MALLIS,K.N.BRAZIN,D.B.FULTON,A.H.ANDREOTTI REVDAT 3 23-FEB-22 1LUM 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1LUM 1 VERSN REVDAT 1 27-NOV-02 1LUM 0 JRNL AUTH R.J.MALLIS,K.N.BRAZIN,D.B.FULTON,A.H.ANDREOTTI JRNL TITL STRUCTURAL CHARACTERIZATION OF A PROLINE-DRIVEN JRNL TITL 2 CONFORMATIONAL SWITCH WITHIN THE ITK SH2 DOMAIN JRNL REF NAT.STRUCT.BIOL. V. 9 900 2002 JRNL REFN ISSN 1072-8368 JRNL PMID 12402030 JRNL DOI 10.1038/NSB864 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR, CNS 1.0 REMARK 3 AUTHORS : BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2323 NOE REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 58 PHI/PSI DIHEDRAL ANGLE REMARK 3 RESTRAINTS,9 CHI DIHEDRAL ANGLE RESTRAINTS AND 30 DISTANCE REMARK 3 RESTRAINTS FROM HYDROGEN BONDS REMARK 4 REMARK 4 1LUM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000016286. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 125MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM ITK SH2, U-15N,13C, 125MM REMARK 210 PHOSPHATE BUFFER, PH 7.4; 1 MM REMARK 210 ITK SH2, U-15N, 125MM PHOSPHATE REMARK 210 BUFFER, PH 7.4; 1 MM ITK SH2, REMARK 210 125MM PHOSPHATE BUFFER, PH 7.4 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; DQF-COSY; 2D REMARK 210 NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 4.1.3 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND ENERGY 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: 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 PHE A 34 H VAL A 109 1.14 REMARK 500 H LYS A 67 O TYR A 77 1.31 REMARK 500 O PRO A 88 H GLN A 92 1.33 REMARK 500 O LYS A 67 HA TYR A 76 1.34 REMARK 500 O ILE A 87 H ILE A 91 1.34 REMARK 500 H VAL A 47 O TYR A 64 1.37 REMARK 500 O TYR A 45 H ILE A 66 1.39 REMARK 500 H TYR A 76 O PHE A 84 1.46 REMARK 500 O TYR A 76 H PHE A 84 1.46 REMARK 500 O TRP A 11 H VAL A 36 1.48 REMARK 500 O MET A 35 H SER A 48 1.50 REMARK 500 H VAL A 49 O LYS A 62 1.50 REMARK 500 O TYR A 45 HD1 HIS A 65 1.50 REMARK 500 H ARG A 37 O THR A 46 1.51 REMARK 500 O VAL A 47 H TYR A 64 1.52 REMARK 500 O VAL A 49 H LYS A 62 1.52 REMARK 500 O ARG A 37 H THR A 46 1.52 REMARK 500 O ALA A 33 H PHE A 50 1.54 REMARK 500 H PHE A 34 O TYR A 107 1.54 REMARK 500 O ILE A 91 H GLN A 95 1.55 REMARK 500 O ALA A 21 H LEU A 25 1.55 REMARK 500 O GLU A 22 H LEU A 26 1.55 REMARK 500 HG2 LYS A 81 CD1 TYR A 82 1.55 REMARK 500 O ILE A 87 HG12 ILE A 91 1.56 REMARK 500 H MET A 35 O SER A 48 1.57 REMARK 500 OG1 THR A 28 HZ3 LYS A 30 1.58 REMARK 500 H ALA A 33 O PHE A 50 1.58 REMARK 500 O LYS A 20 H LEU A 24 1.60 REMARK 500 O PHE A 34 N VAL A 109 1.99 REMARK 500 OG1 THR A 44 O ILE A 66 2.09 REMARK 500 O GLU A 10 O VAL A 109 2.12 REMARK 500 O HIS A 94 O ARG A 104 2.13 REMARK 500 O ILE A 87 N ILE A 91 2.16 REMARK 500 O GLY A 43 OE2 GLU A 68 2.17 REMARK 500 O ARG A 18 OE1 GLU A 22 2.18 REMARK 500 N MET A 35 O SER A 48 2.18 REMARK 500 O THR A 41 N GLY A 43 2.19 REMARK 500 N LYS A 67 O TYR A 77 2.19 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 ASN A 5 91.68 -52.52 REMARK 500 1 LEU A 6 -106.84 -16.63 REMARK 500 1 GLU A 7 92.07 35.05 REMARK 500 1 THR A 8 -14.24 151.99 REMARK 500 1 SER A 15 6.41 50.86 REMARK 500 1 LYS A 30 97.41 -29.82 REMARK 500 1 GLU A 31 109.12 -36.48 REMARK 500 1 SER A 39 -84.34 -108.81 REMARK 500 1 ARG A 40 -33.80 153.06 REMARK 500 1 THR A 41 -157.51 -49.22 REMARK 500 1 PRO A 42 -4.92 -38.09 REMARK 500 1 LYS A 52 99.77 -12.99 REMARK 500 1 ILE A 55 -155.01 -177.36 REMARK 500 1 ASN A 58 -50.36 173.57 REMARK 500 1 PRO A 59 126.37 -33.16 REMARK 500 1 ASN A 70 85.04 12.14 REMARK 500 1 ASP A 71 152.30 -26.90 REMARK 500 1 SER A 72 78.31 79.24 REMARK 500 1 LYS A 74 174.70 40.20 REMARK 500 1 ARG A 75 -52.25 -131.51 REMARK 500 1 ALA A 79 38.72 165.53 REMARK 500 1 GLU A 80 29.17 37.24 REMARK 500 1 TYR A 82 108.36 10.62 REMARK 500 1 TYR A 96 -97.82 -106.44 REMARK 500 1 ASN A 97 -175.72 -43.56 REMARK 500 1 LEU A 101 144.88 52.06 REMARK 500 1 VAL A 102 -51.08 -23.04 REMARK 500 1 THR A 103 31.02 -154.43 REMARK 500 1 LEU A 105 80.22 55.77 REMARK 500 1 TYR A 107 101.84 -167.08 REMARK 500 2 ASN A 5 151.72 -28.71 REMARK 500 2 GLU A 7 -38.04 -21.76 REMARK 500 2 SER A 15 7.28 46.53 REMARK 500 2 SER A 17 -169.07 -125.28 REMARK 500 2 GLU A 31 108.95 -36.39 REMARK 500 2 ALA A 33 109.49 -42.37 REMARK 500 2 THR A 41 -166.36 -46.04 REMARK 500 2 PRO A 42 -3.87 -42.93 REMARK 500 2 ALA A 53 147.33 171.49 REMARK 500 2 ILE A 54 -93.84 25.71 REMARK 500 2 ILE A 55 -114.83 -129.30 REMARK 500 2 ASN A 70 49.73 -95.52 REMARK 500 2 ASP A 71 152.43 50.78 REMARK 500 2 LYS A 74 -168.54 -42.26 REMARK 500 2 TYR A 77 137.37 176.74 REMARK 500 2 VAL A 78 -78.29 -86.69 REMARK 500 2 GLU A 80 34.32 28.98 REMARK 500 2 TYR A 82 91.85 -4.67 REMARK 500 2 SER A 86 143.37 -171.31 REMARK 500 2 TYR A 96 -77.04 -104.80 REMARK 500 REMARK 500 THIS ENTRY HAS 581 RAMACHANDRAN OUTLIERS. 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 112 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LUI RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287CIS, 20 LOW ENERGY REMARK 900 STRUCTURES REMARK 900 RELATED ID: 1LUK RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287CIS, ENERGY MINIMIZED REMARK 900 AVERAGED STRUCTURE REMARK 900 RELATED ID: 1LUN RELATED DB: PDB REMARK 900 NMR STRUCTURES OF THE ITK SH2 DOMAIN, PRO287TRANS ISOFORM, REMARK 900 MINIMIZED AVERAGE STRUCTURE DBREF 1LUM A 4 110 UNP Q03526 ITK_MOUSE 238 344 SEQADV 1LUM GLY A 111 UNP Q03526 CLONING ARTIFACT SEQRES 1 A 110 ACE ASN ASN LEU GLU THR TYR GLU TRP TYR ASN LYS SER SEQRES 2 A 110 ILE SER ARG ASP LYS ALA GLU LYS LEU LEU LEU ASP THR SEQRES 3 A 110 GLY LYS GLU GLY ALA PHE MET VAL ARG ASP SER ARG THR SEQRES 4 A 110 PRO GLY THR TYR THR VAL SER VAL PHE THR LYS ALA ILE SEQRES 5 A 110 ILE SER GLU ASN PRO CYS ILE LYS HIS TYR HIS ILE LYS SEQRES 6 A 110 GLU THR ASN ASP SER PRO LYS ARG TYR TYR VAL ALA GLU SEQRES 7 A 110 LYS TYR VAL PHE ASP SER ILE PRO LEU LEU ILE GLN TYR SEQRES 8 A 110 HIS GLN TYR ASN GLY GLY GLY LEU VAL THR ARG LEU ARG SEQRES 9 A 110 TYR PRO VAL CYS GLY NH2 HET ACE A 3 6 HET NH2 A 112 3 HETNAM ACE ACETYL GROUP HETNAM NH2 AMINO GROUP FORMUL 1 ACE C2 H4 O FORMUL 1 NH2 H2 N HELIX 1 1 SER A 17 GLY A 29 1 13 HELIX 2 2 SER A 86 TYR A 96 1 11 SHEET 1 A 4 ILE A 61 HIS A 65 0 SHEET 2 A 4 TYR A 45 PHE A 50 -1 N VAL A 47 O TYR A 64 SHEET 3 A 4 ALA A 33 ASP A 38 -1 N ARG A 37 O THR A 46 SHEET 4 A 4 TYR A 107 PRO A 108 1 O TYR A 107 N PHE A 34 LINK C ACE A 3 N ASN A 4 1555 1555 1.33 LINK C GLY A 111 N NH2 A 112 1555 1555 1.33 CISPEP 1 SER A 72 PRO A 73 1 0.21 CISPEP 2 SER A 72 PRO A 73 2 0.13 CISPEP 3 SER A 72 PRO A 73 3 0.17 CISPEP 4 SER A 72 PRO A 73 4 -0.09 CISPEP 5 SER A 72 PRO A 73 5 0.08 CISPEP 6 SER A 72 PRO A 73 6 0.12 CISPEP 7 SER A 72 PRO A 73 7 -0.15 CISPEP 8 SER A 72 PRO A 73 8 0.22 CISPEP 9 SER A 72 PRO A 73 9 -0.05 CISPEP 10 SER A 72 PRO A 73 10 0.03 CISPEP 11 SER A 72 PRO A 73 11 -0.15 CISPEP 12 SER A 72 PRO A 73 12 0.19 CISPEP 13 SER A 72 PRO A 73 13 0.36 CISPEP 14 SER A 72 PRO A 73 14 -0.02 CISPEP 15 SER A 72 PRO A 73 15 -0.18 CISPEP 16 SER A 72 PRO A 73 16 -0.11 CISPEP 17 SER A 72 PRO A 73 17 -0.16 CISPEP 18 SER A 72 PRO A 73 18 0.15 CISPEP 19 SER A 72 PRO A 73 19 -0.03 CISPEP 20 SER A 72 PRO A 73 20 0.37 SITE 1 AC2 1 GLY A 111 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 - b 23 2 Bytes