Header list of 2b86.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 06-OCT-05 2B86 TITLE SOLUTION STRUCTURE OF THE FIRST SRC HOMOLOGY 3 DOMAIN OF NCK2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOPLASMIC PROTEIN NCK2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FIRST SH3 DOMAIN, RESIDUES 1-59; COMPND 5 SYNONYM: NCK ADAPTOR PROTEIN 2, SH2/SH3 ADAPTOR PROTEIN NCK-BETA, COMPND 6 NCK-2; 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: NCK2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30A KEYWDS NCK SH3 DOMAIN, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR S.PARK,K.TAKEUCHI,G.WAGNER REVDAT 3 09-MAR-22 2B86 1 REMARK SEQADV REVDAT 2 24-FEB-09 2B86 1 VERSN REVDAT 1 09-MAY-06 2B86 0 JRNL AUTH S.PARK,K.TAKEUCHI,G.WAGNER JRNL TITL SOLUTION STRUCTURE OF THE FIRST SRC HOMOLOGY 3 DOMAIN OF JRNL TITL 2 HUMAN NCK2 JRNL REF J.BIOMOL.NMR V. 34 203 2006 JRNL REFN ISSN 0925-2738 JRNL PMID 16604428 JRNL DOI 10.1007/S10858-006-0019-5 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2B86 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-05. REMARK 100 THE DEPOSITION ID IS D_1000034795. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 600UM NCK SH3 DOMAIN U-15N, 13C, REMARK 210 50MM SODIUM PHOSPHATE, 50MM EDTA, REMARK 210 PH 6.5, 5% D2O, 95% H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3 REMARK 210 METHOD USED : SIMULATED ANNEALING TORTION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: CRYOGENIC PROBES 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-30 REMARK 465 RES C SSSEQI REMARK 465 LEU A 60 REMARK 465 GLU A 61 REMARK 465 HIS A 62 REMARK 465 HIS A 63 REMARK 465 HIS A 64 REMARK 465 HIS A 65 REMARK 465 HIS A 66 REMARK 465 HIS A 67 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 TYR A 55 44.21 -86.91 REMARK 500 2 ASN A 26 22.21 -140.00 REMARK 500 2 ASP A 33 117.41 -160.99 REMARK 500 2 PRO A 52 36.99 -73.63 REMARK 500 2 SER A 53 92.98 -67.69 REMARK 500 3 PRO A 52 36.60 -72.90 REMARK 500 3 SER A 53 97.72 -65.06 REMARK 500 5 ASP A 33 -66.37 -133.72 REMARK 500 5 ASP A 34 16.41 51.60 REMARK 500 5 PRO A 52 46.46 -72.23 REMARK 500 6 ASP A 33 118.36 -161.40 REMARK 500 6 PRO A 52 43.33 -78.26 REMARK 500 7 PRO A 52 39.63 -83.21 REMARK 500 7 SER A 53 90.05 -68.50 REMARK 500 8 PRO A 52 44.34 -75.80 REMARK 500 9 PRO A 52 33.11 -77.31 REMARK 500 9 SER A 53 100.78 -59.10 REMARK 500 10 ASN A 26 27.24 -141.11 REMARK 500 10 PRO A 52 36.23 -71.16 REMARK 500 10 SER A 53 93.45 -67.00 REMARK 500 11 ASP A 33 119.86 -161.02 REMARK 500 11 PRO A 52 31.11 -76.94 REMARK 500 11 SER A 53 87.24 -62.43 REMARK 500 12 PRO A 52 32.93 -73.86 REMARK 500 12 SER A 53 91.69 -65.04 REMARK 500 13 PRO A 52 42.81 -76.08 REMARK 500 14 ASN A 26 28.35 -141.52 REMARK 500 14 SER A 53 91.89 -58.66 REMARK 500 15 ASN A 26 29.38 -151.97 REMARK 500 15 SER A 53 94.36 -66.97 REMARK 500 16 ASP A 33 118.16 -160.99 REMARK 500 16 PRO A 52 30.92 -72.33 REMARK 500 16 SER A 53 85.51 -66.00 REMARK 500 17 ASP A 33 118.88 -160.99 REMARK 500 17 PRO A 52 45.24 -74.73 REMARK 500 17 SER A 53 73.63 -69.61 REMARK 500 18 PRO A 52 41.63 -74.84 REMARK 500 19 ASN A 26 25.35 -140.54 REMARK 500 19 ASP A 33 116.96 -160.68 REMARK 500 19 PRO A 52 44.40 -76.63 REMARK 500 20 PRO A 52 44.50 -70.77 REMARK 500 21 ASN A 26 27.73 -141.78 REMARK 500 21 PRO A 52 35.40 -70.98 REMARK 500 21 SER A 53 81.46 -67.93 REMARK 500 22 ASP A 33 118.38 -161.87 REMARK 500 22 PRO A 52 32.64 -72.05 REMARK 500 23 ASP A 33 118.47 -160.99 REMARK 500 23 PRO A 52 35.87 -73.99 REMARK 500 23 SER A 53 87.52 -68.54 REMARK 500 24 ASN A 26 24.77 -140.72 REMARK 500 REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2B86 A 1 59 UNP O43639 NCK2_HUMAN 1 59 SEQADV 2B86 LEU A 60 UNP O43639 CLONING ARTIFACT SEQADV 2B86 GLU A 61 UNP O43639 CLONING ARTIFACT SEQADV 2B86 HIS A 62 UNP O43639 EXPRESSION TAG SEQADV 2B86 HIS A 63 UNP O43639 EXPRESSION TAG SEQADV 2B86 HIS A 64 UNP O43639 EXPRESSION TAG SEQADV 2B86 HIS A 65 UNP O43639 EXPRESSION TAG SEQADV 2B86 HIS A 66 UNP O43639 EXPRESSION TAG SEQADV 2B86 HIS A 67 UNP O43639 EXPRESSION TAG SEQRES 1 A 67 MET THR GLU GLU VAL ILE VAL ILE ALA LYS TRP ASP TYR SEQRES 2 A 67 THR ALA GLN GLN ASP GLN GLU LEU ASP ILE LYS LYS ASN SEQRES 3 A 67 GLU ARG LEU TRP LEU LEU ASP ASP SER LYS THR TRP TRP SEQRES 4 A 67 ARG VAL ARG ASN ALA ALA ASN ARG THR GLY TYR VAL PRO SEQRES 5 A 67 SER ASN TYR VAL GLU ARG LYS LEU GLU HIS HIS HIS HIS SEQRES 6 A 67 HIS HIS SHEET 1 A 5 THR A 48 TYR A 50 0 SHEET 2 A 5 ARG A 40 ARG A 42 -1 N VAL A 41 O GLY A 49 SHEET 3 A 5 ARG A 28 ASP A 33 -1 N LEU A 32 O ARG A 40 SHEET 4 A 5 VAL A 5 ALA A 9 -1 N VAL A 5 O LEU A 31 SHEET 5 A 5 VAL A 56 ARG A 58 -1 O GLU A 57 N ILE A 8 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 9 2 Bytes