Header list of 1t2m.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 22-APR-04 1T2M TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN OF AF-6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: AF-6 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 TISSUE: BRAIN; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+) KEYWDS CHROMOSOMAL TRANSLOCATION, PROTO-ONCOGENE, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.ZHOU,J.H.WU,Y.Q.XU,A.D.HUANG,Y.Y.SHI REVDAT 4 02-MAR-22 1T2M 1 REMARK SEQADV REVDAT 3 24-FEB-09 1T2M 1 VERSN REVDAT 2 19-APR-05 1T2M 1 JRNL REVDAT 1 08-FEB-05 1T2M 0 JRNL AUTH H.ZHOU,Y.XU,Y.YANG,A.HUANG,J.WU,Y.SHI JRNL TITL SOLUTION STRUCTURE OF AF-6 PDZ DOMAIN AND ITS INTERACTION JRNL TITL 2 WITH THE C-TERMINAL PEPTIDES FROM NEUREXIN AND BCR JRNL REF J.BIOL.CHEM. V. 280 13841 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15684424 JRNL DOI 10.1074/JBC.M411065200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.2, CNS 1.1 REMARK 3 AUTHORS : F. DELAGLIO (NMRPIPE), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS ALSO REFINED WITH CSI REMARK 3 VERSION 1.0 (AUTHORS: DAVID S. WISHART) REMARK 4 REMARK 4 1T2M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000022233. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.9 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE, 1MM EDTA REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 50MM PHOSPHATE BUFFER NA; 1MM REMARK 210 EDTA; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1, MOLMOL 2K.2, SPARKY 3 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY 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 1-20 REMARK 465 RES C SSSEQI REMARK 465 LEU A 94 REMARK 465 GLU A 95 REMARK 465 HIS A 96 REMARK 465 HIS A 97 REMARK 465 HIS A 98 REMARK 465 HIS A 99 REMARK 465 HIS A 100 REMARK 465 HIS A 101 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 15 47.08 -163.40 REMARK 500 1 LYS A 31 -158.81 -122.10 REMARK 500 1 ARG A 50 -67.82 -106.26 REMARK 500 1 LEU A 58 -62.71 -109.07 REMARK 500 1 LEU A 65 51.19 -96.86 REMARK 500 2 PRO A 4 -166.20 -69.86 REMARK 500 2 ASN A 15 32.26 -152.87 REMARK 500 2 LYS A 31 -147.44 -123.66 REMARK 500 2 LEU A 58 -63.12 -108.25 REMARK 500 2 ARG A 79 56.81 -95.35 REMARK 500 2 GLN A 91 -165.78 -101.28 REMARK 500 3 LYS A 2 96.58 64.00 REMARK 500 3 GLU A 3 78.82 59.11 REMARK 500 3 GLN A 14 56.80 -92.82 REMARK 500 3 MET A 17 -68.34 -138.71 REMARK 500 3 LYS A 31 -155.43 -121.47 REMARK 500 3 ARG A 79 44.30 -92.71 REMARK 500 3 LYS A 90 87.95 -66.45 REMARK 500 3 GLN A 91 -168.16 -110.55 REMARK 500 4 LYS A 2 75.42 64.27 REMARK 500 4 GLU A 3 146.29 68.45 REMARK 500 4 GLN A 14 68.69 -101.04 REMARK 500 4 ARG A 79 65.10 -101.72 REMARK 500 4 LYS A 90 83.57 -66.83 REMARK 500 4 GLN A 91 -168.49 -108.02 REMARK 500 5 GLU A 3 98.05 61.94 REMARK 500 5 PRO A 4 -178.19 -59.93 REMARK 500 5 MET A 17 -59.11 -127.32 REMARK 500 5 LYS A 31 -151.54 -124.01 REMARK 500 5 LYS A 90 83.97 -66.20 REMARK 500 6 GLN A 14 73.16 -115.06 REMARK 500 6 MET A 17 -65.21 -100.72 REMARK 500 6 LEU A 58 -54.76 -145.18 REMARK 500 6 LYS A 90 91.56 -66.28 REMARK 500 6 GLN A 91 -165.87 -113.07 REMARK 500 7 ASN A 15 42.54 -160.32 REMARK 500 7 ASP A 30 37.26 -95.22 REMARK 500 7 LYS A 31 -148.50 -140.21 REMARK 500 7 LYS A 41 109.01 -59.58 REMARK 500 7 ARG A 50 -51.39 -144.10 REMARK 500 7 LEU A 58 -63.63 -95.18 REMARK 500 7 ARG A 79 58.02 -91.21 REMARK 500 8 ASN A 15 38.57 -164.91 REMARK 500 8 MET A 17 -66.47 -129.60 REMARK 500 8 LYS A 31 -154.38 -120.99 REMARK 500 8 ARG A 50 -51.03 -120.57 REMARK 500 8 VAL A 66 87.07 -67.58 REMARK 500 8 ARG A 79 49.18 -89.17 REMARK 500 8 GLN A 91 -169.90 -161.30 REMARK 500 9 ASN A 15 42.54 -166.21 REMARK 500 REMARK 500 THIS ENTRY HAS 132 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1T2M A 2 93 UNP P55196 AFAD_HUMAN 987 1077 SEQADV 1T2M MET A 1 UNP P55196 INITIATING METHIONINE SEQADV 1T2M LEU A 94 UNP P55196 EXPRESSION TAG SEQADV 1T2M GLU A 95 UNP P55196 EXPRESSION TAG SEQADV 1T2M HIS A 96 UNP P55196 EXPRESSION TAG SEQADV 1T2M HIS A 97 UNP P55196 EXPRESSION TAG SEQADV 1T2M HIS A 98 UNP P55196 EXPRESSION TAG SEQADV 1T2M HIS A 99 UNP P55196 EXPRESSION TAG SEQADV 1T2M HIS A 100 UNP P55196 EXPRESSION TAG SEQADV 1T2M HIS A 101 UNP P55196 EXPRESSION TAG SEQRES 1 A 101 MET LYS GLU PRO GLU ILE ILE THR VAL THR LEU LYS LYS SEQRES 2 A 101 GLN ASN GLY MET GLY LEU SER ILE VAL ALA ALA LYS GLY SEQRES 3 A 101 ALA GLY GLN ASP LYS LEU GLY ILE TYR VAL LYS SER VAL SEQRES 4 A 101 VAL LYS GLY GLY ALA ALA ASP VAL ASP GLY ARG LEU ALA SEQRES 5 A 101 ALA GLY ASP GLN LEU LEU SER VAL ASP GLY ARG SER LEU SEQRES 6 A 101 VAL GLY LEU SER GLN GLU ARG ALA ALA GLU LEU MET THR SEQRES 7 A 101 ARG THR SER SER VAL VAL THR LEU GLU VAL ALA LYS GLN SEQRES 8 A 101 GLY ALA LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 GLY A 43 GLY A 49 1 7 HELIX 2 2 SER A 69 ARG A 79 1 11 SHEET 1 A 5 GLU A 5 LYS A 12 0 SHEET 2 A 5 VAL A 83 LYS A 90 -1 O VAL A 84 N LEU A 11 SHEET 3 A 5 ASP A 55 VAL A 60 -1 N GLN A 56 O ALA A 89 SHEET 4 A 5 GLY A 33 VAL A 39 -1 N VAL A 36 O ASP A 55 SHEET 5 A 5 LEU A 19 ALA A 24 -1 N VAL A 22 O TYR A 35 SHEET 1 B 4 GLU A 5 LYS A 12 0 SHEET 2 B 4 VAL A 83 LYS A 90 -1 O VAL A 84 N LEU A 11 SHEET 3 B 4 ASP A 55 VAL A 60 -1 N GLN A 56 O ALA A 89 SHEET 4 B 4 ARG A 63 SER A 64 -1 O ARG A 63 N VAL A 60 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