Header list of 2nmb.pdb file
Complete list - r 16 2 Bytes
HEADER CELL CYCLE/GENE REGULATION 29-OCT-98 2NMB TITLE DNUMB PTB DOMAIN COMPLEXED WITH A PHOSPHOTYROSINE PEPTIDE, NMR, TITLE 2 ENSEMBLE OF STRUCTURES. COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (NUMB PROTEIN); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PTB DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN (GPPY PEPTIDE); COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: CHEMICALLY SYNTHESIZED SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 GENE: NUMB; 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_PLASMID: PGEX4T2; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES KEYWDS COMPLEX, SIGNAL TRANSDUCTION, PHOSPHOTYROSINE BINDING DOMAIN (PTB), KEYWDS 2 ASYMETR IC CELL DIVISION, CELL CYCLE-GENE REGULATION COMPLEX EXPDTA SOLUTION NMR NUMMDL 14 AUTHOR S.-C.LI,C.ZWAHLEN,S.J.F.VINCENT,C.J.MCGLADE,T.PAWSON,J.D.FORMAN-KAY REVDAT 6 16-MAR-22 2NMB 1 REMARK LINK REVDAT 5 24-FEB-09 2NMB 1 VERSN REVDAT 4 01-APR-03 2NMB 1 JRNL REVDAT 3 26-SEP-01 2NMB 3 ATOM REVDAT 2 20-JAN-00 2NMB 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 04-NOV-98 2NMB 0 JRNL AUTH S.C.LI,C.ZWAHLEN,S.J.VINCENT,C.J.MCGLADE,L.E.KAY,T.PAWSON, JRNL AUTH 2 J.D.FORMAN-KAY JRNL TITL STRUCTURE OF A NUMB PTB DOMAIN-PEPTIDE COMPLEX SUGGESTS A JRNL TITL 2 BASIS FOR DIVERSE BINDING SPECIFICITY. JRNL REF NAT.STRUCT.BIOL. V. 5 1075 1998 JRNL REFN ISSN 1072-8368 JRNL PMID 9846878 JRNL DOI 10.1038/4185 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.-C.LI,Z.SONGYANG,S.J.F.VINCENT,C.ZWAHLEN,S.WILEY, REMARK 1 AUTH 2 L.CANTLEY,L.E.KAY,J.D.FORMAN-KAY,T.PAWSON REMARK 1 TITL HIGH-AFFINITY BINDING OF THE DROSOPHILA NUMB REMARK 1 TITL 2 PHOSPHOTYROSINE-BINDING DOMAIN TO PEP TIDES CONTAINING A REMARK 1 TITL 3 GLY-PRO-(P)TYR MOTIF REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 94 7204 1997 REMARK 1 REFN ISSN 0027-8424 REMARK 1 DOI 10.1073/PNAS.94.14.7204 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: MODIFICATION OF X-PLOR TO INCORPORATE REMARK 3 ARIA PROTOCOL FOR AMBIGUOUS NOE ASSIGNMENT. REMARK 4 REMARK 4 2NMB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000001415. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCACONNH; REMARK 210 HAHBCBCACONNH; CCCTOCSYCONNH; REMARK 210 HCCTOCSYCONNH; HCCHTOCSY; N- REMARK 210 NOESY HSQC; CN-NOESY; C-HSQC- REMARK 210 NOESY; VAL-CB-NOESY; HALF-FILTER- REMARK 210 NOESY; FILTER-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA/X-PLOR 3.851 REMARK 210 METHOD USED : SIMULATED ANNEALING WITH REMARK 210 AMBIGUOUS RESTRAINTS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATION > 0.3 A REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4 REMARK 210 REMARK 210 REMARK: NOE MIXING TIME 50MS AND 90MS FOR N-NOESY-HSQC, C-HSQC REMARK 210 -NOESY, CN-NOESY NOE MIXING TIME 150MS FOR HALF-FILTER-NOESY, REMARK 210 FILTER-NOESY 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 1-14 REMARK 465 RES C SSSEQI REMARK 465 GLY A 52 REMARK 465 SER A 53 REMARK 465 PRO A 54 REMARK 465 GLY A 55 REMARK 465 ILE A 56 REMARK 465 PRO A 57 REMARK 465 ASP A 58 REMARK 465 ARG A 59 REMARK 465 VAL A 60 REMARK 465 PRO A 61 REMARK 465 GLU A 62 REMARK 465 SER A 63 REMARK 465 SER A 211 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 81 HG SER A 82 1.58 REMARK 500 O ASP A 126 H ILE A 144 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 LYS A 65 175.22 52.24 REMARK 500 1 PRO A 66 105.67 -44.84 REMARK 500 1 HIS A 67 -82.05 171.20 REMARK 500 1 ALA A 79 78.51 65.92 REMARK 500 1 THR A 80 60.03 176.19 REMARK 500 1 SER A 82 153.96 174.16 REMARK 500 1 VAL A 85 160.30 178.67 REMARK 500 1 LYS A 86 71.27 -111.31 REMARK 500 1 TYR A 87 107.95 -55.02 REMARK 500 1 LEU A 88 -76.24 -48.50 REMARK 500 1 GLU A 95 -74.29 -144.84 REMARK 500 1 SER A 96 19.48 59.45 REMARK 500 1 SER A 112 -165.74 -79.87 REMARK 500 1 ARG A 113 42.44 -109.41 REMARK 500 1 SER A 124 44.94 -142.82 REMARK 500 1 ASP A 126 -40.03 -164.94 REMARK 500 1 ARG A 129 78.94 -117.99 REMARK 500 1 VAL A 140 67.45 -111.48 REMARK 500 1 PHE A 149 174.66 80.86 REMARK 500 1 ASP A 153 -80.91 -41.49 REMARK 500 1 ARG A 154 23.26 -156.67 REMARK 500 1 ASN A 155 29.64 44.25 REMARK 500 1 GLU A 157 25.33 -157.33 REMARK 500 1 SER A 161 134.05 -172.26 REMARK 500 1 ASP A 166 -90.16 50.84 REMARK 500 1 THR A 168 25.15 -140.96 REMARK 500 1 ARG A 170 -72.29 86.74 REMARK 500 1 TRP A 172 90.17 -56.01 REMARK 500 1 ASP A 182 83.05 63.27 REMARK 500 1 SER A 183 28.88 -172.22 REMARK 500 1 ARG A 186 -42.72 -159.63 REMARK 500 1 LEU A 199 51.91 -117.54 REMARK 500 1 ALA A 209 103.21 69.06 REMARK 500 1 TYR B 2 -89.69 -163.34 REMARK 500 1 PTR B 6 -67.65 177.44 REMARK 500 2 LYS A 65 70.92 48.44 REMARK 500 2 PRO A 66 -77.25 -56.59 REMARK 500 2 HIS A 67 -69.87 -154.04 REMARK 500 2 ALA A 79 90.09 49.21 REMARK 500 2 THR A 80 44.63 179.50 REMARK 500 2 ARG A 97 23.90 -148.30 REMARK 500 2 ARG A 114 92.71 -46.05 REMARK 500 2 ASP A 126 -44.30 -133.92 REMARK 500 2 VAL A 140 65.86 -111.11 REMARK 500 2 ASP A 141 66.92 -68.16 REMARK 500 2 THR A 143 -176.62 -54.19 REMARK 500 2 PHE A 149 149.56 73.66 REMARK 500 2 ALA A 151 80.83 171.75 REMARK 500 2 ARG A 154 31.14 -172.34 REMARK 500 2 GLU A 157 19.18 -152.24 REMARK 500 REMARK 500 THIS ENTRY HAS 449 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2NMB A 52 205 UNP P16554 NUMB_DROME 52 205 DBREF 2NMB B 1 7 PDB 2NMB 2NMB 1 7 SEQADV 2NMB THR A 206 UNP P16554 SEE REMARK 999 SEQADV 2NMB ARG A 207 UNP P16554 SEE REMARK 999 SEQADV 2NMB ALA A 208 UNP P16554 SEE REMARK 999 SEQADV 2NMB ALA A 209 UNP P16554 SEE REMARK 999 SEQADV 2NMB ALA A 210 UNP P16554 SEE REMARK 999 SEQRES 1 A 160 GLY SER PRO GLY ILE PRO ASP ARG VAL PRO GLU SER SER SEQRES 2 A 160 LYS PRO HIS GLN TRP GLN ALA ASP GLU GLU ALA VAL ARG SEQRES 3 A 160 SER ALA THR CYS SER PHE SER VAL LYS TYR LEU GLY CYS SEQRES 4 A 160 VAL GLU VAL PHE GLU SER ARG GLY MET GLN VAL CYS GLU SEQRES 5 A 160 GLU ALA LEU LYS VAL LEU ARG GLN SER ARG ARG ARG PRO SEQRES 6 A 160 VAL ARG GLY LEU LEU HIS VAL SER GLY ASP GLY LEU ARG SEQRES 7 A 160 VAL VAL ASP ASP GLU THR LYS GLY LEU ILE VAL ASP GLN SEQRES 8 A 160 THR ILE GLU LYS VAL SER PHE CYS ALA PRO ASP ARG ASN SEQRES 9 A 160 HIS GLU ARG GLY PHE SER TYR ILE CYS ARG ASP GLY THR SEQRES 10 A 160 THR ARG ARG TRP MET CYS HIS GLY PHE LEU ALA CYS LYS SEQRES 11 A 160 ASP SER GLY GLU ARG LEU SER HIS ALA VAL GLY CYS ALA SEQRES 12 A 160 PHE ALA VAL CYS LEU GLU ARG LYS GLN ARG ARG THR ARG SEQRES 13 A 160 ALA ALA ALA SER SEQRES 1 B 7 ALA TYR ILE GLY PRO PTR LEU MODRES 2NMB PTR B 6 TYR O-PHOSPHOTYROSINE HET PTR B 6 24 HETNAM PTR O-PHOSPHOTYROSINE HETSYN PTR PHOSPHONOTYROSINE FORMUL 2 PTR C9 H12 N O6 P HELIX 1 1 GLN A 68 ALA A 79 1 12 HELIX 2 2 MET A 99 SER A 112 1 14 HELIX 3 3 LEU A 187 PHE A 195 1 9 SHEET 1 A 5 ARG A 129 ASP A 132 0 SHEET 2 A 5 GLY A 119 HIS A 122 -1 N LEU A 120 O VAL A 131 SHEET 3 A 5 PHE A 83 GLU A 92 -1 O PHE A 83 N LEU A 121 SHEET 4 A 5 TRP A 172 ALA A 179 -1 O CYS A 174 N VAL A 91 SHEET 5 A 5 ILE A 163 ARG A 165 -1 O CYS A 164 N MET A 173 LINK C PRO B 5 N PTR B 6 1555 1555 1.33 LINK C PTR B 6 N LEU B 7 1555 1555 1.33 CISPEP 1 GLY B 4 PRO B 5 8 6.21 CISPEP 2 GLY B 4 PRO B 5 12 4.56 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 16 2 Bytes