Header list of 1ssf.pdb file
Complete list - r 2 2 Bytes
HEADER CELL CYCLE 24-MAR-04 1SSF TITLE SOLUTION STRUCTURE OF THE MOUSE 53BP1 FRAGMENT (RESIDUES 1463-1617) COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSFORMATION RELATED PROTEIN 53 BINDING PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1463-1617; COMPND 5 SYNONYM: MURINE P53-BINDING PROTEIN; COMPND 6 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; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST15 KEYWDS TUDOR DOMAINS, TANDEM, SH3-LIKE FOLD, BETA BARREL, ALPHA-HELIX, CELL KEYWDS 2 CYCLE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR G.CHARIER,J.COUPRIE,B.ALPHA-BAZIN,V.MEYER,E.QUEMENEUR,R.GUEROIS, AUTHOR 2 I.CALLEBAUT,B.GILQUIN,S.ZINN-JUSTIN REVDAT 3 02-MAR-22 1SSF 1 REMARK SEQADV REVDAT 2 24-FEB-09 1SSF 1 VERSN REVDAT 1 14-SEP-04 1SSF 0 JRNL AUTH G.CHARIER,J.COUPRIE,B.ALPHA-BAZIN,V.MEYER,E.QUEMENEUR, JRNL AUTH 2 R.GUEROIS,I.CALLEBAUT,B.GILQUIN,S.ZINN-JUSTIN JRNL TITL THE TUDOR TANDEM OF 53BP1; A NEW STRUCTURAL MOTIF INVOLVED JRNL TITL 2 IN DNA AND RG-RICH PEPTIDE BINDING JRNL REF STRUCTURE V. 12 1551 2004 JRNL REFN ISSN 0969-2126 JRNL PMID 15341721 JRNL DOI 10.1016/J.STR.2004.06.014 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, CNS 1.0 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2337 NOE-DERIVED RESTRAINTS, 206 DIHEDRAL ANGLE RESTRAINTS, AND REMARK 3 60 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1SSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000021963. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : 50MM TRIS-HCL, 150MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.6MM MOUSE 53BP1 (1463-1617) REMARK 210 FRAGMENT, U-15N, 50MM TRIS-HCL REMARK 210 BUFFER, 150MM NACL, 90% H2O, 10% REMARK 210 D2O; 0.9MM MOUSE 53BP1 (1463- REMARK 210 1617) FRAGMENT, U-15N,13C, 50MM REMARK 210 TRIS-HCL BUFFER, 150MM NACL, 90% REMARK 210 H2O, 10% D2O; 0.9MM MOUSE 53BP1 REMARK 210 (1463-1617) FRAGMENT, U-15N,13C, REMARK 210 50MM TRIS-HCL BUFFER, 150MM NACL, REMARK 210 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_13C_NOESY_ REMARK 210 AROMATIC REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.0, FELIX 2000.1, CNS REMARK 210 1.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH REMARK 210 EXPERIMENTAL NOESY SPECTRUM, REMARK 210 STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY, STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE 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 1-10 REMARK 465 RES C SSSEQI REMARK 465 GLY A 0 REMARK 465 ASP A 1 REMARK 465 SER A 2 REMARK 465 SER A 3 REMARK 465 SER A 4 REMARK 465 SER A 5 REMARK 465 GLY A 6 REMARK 465 ALA A 130 REMARK 465 VAL A 131 REMARK 465 THR A 132 REMARK 465 PRO A 133 REMARK 465 LEU A 134 REMARK 465 THR A 135 REMARK 465 LYS A 136 REMARK 465 ALA A 137 REMARK 465 ALA A 138 REMARK 465 ASP A 139 REMARK 465 ILE A 140 REMARK 465 SER A 141 REMARK 465 LEU A 142 REMARK 465 ASP A 143 REMARK 465 ASN A 144 REMARK 465 LEU A 145 REMARK 465 VAL A 146 REMARK 465 GLU A 147 REMARK 465 GLY A 148 REMARK 465 LYS A 149 REMARK 465 ARG A 150 REMARK 465 LYS A 151 REMARK 465 ARG A 152 REMARK 465 ARG A 153 REMARK 465 SER A 154 REMARK 465 ASN A 155 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 PRO A 62 HG1 THR A 65 1.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 PHE A 9 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 LEU A 12 CB - CA - C ANGL. DEV. = 13.3 DEGREES REMARK 500 1 LEU A 12 CA - CB - CG ANGL. DEV. = 13.9 DEGREES REMARK 500 1 VAL A 14 CA - CB - CG2 ANGL. DEV. = 10.1 DEGREES REMARK 500 1 CYS A 58 CB - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 1 LEU A 63 C - N - CA ANGL. DEV. = 15.1 DEGREES REMARK 500 1 SER A 71 C - N - CA ANGL. DEV. = 15.9 DEGREES REMARK 500 1 SER A 94 N - CA - CB ANGL. DEV. = 11.0 DEGREES REMARK 500 1 LEU A 119 C - N - CA ANGL. DEV. = 15.3 DEGREES REMARK 500 1 TYR A 123 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 2 PHE A 24 CB - CG - CD2 ANGL. DEV. = 4.3 DEGREES REMARK 500 2 LEU A 41 CB - CA - C ANGL. DEV. = 13.5 DEGREES REMARK 500 2 PHE A 42 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 2 PHE A 42 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 SER A 71 C - N - CA ANGL. DEV. = 16.0 DEGREES REMARK 500 2 PHE A 76 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES REMARK 500 2 PHE A 76 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 2 TYR A 104 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 2 TYR A 104 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 LEU A 113 N - CA - CB ANGL. DEV. = 17.3 DEGREES REMARK 500 3 PHE A 9 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 3 VAL A 14 CA - CB - CG2 ANGL. DEV. = 14.3 DEGREES REMARK 500 3 SER A 26 N - CA - CB ANGL. DEV. = -10.5 DEGREES REMARK 500 3 LEU A 41 CB - CA - C ANGL. DEV. = 12.4 DEGREES REMARK 500 3 CYS A 58 CB - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 3 PRO A 62 C - N - CA ANGL. DEV. = 9.3 DEGREES REMARK 500 3 LEU A 63 N - CA - C ANGL. DEV. = 17.2 DEGREES REMARK 500 3 PHE A 76 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES REMARK 500 3 TYR A 92 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 3 TYR A 92 CB - CG - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 3 TYR A 92 CB - CG - CD1 ANGL. DEV. = 7.0 DEGREES REMARK 500 3 LEU A 113 N - CA - CB ANGL. DEV. = 14.7 DEGREES REMARK 500 4 GLY A 27 C - N - CA ANGL. DEV. = 13.2 DEGREES REMARK 500 4 LEU A 40 CB - CG - CD1 ANGL. DEV. = 10.6 DEGREES REMARK 500 4 LEU A 41 CB - CA - C ANGL. DEV. = 11.5 DEGREES REMARK 500 4 PHE A 42 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES REMARK 500 4 ILE A 61 CB - CA - C ANGL. DEV. = 13.1 DEGREES REMARK 500 4 SER A 71 C - N - CA ANGL. DEV. = 15.1 DEGREES REMARK 500 4 PHE A 76 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 4 PHE A 76 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES REMARK 500 4 LEU A 113 N - CA - CB ANGL. DEV. = 13.9 DEGREES REMARK 500 4 TYR A 123 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 5 LEU A 12 CB - CG - CD2 ANGL. DEV. = -11.9 DEGREES REMARK 500 5 TRP A 18 CB - CG - CD2 ANGL. DEV. = -8.2 DEGREES REMARK 500 5 TYR A 25 C - N - CA ANGL. DEV. = 15.3 DEGREES REMARK 500 5 LEU A 41 CB - CA - C ANGL. DEV. = 17.3 DEGREES REMARK 500 5 CYS A 58 CB - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 5 PRO A 60 N - CA - CB ANGL. DEV. = 7.9 DEGREES REMARK 500 5 PRO A 62 N - CA - CB ANGL. DEV. = -9.7 DEGREES REMARK 500 5 ASP A 64 N - CA - CB ANGL. DEV. = -11.0 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 93 ANGLE DEVIATIONS. 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 SER A 8 -116.37 -162.77 REMARK 500 1 LYS A 53 0.29 -60.92 REMARK 500 1 ASP A 54 -75.23 -109.40 REMARK 500 1 LEU A 57 102.10 -50.91 REMARK 500 1 PRO A 60 -78.86 -55.87 REMARK 500 1 LEU A 63 14.98 -46.25 REMARK 500 1 ASP A 64 27.87 -143.93 REMARK 500 1 GLU A 66 93.99 -66.71 REMARK 500 1 LEU A 70 97.16 -65.35 REMARK 500 1 GLU A 72 159.47 -38.40 REMARK 500 1 LYS A 82 -48.17 -133.79 REMARK 500 1 SER A 88 66.11 -65.76 REMARK 500 1 ARG A 106 -24.80 -31.45 REMARK 500 1 ARG A 120 -31.61 -39.69 REMARK 500 1 LEU A 125 14.19 -48.54 REMARK 500 2 PHE A 9 -8.82 78.05 REMARK 500 2 VAL A 10 5.62 -67.26 REMARK 500 2 TRP A 18 -81.65 -92.23 REMARK 500 2 LYS A 53 27.15 -61.12 REMARK 500 2 ASP A 54 -73.13 -136.84 REMARK 500 2 LEU A 57 107.48 -48.78 REMARK 500 2 PRO A 60 -75.60 -65.53 REMARK 500 2 LEU A 63 14.84 -37.85 REMARK 500 2 ASP A 64 48.25 -162.32 REMARK 500 2 GLU A 66 94.34 -64.50 REMARK 500 2 GLU A 72 144.05 -38.09 REMARK 500 2 SER A 88 76.15 -61.30 REMARK 500 2 LEU A 125 13.08 -49.33 REMARK 500 3 SER A 8 41.62 -67.95 REMARK 500 3 VAL A 10 6.94 -60.45 REMARK 500 3 LEU A 12 166.23 -45.70 REMARK 500 3 ASP A 43 -17.84 -49.95 REMARK 500 3 LYS A 53 17.94 -59.47 REMARK 500 3 ASP A 54 -79.50 -126.72 REMARK 500 3 LEU A 57 102.85 -52.46 REMARK 500 3 PRO A 60 -73.48 -64.53 REMARK 500 3 PRO A 62 106.10 -52.98 REMARK 500 3 LEU A 63 13.48 -38.10 REMARK 500 3 ASP A 64 40.44 -159.12 REMARK 500 3 GLU A 72 169.02 -39.79 REMARK 500 3 SER A 88 65.01 -62.94 REMARK 500 3 LEU A 125 9.27 -49.16 REMARK 500 3 PRO A 127 33.45 -95.65 REMARK 500 4 ASP A 54 -78.30 -104.04 REMARK 500 4 LEU A 57 102.85 -48.75 REMARK 500 4 PRO A 60 -73.99 -71.76 REMARK 500 4 LEU A 63 15.32 -39.07 REMARK 500 4 ASP A 64 20.86 -142.30 REMARK 500 4 GLU A 66 95.32 -66.50 REMARK 500 4 LEU A 70 99.62 -65.56 REMARK 500 REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU A 51 GLY A 52 1 -149.76 REMARK 500 LEU A 51 GLY A 52 2 -147.02 REMARK 500 LEU A 51 GLY A 52 3 -140.15 REMARK 500 LEU A 51 GLY A 52 9 -148.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 PHE A 9 0.09 SIDE CHAIN REMARK 500 1 PHE A 24 0.11 SIDE CHAIN REMARK 500 1 TYR A 25 0.10 SIDE CHAIN REMARK 500 1 TYR A 93 0.13 SIDE CHAIN REMARK 500 1 TYR A 104 0.12 SIDE CHAIN REMARK 500 2 TYR A 46 0.09 SIDE CHAIN REMARK 500 2 TYR A 93 0.10 SIDE CHAIN REMARK 500 2 TYR A 104 0.12 SIDE CHAIN REMARK 500 3 TYR A 25 0.12 SIDE CHAIN REMARK 500 3 TYR A 92 0.09 SIDE CHAIN REMARK 500 3 TYR A 93 0.09 SIDE CHAIN REMARK 500 3 TYR A 104 0.07 SIDE CHAIN REMARK 500 4 PHE A 24 0.17 SIDE CHAIN REMARK 500 4 TYR A 25 0.07 SIDE CHAIN REMARK 500 4 TYR A 46 0.09 SIDE CHAIN REMARK 500 4 TYR A 93 0.10 SIDE CHAIN REMARK 500 4 TYR A 104 0.08 SIDE CHAIN REMARK 500 5 TYR A 38 0.10 SIDE CHAIN REMARK 500 5 TYR A 104 0.15 SIDE CHAIN REMARK 500 5 TYR A 123 0.08 SIDE CHAIN REMARK 500 6 PHE A 24 0.09 SIDE CHAIN REMARK 500 6 TYR A 38 0.07 SIDE CHAIN REMARK 500 6 TYR A 92 0.09 SIDE CHAIN REMARK 500 6 TYR A 93 0.10 SIDE CHAIN REMARK 500 6 TYR A 123 0.10 SIDE CHAIN REMARK 500 7 TYR A 25 0.08 SIDE CHAIN REMARK 500 7 TYR A 46 0.08 SIDE CHAIN REMARK 500 7 TYR A 93 0.25 SIDE CHAIN REMARK 500 7 TYR A 104 0.09 SIDE CHAIN REMARK 500 8 PHE A 24 0.09 SIDE CHAIN REMARK 500 8 TYR A 38 0.08 SIDE CHAIN REMARK 500 8 TYR A 104 0.08 SIDE CHAIN REMARK 500 9 TYR A 25 0.11 SIDE CHAIN REMARK 500 9 TYR A 38 0.09 SIDE CHAIN REMARK 500 9 TYR A 46 0.07 SIDE CHAIN REMARK 500 9 TYR A 92 0.09 SIDE CHAIN REMARK 500 9 TYR A 93 0.07 SIDE CHAIN REMARK 500 9 TYR A 123 0.07 SIDE CHAIN REMARK 500 10 TYR A 23 0.08 SIDE CHAIN REMARK 500 10 TYR A 38 0.09 SIDE CHAIN REMARK 500 10 TYR A 92 0.09 SIDE CHAIN REMARK 500 10 TYR A 93 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1SSF A 1 155 UNP Q91YC9 Q91YC9_MOUSE 1463 1617 SEQADV 1SSF GLY A 0 UNP Q91YC9 CLONING ARTIFACT SEQRES 1 A 156 GLY ASP SER SER SER SER GLY ASN SER PHE VAL GLY LEU SEQRES 2 A 156 ARG VAL VAL ALA LYS TRP SER SER ASN GLY TYR PHE TYR SEQRES 3 A 156 SER GLY LYS ILE THR ARG ASP VAL GLY ALA GLY LYS TYR SEQRES 4 A 156 LYS LEU LEU PHE ASP ASP GLY TYR GLU CYS ASP VAL LEU SEQRES 5 A 156 GLY LYS ASP ILE LEU LEU CYS ASP PRO ILE PRO LEU ASP SEQRES 6 A 156 THR GLU VAL THR ALA LEU SER GLU ASP GLU TYR PHE SER SEQRES 7 A 156 ALA GLY VAL VAL LYS GLY HIS ARG LYS GLU SER GLY GLU SEQRES 8 A 156 LEU TYR TYR SER ILE GLU LYS GLU GLY GLN ARG LYS TRP SEQRES 9 A 156 TYR LYS ARG MET ALA VAL ILE LEU SER LEU GLU GLN GLY SEQRES 10 A 156 ASN ARG LEU ARG GLU GLN TYR GLY LEU GLY PRO TYR GLU SEQRES 11 A 156 ALA VAL THR PRO LEU THR LYS ALA ALA ASP ILE SER LEU SEQRES 12 A 156 ASP ASN LEU VAL GLU GLY LYS ARG LYS ARG ARG SER ASN HELIX 1 1 LYS A 105 MET A 107 5 3 HELIX 2 2 LEU A 113 ARG A 118 1 6 SHEET 1 A 5 GLU A 47 LEU A 51 0 SHEET 2 A 5 LYS A 37 LEU A 41 -1 N LEU A 40 O CYS A 48 SHEET 3 A 5 TYR A 23 ARG A 31 -1 N THR A 30 O LYS A 39 SHEET 4 A 5 ARG A 13 ALA A 16 -1 N ALA A 16 O TYR A 25 SHEET 5 A 5 ILE A 55 CYS A 58 -1 O CYS A 58 N ARG A 13 SHEET 1 B 8 GLU A 47 LEU A 51 0 SHEET 2 B 8 LYS A 37 LEU A 41 -1 N LEU A 40 O CYS A 48 SHEET 3 B 8 TYR A 23 ARG A 31 -1 N THR A 30 O LYS A 39 SHEET 4 B 8 VAL A 109 SER A 112 -1 O LEU A 111 N PHE A 24 SHEET 5 B 8 THR A 65 ALA A 69 -1 N THR A 68 O ILE A 110 SHEET 6 B 8 SER A 77 GLU A 87 -1 O SER A 77 N ALA A 69 SHEET 7 B 8 GLU A 90 LYS A 97 -1 O GLU A 96 N VAL A 80 SHEET 8 B 8 GLN A 100 TYR A 104 -1 O GLN A 100 N LYS A 97 CISPEP 1 ASP A 59 PRO A 60 1 2.82 CISPEP 2 ASP A 59 PRO A 60 2 2.57 CISPEP 3 ASP A 59 PRO A 60 3 0.01 CISPEP 4 ASP A 59 PRO A 60 4 5.45 CISPEP 5 ASP A 59 PRO A 60 5 5.45 CISPEP 6 ASP A 59 PRO A 60 6 -0.30 CISPEP 7 ASP A 59 PRO A 60 7 7.26 CISPEP 8 ASP A 59 PRO A 60 8 5.12 CISPEP 9 ASP A 59 PRO A 60 9 0.93 CISPEP 10 ASP A 59 PRO A 60 10 8.22 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