Header list of 2a4j.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN 29-JUN-05 2A4J TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN (T94-Y172) OF THE HUMAN TITLE 2 CENTRIN 2 IN COMPLEX WITH A 17 RESIDUES PEPTIDE (P1-XPC) FROM TITLE 3 XERODERMA PIGMENTOSUM GROUP C PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CENTRIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 94-172); COMPND 5 SYNONYM: CALTRACTIN ISOFORM 1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 17-MER PEPTIDE P1-XPC FROM DNA-REPAIR PROTEIN COMPLEMENTING COMPND 9 XP-C CELLS; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: RESIDUES 847-863; COMPND 12 SYNONYM: XERODERMA PIGMENTOSUM GROUP C COMPLEMENTING PROTEIN P125; COMPND 13 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: CEN2; 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: PET24A(+); SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: THIS SEQUENS OCCURS IN HOMO SAPIENS KEYWDS EF-HAND, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.YANG,S.MIRON,L.MOUAWAD,P.DUCHAMBON,Y.BLOUQUIT,C.T.CRAESCU REVDAT 4 09-MAR-22 2A4J 1 REMARK REVDAT 3 14-APR-09 2A4J 1 JRNL REVDAT 2 24-FEB-09 2A4J 1 VERSN REVDAT 1 12-JUL-05 2A4J 0 SPRSDE 12-JUL-05 2A4J 1T2G JRNL AUTH A.YANG,S.MIRON,L.MOUAWAD,P.DUCHAMBON,Y.BLOUQUIT,C.T.CRAESCU JRNL TITL FLEXIBILITY AND PLASTICITY OF HUMAN CENTRIN 2 BINDING TO THE JRNL TITL 2 XERODERMA PIGMENTOSUM GROUP C PROTEIN (XPC) FROM NUCLEAR JRNL TITL 3 EXCISION REPAIR. JRNL REF BIOCHEMISTRY V. 45 3653 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16533048 JRNL DOI 10.1021/BI0524868 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 2000.1, INSIGHT II 2000 REMARK 3 AUTHORS : ACCELRYS (FELIX), ACCELRYS (INSIGHT II) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1298 NOE REMARK 3 DISTANCE RESTRAINTS, 121 DIHEDRAL ANGLE RESTRAINTS, AND 84 REMARK 3 HYDROGEN BOND RESTRAINTS. REMARK 4 REMARK 4 2A4J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033478. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2 MM UNLABELED SC_HSCEN2(T94 REMARK 210 -Y172);DEUTERATED TRIS/HCL 20 MM BUFFER; 100 MM NACL;5MM CACL2; REMARK 210 PH 6.5; 1.4 MM UNLABELED P1-XPC;; 1.2 MM UNLABELED SC_HSCEN2(T94- REMARK 210 Y172)U-15N;DEUTERATED TRIS/HCL 20 MM BUFFER; 100 MM NACL;5MM REMARK 210 CACL2;PH 6.5; 1.4 MM UNLABELED P1-XPC;; 1.2 MM UNLABELED SC_ REMARK 210 HSCEN2(T94-Y172)U-15N, 13C; DEUTERATED TRIS/HCL 20 MM BUFFER; REMARK 210 100 MM NACL;5MM CACL2;PH 6.5; 1.4 MM UNLABELED P1-XPC; REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; REMARK 210 3D_15N_SEPARATED_TOCSY; 3D_15N- REMARK 210 SEPARATED_NOESY; 2D_15N_HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DISCOVER 2.98 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 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 HB3 ARG B 14 H LEU B 15 1.26 REMARK 500 O LYS A 127 HB2 LYS A 131 1.37 REMARK 500 O GLU A 104 HB2 LYS A 108 1.46 REMARK 500 O GLN A 160 HB3 ARG A 164 1.47 REMARK 500 O GLN A 95 HB2 LYS A 96 1.57 REMARK 500 O LEU B 15 HB2 LYS B 16 1.60 REMARK 500 O GLN A 160 CB ARG A 164 2.04 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 113 CB - CG - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 1 PHE A 113 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 1 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 VAL A 157 CA - CB - CG1 ANGL. DEV. = 11.9 DEGREES REMARK 500 1 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 LEU B 9 CB - CG - CD2 ANGL. DEV. = 10.2 DEGREES REMARK 500 1 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG B 14 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 PHE A 113 CA - CB - CG ANGL. DEV. = 15.0 DEGREES REMARK 500 2 PHE A 113 CB - CG - CD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 2 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 2 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 LEU B 9 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES REMARK 500 2 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 2 ARG B 14 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 3 PHE A 113 CA - CB - CG ANGL. DEV. = 16.5 DEGREES REMARK 500 3 PHE A 113 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 3 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 3 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 3 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 3 LEU B 9 CB - CG - CD2 ANGL. DEV. = 11.0 DEGREES REMARK 500 3 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 3 ARG B 14 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 3 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 PHE A 113 CA - CB - CG ANGL. DEV. = 16.3 DEGREES REMARK 500 4 PHE A 113 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 4 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 4 LEU B 9 CB - CG - CD2 ANGL. DEV. = 11.6 DEGREES REMARK 500 4 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 4 ARG B 14 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 5 PHE A 113 CA - CB - CG ANGL. DEV. = 16.6 DEGREES REMARK 500 5 PHE A 113 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 5 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 5 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 5 VAL A 157 CA - CB - CG1 ANGL. DEV. = 12.5 DEGREES REMARK 500 5 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 5 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 5 ARG B 14 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 5 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 6 PHE A 113 CA - CB - CG ANGL. DEV. = 15.6 DEGREES REMARK 500 6 PHE A 113 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 6 ASP A 114 N - CA - CB ANGL. DEV. = -11.0 DEGREES REMARK 500 6 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 181 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 LYS A 96 98.70 140.85 REMARK 500 1 LYS A 100 -28.01 -166.21 REMARK 500 1 GLU A 117 85.03 64.54 REMARK 500 1 THR A 118 -21.64 -140.39 REMARK 500 1 PHE A 123 -55.32 -29.04 REMARK 500 1 GLU A 135 122.61 79.88 REMARK 500 1 LYS A 167 -70.13 -70.36 REMARK 500 1 ILE B 11 -13.93 -30.25 REMARK 500 1 GLU B 13 -78.94 -88.38 REMARK 500 1 ARG B 14 -142.70 -147.80 REMARK 500 1 LEU B 15 -72.67 -134.77 REMARK 500 1 LYS B 16 -106.09 147.24 REMARK 500 2 LYS A 96 128.90 116.40 REMARK 500 2 LYS A 100 -14.19 170.08 REMARK 500 2 ASP A 114 47.51 -73.25 REMARK 500 2 THR A 118 42.22 -89.56 REMARK 500 2 ASP A 152 57.44 -113.21 REMARK 500 2 ASP A 154 -39.07 78.15 REMARK 500 2 LYS A 167 -73.59 -76.43 REMARK 500 2 ILE B 11 -12.23 -37.41 REMARK 500 2 LYS B 16 -98.36 147.84 REMARK 500 3 LYS A 96 95.02 -165.87 REMARK 500 3 MET A 97 94.83 65.92 REMARK 500 3 ASP A 115 93.14 -66.22 REMARK 500 3 ASP A 154 -59.64 -160.75 REMARK 500 3 LYS A 167 -70.22 -66.49 REMARK 500 3 ILE B 11 -11.02 -36.32 REMARK 500 3 ARG B 12 -44.35 -28.98 REMARK 500 4 LYS A 96 100.17 -174.85 REMARK 500 4 LYS A 100 -70.55 138.02 REMARK 500 4 GLU A 117 71.56 53.11 REMARK 500 4 THR A 118 -55.95 -130.32 REMARK 500 4 ASP A 150 61.25 -100.64 REMARK 500 4 LYS A 167 -72.22 -71.71 REMARK 500 4 LYS A 168 95.69 48.33 REMARK 500 4 ILE B 11 -12.54 -34.50 REMARK 500 4 GLU B 13 110.99 70.08 REMARK 500 4 ARG B 14 84.80 177.25 REMARK 500 4 LYS B 16 111.91 173.93 REMARK 500 5 LYS A 96 93.83 119.69 REMARK 500 5 GLU A 99 -47.38 85.71 REMARK 500 5 ASN A 136 83.49 -68.09 REMARK 500 5 ASP A 154 -55.35 -162.63 REMARK 500 5 LYS A 167 -71.50 -73.00 REMARK 500 5 LEU A 171 75.97 -163.69 REMARK 500 5 ILE B 11 -9.20 -38.18 REMARK 500 5 ARG B 12 -47.78 -26.07 REMARK 500 5 LYS B 16 -97.52 -87.83 REMARK 500 6 GLN A 95 -77.87 -91.46 REMARK 500 6 LYS A 96 99.07 98.06 REMARK 500 REMARK 500 THIS ENTRY HAS 206 RAMACHANDRAN OUTLIERS. 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 110 0.09 SIDE CHAIN REMARK 500 1 PHE A 113 0.10 SIDE CHAIN REMARK 500 1 PHE A 162 0.13 SIDE CHAIN REMARK 500 2 PHE A 113 0.18 SIDE CHAIN REMARK 500 2 PHE A 162 0.12 SIDE CHAIN REMARK 500 3 PHE A 110 0.09 SIDE CHAIN REMARK 500 3 PHE A 113 0.16 SIDE CHAIN REMARK 500 3 PHE A 162 0.12 SIDE CHAIN REMARK 500 4 PHE A 110 0.08 SIDE CHAIN REMARK 500 4 PHE A 113 0.17 SIDE CHAIN REMARK 500 4 PHE A 162 0.12 SIDE CHAIN REMARK 500 5 PHE A 110 0.09 SIDE CHAIN REMARK 500 5 PHE A 113 0.14 SIDE CHAIN REMARK 500 5 PHE A 162 0.12 SIDE CHAIN REMARK 500 6 PHE A 113 0.19 SIDE CHAIN REMARK 500 6 PHE A 162 0.12 SIDE CHAIN REMARK 500 7 PHE A 110 0.09 SIDE CHAIN REMARK 500 7 PHE A 113 0.16 SIDE CHAIN REMARK 500 7 PHE A 162 0.11 SIDE CHAIN REMARK 500 8 PHE A 110 0.09 SIDE CHAIN REMARK 500 8 PHE A 113 0.14 SIDE CHAIN REMARK 500 8 PHE A 162 0.11 SIDE CHAIN REMARK 500 9 PHE A 110 0.09 SIDE CHAIN REMARK 500 9 PHE A 113 0.11 SIDE CHAIN REMARK 500 9 PHE A 162 0.11 SIDE CHAIN REMARK 500 10 PHE A 110 0.09 SIDE CHAIN REMARK 500 10 PHE A 113 0.17 SIDE CHAIN REMARK 500 10 PHE A 162 0.12 SIDE CHAIN REMARK 500 11 PHE A 110 0.09 SIDE CHAIN REMARK 500 11 PHE A 113 0.18 SIDE CHAIN REMARK 500 11 PHE A 162 0.12 SIDE CHAIN REMARK 500 12 PHE A 110 0.08 SIDE CHAIN REMARK 500 12 PHE A 113 0.16 SIDE CHAIN REMARK 500 12 PHE A 162 0.11 SIDE CHAIN REMARK 500 13 PHE A 113 0.09 SIDE CHAIN REMARK 500 13 PHE A 162 0.12 SIDE CHAIN REMARK 500 14 PHE A 110 0.09 SIDE CHAIN REMARK 500 14 PHE A 113 0.16 SIDE CHAIN REMARK 500 14 PHE A 162 0.11 SIDE CHAIN REMARK 500 15 PHE A 110 0.08 SIDE CHAIN REMARK 500 15 PHE A 113 0.18 SIDE CHAIN REMARK 500 15 PHE A 162 0.12 SIDE CHAIN REMARK 500 16 PHE A 110 0.08 SIDE CHAIN REMARK 500 16 PHE A 113 0.19 SIDE CHAIN REMARK 500 16 PHE A 162 0.12 SIDE CHAIN REMARK 500 17 PHE A 110 0.09 SIDE CHAIN REMARK 500 17 PHE A 113 0.12 SIDE CHAIN REMARK 500 17 PHE A 162 0.12 SIDE CHAIN REMARK 500 18 PHE A 110 0.09 SIDE CHAIN REMARK 500 18 PHE A 113 0.18 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2A4J A 94 172 UNP P41208 CETN2_HUMAN 94 172 DBREF 2A4J B 1 17 UNP Q96AX0 XPC_HUMAN 847 863 SEQRES 1 A 79 THR GLN LYS MET SER GLU LYS ASP THR LYS GLU GLU ILE SEQRES 2 A 79 LEU LYS ALA PHE LYS LEU PHE ASP ASP ASP GLU THR GLY SEQRES 3 A 79 LYS ILE SER PHE LYS ASN LEU LYS ARG VAL ALA LYS GLU SEQRES 4 A 79 LEU GLY GLU ASN LEU THR ASP GLU GLU LEU GLN GLU MET SEQRES 5 A 79 ILE ASP GLU ALA ASP ARG ASP GLY ASP GLY GLU VAL SER SEQRES 6 A 79 GLU GLN GLU PHE LEU ARG ILE MET LYS LYS THR SER LEU SEQRES 7 A 79 TYR SEQRES 1 B 17 ASN TRP LYS LEU LEU ALA LYS GLY LEU LEU ILE ARG GLU SEQRES 2 B 17 ARG LEU LYS ARG HELIX 1 1 LYS A 100 ASP A 114 1 15 HELIX 2 2 SER A 122 GLY A 134 1 13 HELIX 3 3 THR A 138 ASP A 150 1 13 HELIX 4 4 GLU A 161 LYS A 168 1 8 HELIX 5 5 ASN B 1 ILE B 11 1 11 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