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PDBsum entry 1xsl

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Top Page protein dna_rna ligands metals Protein-protein interface(s) links
Transferase/DNA PDB id
1xsl
Jmol
Contents
Protein chains
327 a.a.
DNA/RNA
Ligands
CAC
Metals
_MG ×3
_NA ×6
Waters ×843
HEADER    TRANSFERASE/DNA                         19-OCT-04   1XSL
TITLE     CRYSTAL STRUCTURE OF HUMAN DNA POLYMERASE LAMBDA IN COMPLEX WITH A ONE
TITLE    2 NUCLEOTIDE DNA GAP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*CP*GP*GP*CP*AP*GP*CP*GP*CP*AP*C)-3';
COMPND   3 CHAIN: B, F, J, N;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: 5'-D(*GP*TP*GP*CP*GP*C)-3';
COMPND   7 CHAIN: C, G, K, O;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 3;
COMPND  10 MOLECULE: 5'-D(P*GP*CP*CP*G)-3';
COMPND  11 CHAIN: D, H, L, P;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 4;
COMPND  14 MOLECULE: DNA POLYMERASE LAMBDA;
COMPND  15 CHAIN: A, E, I, M;
COMPND  16 FRAGMENT: 39 KDA CATALYTIC C-TERMINAL DOMAIN;
COMPND  17 SYNONYM: POL LAMBDA, DNA POLYMERASE BETA-2, POL BETA2;
COMPND  18 EC: 2.7.7.7;
COMPND  19 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: TEMPLATE DNA;
SOURCE   4 MOL_ID: 2;
SOURCE   5 SYNTHETIC: YES;
SOURCE   6 OTHER_DETAILS: PRIMER DNA;
SOURCE   7 MOL_ID: 3;
SOURCE   8 SYNTHETIC: YES;
SOURCE   9 OTHER_DETAILS: DOWNSTREAM PRIMER DNA;
SOURCE  10 MOL_ID: 4;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606;
SOURCE  14 GENE: POLL;
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS    DNA POLYMERASE LAMBDA, PROTEIN-DNA COMPLEX, HELIX-HAIRPIN-HELIX,
KEYWDS   2 TRANSFERASE-DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.GARCIA-DIAZ,K.BEBENEK,J.M.KRAHN,T.A.KUNKEL,L.C.PEDERSEN
REVDAT   3   13-JUL-11 1XSL    1       VERSN
REVDAT   2   24-FEB-09 1XSL    1       VERSN
REVDAT   1   18-JAN-05 1XSL    0
JRNL        AUTH   M.GARCIA-DIAZ,K.BEBENEK,J.M.KRAHN,T.A.KUNKEL,L.C.PEDERSEN
JRNL        TITL   A CLOSED CONFORMATION FOR THE POL LAMBDA CATALYTIC CYCLE.
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  12    97 2005
JRNL        REFN                   ISSN 1545-9993
JRNL        PMID   15608652
JRNL        DOI    10.1038/NSMB876
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.GARCIA-DIAZ,K.BEBENEK,J.M.KRAHN,L.BLANCO,T.A.KUNKEL,
REMARK   1  AUTH 2 L.C.PEDERSEN
REMARK   1  TITL   A STRUCTURAL SOLUTION FOR THE DNA POLYMERASE-LAMBDA
REMARK   1  TITL 2 DEPENDENT REPAIR OF DNA GAPS WITH MINIMAL HOMOLOGY
REMARK   1  REF    MOL.CELL                      V.  13   561 2004
REMARK   1  REFN                   ISSN 1097-2765
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M GARCIA-DIAZ,K.BEBENEK,R.SABARIEGOS,O.DOMINGUEZ,
REMARK   1  AUTH 2 J.RODRIGUEZ,T.KIRCHHOFF,E.GARCIA-PALOMERO,A.J.PICHER,
REMARK   1  AUTH 3 R.JUAREZ,J.F.RUIZ,T.A.KUNKEL,L.BLANCO
REMARK   1  TITL   DNA POLYMERASE LAMBDA, A NOVEL DNA REPAIR ENZYME IN HUMAN
REMARK   1  TITL 2 CELLS
REMARK   1  REF    J.BIOL.CHEM.                  V. 277 13184 2002
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 3
REMARK   1  AUTH   K.BEBENEK,K.GARCIA-DIAZ,L.BLANCO,T.A.KUNKEL
REMARK   1  TITL   THE FRAMESHIFT INFIDELITY OF HUMAN DNA POLYMERASE LAMBDA.
REMARK   1  TITL 2 IMPLICATIONS FOR FUNCTION.
REMARK   1  REF    J.BIOL.CHEM.                  V. 278 34685 2003
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 4
REMARK   1  AUTH   M.GARCIA-DIAZ,K.BEBENEK,T.A.KUNKEL,L.BLANCO
REMARK   1  TITL   IDENTIFICATION OF AN INTRINSIC 5'-DEOXYRIBOSE-5-PHOSPHATE
REMARK   1  TITL 2 LYASE ACTIVITY IN HUMAN DNA POLYMERASE LAMBDA: A POSSIBLE
REMARK   1  TITL 3 ROLE IN BASE EXCISION REPAIR
REMARK   1  REF    J.BIOL.CHEM.                  V. 276 34659 2001
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.47
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 447347.110
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.2
REMARK   3   NUMBER OF REFLECTIONS             : 82636
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.252
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4166
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 11524
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740
REMARK   3   BIN FREE R VALUE                    : 0.3270
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 553
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10181
REMARK   3   NUCLEIC ACID ATOMS       : 1704
REMARK   3   HETEROGEN ATOMS          : 14
REMARK   3   SOLVENT ATOMS            : 843
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 29.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.60
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.29000
REMARK   3    B22 (A**2) : -3.54000
REMARK   3    B33 (A**2) : 0.25000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28
REMARK   3   ESD FROM SIGMAA              (A) : 0.28
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.94
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.260 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.040 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.840 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.390 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.31
REMARK   3   BSOL        : 33.89
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : GCMPD1.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : GCMPD1.TOP
REMARK   3  TOPOLOGY FILE  5   : ION.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1XSL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-04.
REMARK 100 THE RCSB ID CODE IS RCSB030720.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88074
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.14500
REMARK 200   FOR THE DATA SET  : 8.1700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CACODYLATE, SODIUM CHLORIDE, PH
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       95.75200
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.40600
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       95.75200
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.40600
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: THE PROTEIN IS A MONOMER THUS THE ASYMMETRIC UNIT
REMARK 300 REPRESENTS FOUR BIOLOGICAL UNITS
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, E
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, I
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, O, P, M
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH E1066  LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   241
REMARK 465     ALA A   242
REMARK 465     GLN A   243
REMARK 465     PRO A   244
REMARK 465     SER A   245
REMARK 465     SER A   246
REMARK 465     GLN A   247
REMARK 465     LYS A   248
REMARK 465     MET E   241
REMARK 465     ALA E   242
REMARK 465     GLN E   243
REMARK 465     PRO E   244
REMARK 465     SER E   245
REMARK 465     SER E   246
REMARK 465     GLN E   247
REMARK 465     LYS E   248
REMARK 465     ALA E   249
REMARK 465     THR E   250
REMARK 465     MET I   241
REMARK 465     ALA I   242
REMARK 465     GLN I   243
REMARK 465     PRO I   244
REMARK 465     SER I   245
REMARK 465     SER I   246
REMARK 465     GLN I   247
REMARK 465     LYS I   248
REMARK 465     ALA I   249
REMARK 465     MET M   241
REMARK 465     ALA M   242
REMARK 465     GLN M   243
REMARK 465     PRO M   244
REMARK 465     SER M   245
REMARK 465     SER M   246
REMARK 465     GLN M   247
REMARK 465     LYS M   248
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A 544    CG   CD   CE   NZ
REMARK 470     VAL A 545    CG1  CG2
REMARK 470     LEU E 254    CG   CD1  CD2
REMARK 470     LYS E 265    CG   CD   CE   NZ
REMARK 470     GLU E 311    CG   CD   OE1  OE2
REMARK 470     ARG E 323    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU E 330    CG   CD   OE1  OE2
REMARK 470     GLU E 361    CG   CD   OE1  OE2
REMARK 470     GLU E 390    CG   CD   OE1  OE2
REMARK 470     GLN E 453    CG   CD   OE1  NE2
REMARK 470     LYS E 544    CG   CD   CE   NZ
REMARK 470     VAL E 545    CG1  CG2
REMARK 470     THR I 250    OG1  CG2
REMARK 470     HIS I 255    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS I 273    CG   CD   CE   NZ
REMARK 470     HIS I 321    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG I 323    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU I 330    CG   CD   OE1  OE2
REMARK 470     GLU I 385    CG   CD   OE1  OE2
REMARK 470     LYS I 401    CG   CD   CE   NZ
REMARK 470     ASN I 539    CG   OD1
REMARK 470     LYS I 544    CG   CD   CE   NZ
REMARK 470     VAL I 545    CG1  CG2
REMARK 470     LYS M 544    CG   CD   CE   NZ
REMARK 470     VAL M 545    CG1  CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500     DG D   1   P      DG D   1   OP3    -0.087
REMARK 500     DG H   1   P      DG H   1   OP3    -0.085
REMARK 500     DG L   1   P      DG L   1   OP3    -0.085
REMARK 500     DG P   1   P      DG P   1   OP3    -0.086
REMARK 500    LEU I 565   C     PRO I 566   N       0.156
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    HIS A 290       10.75    -67.36
REMARK 500    LYS A 291      175.73    179.11
REMARK 500    CYS A 415     -131.55   -106.38
REMARK 500    ASN A 539     -178.40    -66.17
REMARK 500    VAL A 545       24.26   -141.45
REMARK 500    HIS E 321     -153.22   -139.50
REMARK 500    LEU E 322       92.17   -160.02
REMARK 500    ASN E 407      108.71   -166.39
REMARK 500    CYS E 415     -138.98   -104.24
REMARK 500    ARG E 438      -19.24   -140.59
REMARK 500    SER E 509     -177.25    -68.65
REMARK 500    ASN E 539     -152.82   -105.43
REMARK 500    CYS E 543     -168.60    -69.76
REMARK 500    ARG E 573       38.44    -98.71
REMARK 500    ASN I 253       42.91   -150.53
REMARK 500    SER I 319       -7.50   -150.74
REMARK 500    LYS I 324      -35.45    -37.07
REMARK 500    ASN I 407      107.94   -167.22
REMARK 500    CYS I 415     -134.36   -107.91
REMARK 500    ARG I 438      -35.60   -134.44
REMARK 500    GLU I 454        0.18    -68.33
REMARK 500    ARG I 573       43.38   -104.18
REMARK 500    ASN M 407      106.83   -161.77
REMARK 500    CYS M 415     -138.76   -108.66
REMARK 500    ASN M 539     -164.44    -74.78
REMARK 500    LYS M 544      107.44    -45.16
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     DG H   1         0.06    SIDE CHAIN
REMARK 500     DG L   1         0.06    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    LEU I 565        -15.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1131        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A1164        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH B 703        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH H 856        DISTANCE =  5.70 ANGSTROMS
REMARK 525    HOH H 873        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH I1079        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH I1084        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH J 643        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH L 645        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH M1002        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH M1081        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH M1120        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH M1195        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH N 945        DISTANCE =  5.23 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A 961  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1  DG C   5   OP1
REMARK 620 2 SER A 339   O   173.7
REMARK 620 3 ILE A 341   O    91.3  91.9
REMARK 620 4 ALA A 344   O    93.3  92.6  81.2
REMARK 620 5 HOH C   8   O    89.8  88.0 170.5  89.3
REMARK 620 6 HOH C 156   O    87.5  86.7  97.4 178.4  92.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 991  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 702   O
REMARK 620 2 HOH B 703   O    87.3
REMARK 620 3 HOH B 704   O    70.7  91.1
REMARK 620 4 HOH D 701   O   164.6  94.3  93.9
REMARK 620 5 HOH B 700   O    87.3 173.5  83.6  89.9
REMARK 620 6 HOH B 705   O    99.2  90.4 169.7  96.1  94.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA E 962  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER E 339   O
REMARK 620 2  DG G   5   OP1 151.4
REMARK 620 3 ILE E 341   O   107.4  89.6
REMARK 620 4 ALA E 344   O    86.5  74.3  78.2
REMARK 620 5 HOH E1016   O    95.2 106.2  95.7 173.9
REMARK 620 6 HOH G 508   O    77.0  78.3 155.3  77.8 108.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F 992  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H 855   O
REMARK 620 2 HOH F 858   O    85.7
REMARK 620 3 HOH H 856   O    90.9  88.5
REMARK 620 4 HOH F 859   O   102.0 166.4 102.4
REMARK 620 5 HOH F 857   O    87.4  79.7 168.2  89.3
REMARK 620 6 HOH F 854   O   159.1  88.0 108.8  80.9  71.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 993  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H 868   O
REMARK 620 2 HOH H 872   O    67.2
REMARK 620 3 HOH H 873   O    78.1 117.7
REMARK 620 4 HOH H 874   O   166.4 111.8  91.2
REMARK 620 5 HOH L 870   O   104.0  66.6 175.7  87.3
REMARK 620 6 HOH H 871   O    80.3 131.4  87.8 107.9  88.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA I 963  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH K 303   O
REMARK 620 2  DG K   5   OP1  97.2
REMARK 620 3 SER I 339   O   100.5 162.1
REMARK 620 4 ILE I 341   O   105.0  85.4  87.4
REMARK 620 5 ALA I 344   O   174.3  77.6  84.7  72.5
REMARK 620 6 HOH K 875   O   108.3  83.0  94.0 145.9  73.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA J 965  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH L 645   O
REMARK 620 2 HOH J 642   O   105.1
REMARK 620 3 HOH J 643   O    93.9 148.1
REMARK 620 4 HOH J 641   O   110.9  89.7 107.3
REMARK 620 5 HOH J 644   O   156.0  82.0  71.0  91.7
REMARK 620 6 HOH L 640   O    83.4  68.3  89.2 156.7  78.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA M 964  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA M 344   O
REMARK 620 2 ILE M 341   O    84.7
REMARK 620 3 SER M 339   O    87.2  94.6
REMARK 620 4  DG O   5   OP1  91.9  97.5 167.7
REMARK 620 5 HOH M 978   O   171.1 101.9  86.4  93.1
REMARK 620 6 HOH O  39   O    79.9 164.6  84.2  83.6  93.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA N 966  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH P 940   O
REMARK 620 2 HOH N 945   O   118.9
REMARK 620 3 HOH N 944   O   161.4  79.1
REMARK 620 4 HOH N 943   O    90.2 150.6  71.6
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 961
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 962
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA I 963
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA M 964
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA J 965
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 966
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 991
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 992
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 993
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC D 950
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XSN   RELATED DB: PDB
REMARK 900 RELATED ID: 1XSP   RELATED DB: PDB
DBREF  1XSL A  242   575  UNP    Q9UGP5   DPOL_HUMAN     242    575
DBREF  1XSL M  242   575  UNP    Q9UGP5   DPOL_HUMAN     242    575
DBREF  1XSL E  242   575  UNP    Q9UGP5   DPOL_HUMAN     242    575
DBREF  1XSL I  242   575  UNP    Q9UGP5   DPOL_HUMAN     242    575
DBREF  1XSL B    1    11  PDB    1XSL     1XSL             1     11
DBREF  1XSL C    1     6  PDB    1XSL     1XSL             1      6
DBREF  1XSL D    1     4  PDB    1XSL     1XSL             1      4
DBREF  1XSL F    1    11  PDB    1XSL     1XSL             1     11
DBREF  1XSL G    1     6  PDB    1XSL     1XSL             1      6
DBREF  1XSL H    1     4  PDB    1XSL     1XSL             1      4
DBREF  1XSL J    1    11  PDB    1XSL     1XSL             1     11
DBREF  1XSL K    1     6  PDB    1XSL     1XSL             1      6
DBREF  1XSL L    1     4  PDB    1XSL     1XSL             1      4
DBREF  1XSL N    1    11  PDB    1XSL     1XSL             1     11
DBREF  1XSL O    1     6  PDB    1XSL     1XSL             1      6
DBREF  1XSL P    1     4  PDB    1XSL     1XSL             1      4
SEQADV 1XSL MET A  241  UNP  Q9UGP5              INITIATING METHIONINE
SEQADV 1XSL MET M  241  UNP  Q9UGP5              INITIATING METHIONINE
SEQADV 1XSL MET E  241  UNP  Q9UGP5              INITIATING METHIONINE
SEQADV 1XSL MET I  241  UNP  Q9UGP5              INITIATING METHIONINE
SEQRES   1 B   11   DC  DG  DG  DC  DA  DG  DC  DG  DC  DA  DC
SEQRES   1 C    6   DG  DT  DG  DC  DG  DC
SEQRES   1 D    4   DG  DC  DC  DG
SEQRES   1 F   11   DC  DG  DG  DC  DA  DG  DC  DG  DC  DA  DC
SEQRES   1 G    6   DG  DT  DG  DC  DG  DC
SEQRES   1 H    4   DG  DC  DC  DG
SEQRES   1 J   11   DC  DG  DG  DC  DA  DG  DC  DG  DC  DA  DC
SEQRES   1 K    6   DG  DT  DG  DC  DG  DC
SEQRES   1 L    4   DG  DC  DC  DG
SEQRES   1 N   11   DC  DG  DG  DC  DA  DG  DC  DG  DC  DA  DC
SEQRES   1 O    6   DG  DT  DG  DC  DG  DC
SEQRES   1 P    4   DG  DC  DC  DG
SEQRES   1 A  335  MET ALA GLN PRO SER SER GLN LYS ALA THR ASN HIS ASN
SEQRES   2 A  335  LEU HIS ILE THR GLU LYS LEU GLU VAL LEU ALA LYS ALA
SEQRES   3 A  335  TYR SER VAL GLN GLY ASP LYS TRP ARG ALA LEU GLY TYR
SEQRES   4 A  335  ALA LYS ALA ILE ASN ALA LEU LYS SER PHE HIS LYS PRO
SEQRES   5 A  335  VAL THR SER TYR GLN GLU ALA CYS SER ILE PRO GLY ILE
SEQRES   6 A  335  GLY LYS ARG MET ALA GLU LYS ILE ILE GLU ILE LEU GLU
SEQRES   7 A  335  SER GLY HIS LEU ARG LYS LEU ASP HIS ILE SER GLU SER
SEQRES   8 A  335  VAL PRO VAL LEU GLU LEU PHE SER ASN ILE TRP GLY ALA
SEQRES   9 A  335  GLY THR LYS THR ALA GLN MET TRP TYR GLN GLN GLY PHE
SEQRES  10 A  335  ARG SER LEU GLU ASP ILE ARG SER GLN ALA SER LEU THR
SEQRES  11 A  335  THR GLN GLN ALA ILE GLY LEU LYS HIS TYR SER ASP PHE
SEQRES  12 A  335  LEU GLU ARG MET PRO ARG GLU GLU ALA THR GLU ILE GLU
SEQRES  13 A  335  GLN THR VAL GLN LYS ALA ALA GLN ALA PHE ASN SER GLY
SEQRES  14 A  335  LEU LEU CYS VAL ALA CYS GLY SER TYR ARG ARG GLY LYS
SEQRES  15 A  335  ALA THR CYS GLY ASP VAL ASP VAL LEU ILE THR HIS PRO
SEQRES  16 A  335  ASP GLY ARG SER HIS ARG GLY ILE PHE SER ARG LEU LEU
SEQRES  17 A  335  ASP SER LEU ARG GLN GLU GLY PHE LEU THR ASP ASP LEU
SEQRES  18 A  335  VAL SER GLN GLU GLU ASN GLY GLN GLN GLN LYS TYR LEU
SEQRES  19 A  335  GLY VAL CYS ARG LEU PRO GLY PRO GLY ARG ARG HIS ARG
SEQRES  20 A  335  ARG LEU ASP ILE ILE VAL VAL PRO TYR SER GLU PHE ALA
SEQRES  21 A  335  CYS ALA LEU LEU TYR PHE THR GLY SER ALA HIS PHE ASN
SEQRES  22 A  335  ARG SER MET ARG ALA LEU ALA LYS THR LYS GLY MET SER
SEQRES  23 A  335  LEU SER GLU HIS ALA LEU SER THR ALA VAL VAL ARG ASN
SEQRES  24 A  335  THR HIS GLY CYS LYS VAL GLY PRO GLY ARG VAL LEU PRO
SEQRES  25 A  335  THR PRO THR GLU LYS ASP VAL PHE ARG LEU LEU GLY LEU
SEQRES  26 A  335  PRO TYR ARG GLU PRO ALA GLU ARG ASP TRP
SEQRES   1 E  335  MET ALA GLN PRO SER SER GLN LYS ALA THR ASN HIS ASN
SEQRES   2 E  335  LEU HIS ILE THR GLU LYS LEU GLU VAL LEU ALA LYS ALA
SEQRES   3 E  335  TYR SER VAL GLN GLY ASP LYS TRP ARG ALA LEU GLY TYR
SEQRES   4 E  335  ALA LYS ALA ILE ASN ALA LEU LYS SER PHE HIS LYS PRO
SEQRES   5 E  335  VAL THR SER TYR GLN GLU ALA CYS SER ILE PRO GLY ILE
SEQRES   6 E  335  GLY LYS ARG MET ALA GLU LYS ILE ILE GLU ILE LEU GLU
SEQRES   7 E  335  SER GLY HIS LEU ARG LYS LEU ASP HIS ILE SER GLU SER
SEQRES   8 E  335  VAL PRO VAL LEU GLU LEU PHE SER ASN ILE TRP GLY ALA
SEQRES   9 E  335  GLY THR LYS THR ALA GLN MET TRP TYR GLN GLN GLY PHE
SEQRES  10 E  335  ARG SER LEU GLU ASP ILE ARG SER GLN ALA SER LEU THR
SEQRES  11 E  335  THR GLN GLN ALA ILE GLY LEU LYS HIS TYR SER ASP PHE
SEQRES  12 E  335  LEU GLU ARG MET PRO ARG GLU GLU ALA THR GLU ILE GLU
SEQRES  13 E  335  GLN THR VAL GLN LYS ALA ALA GLN ALA PHE ASN SER GLY
SEQRES  14 E  335  LEU LEU CYS VAL ALA CYS GLY SER TYR ARG ARG GLY LYS
SEQRES  15 E  335  ALA THR CYS GLY ASP VAL ASP VAL LEU ILE THR HIS PRO
SEQRES  16 E  335  ASP GLY ARG SER HIS ARG GLY ILE PHE SER ARG LEU LEU
SEQRES  17 E  335  ASP SER LEU ARG GLN GLU GLY PHE LEU THR ASP ASP LEU
SEQRES  18 E  335  VAL SER GLN GLU GLU ASN GLY GLN GLN GLN LYS TYR LEU
SEQRES  19 E  335  GLY VAL CYS ARG LEU PRO GLY PRO GLY ARG ARG HIS ARG
SEQRES  20 E  335  ARG LEU ASP ILE ILE VAL VAL PRO TYR SER GLU PHE ALA
SEQRES  21 E  335  CYS ALA LEU LEU TYR PHE THR GLY SER ALA HIS PHE ASN
SEQRES  22 E  335  ARG SER MET ARG ALA LEU ALA LYS THR LYS GLY MET SER
SEQRES  23 E  335  LEU SER GLU HIS ALA LEU SER THR ALA VAL VAL ARG ASN
SEQRES  24 E  335  THR HIS GLY CYS LYS VAL GLY PRO GLY ARG VAL LEU PRO
SEQRES  25 E  335  THR PRO THR GLU LYS ASP VAL PHE ARG LEU LEU GLY LEU
SEQRES  26 E  335  PRO TYR ARG GLU PRO ALA GLU ARG ASP TRP
SEQRES   1 I  335  MET ALA GLN PRO SER SER GLN LYS ALA THR ASN HIS ASN
SEQRES   2 I  335  LEU HIS ILE THR GLU LYS LEU GLU VAL LEU ALA LYS ALA
SEQRES   3 I  335  TYR SER VAL GLN GLY ASP LYS TRP ARG ALA LEU GLY TYR
SEQRES   4 I  335  ALA LYS ALA ILE ASN ALA LEU LYS SER PHE HIS LYS PRO
SEQRES   5 I  335  VAL THR SER TYR GLN GLU ALA CYS SER ILE PRO GLY ILE
SEQRES   6 I  335  GLY LYS ARG MET ALA GLU LYS ILE ILE GLU ILE LEU GLU
SEQRES   7 I  335  SER GLY HIS LEU ARG LYS LEU ASP HIS ILE SER GLU SER
SEQRES   8 I  335  VAL PRO VAL LEU GLU LEU PHE SER ASN ILE TRP GLY ALA
SEQRES   9 I  335  GLY THR LYS THR ALA GLN MET TRP TYR GLN GLN GLY PHE
SEQRES  10 I  335  ARG SER LEU GLU ASP ILE ARG SER GLN ALA SER LEU THR
SEQRES  11 I  335  THR GLN GLN ALA ILE GLY LEU LYS HIS TYR SER ASP PHE
SEQRES  12 I  335  LEU GLU ARG MET PRO ARG GLU GLU ALA THR GLU ILE GLU
SEQRES  13 I  335  GLN THR VAL GLN LYS ALA ALA GLN ALA PHE ASN SER GLY
SEQRES  14 I  335  LEU LEU CYS VAL ALA CYS GLY SER TYR ARG ARG GLY LYS
SEQRES  15 I  335  ALA THR CYS GLY ASP VAL ASP VAL LEU ILE THR HIS PRO
SEQRES  16 I  335  ASP GLY ARG SER HIS ARG GLY ILE PHE SER ARG LEU LEU
SEQRES  17 I  335  ASP SER LEU ARG GLN GLU GLY PHE LEU THR ASP ASP LEU
SEQRES  18 I  335  VAL SER GLN GLU GLU ASN GLY GLN GLN GLN LYS TYR LEU
SEQRES  19 I  335  GLY VAL CYS ARG LEU PRO GLY PRO GLY ARG ARG HIS ARG
SEQRES  20 I  335  ARG LEU ASP ILE ILE VAL VAL PRO TYR SER GLU PHE ALA
SEQRES  21 I  335  CYS ALA LEU LEU TYR PHE THR GLY SER ALA HIS PHE ASN
SEQRES  22 I  335  ARG SER MET ARG ALA LEU ALA LYS THR LYS GLY MET SER
SEQRES  23 I  335  LEU SER GLU HIS ALA LEU SER THR ALA VAL VAL ARG ASN
SEQRES  24 I  335  THR HIS GLY CYS LYS VAL GLY PRO GLY ARG VAL LEU PRO
SEQRES  25 I  335  THR PRO THR GLU LYS ASP VAL PHE ARG LEU LEU GLY LEU
SEQRES  26 I  335  PRO TYR ARG GLU PRO ALA GLU ARG ASP TRP
SEQRES   1 M  335  MET ALA GLN PRO SER SER GLN LYS ALA THR ASN HIS ASN
SEQRES   2 M  335  LEU HIS ILE THR GLU LYS LEU GLU VAL LEU ALA LYS ALA
SEQRES   3 M  335  TYR SER VAL GLN GLY ASP LYS TRP ARG ALA LEU GLY TYR
SEQRES   4 M  335  ALA LYS ALA ILE ASN ALA LEU LYS SER PHE HIS LYS PRO
SEQRES   5 M  335  VAL THR SER TYR GLN GLU ALA CYS SER ILE PRO GLY ILE
SEQRES   6 M  335  GLY LYS ARG MET ALA GLU LYS ILE ILE GLU ILE LEU GLU
SEQRES   7 M  335  SER GLY HIS LEU ARG LYS LEU ASP HIS ILE SER GLU SER
SEQRES   8 M  335  VAL PRO VAL LEU GLU LEU PHE SER ASN ILE TRP GLY ALA
SEQRES   9 M  335  GLY THR LYS THR ALA GLN MET TRP TYR GLN GLN GLY PHE
SEQRES  10 M  335  ARG SER LEU GLU ASP ILE ARG SER GLN ALA SER LEU THR
SEQRES  11 M  335  THR GLN GLN ALA ILE GLY LEU LYS HIS TYR SER ASP PHE
SEQRES  12 M  335  LEU GLU ARG MET PRO ARG GLU GLU ALA THR GLU ILE GLU
SEQRES  13 M  335  GLN THR VAL GLN LYS ALA ALA GLN ALA PHE ASN SER GLY
SEQRES  14 M  335  LEU LEU CYS VAL ALA CYS GLY SER TYR ARG ARG GLY LYS
SEQRES  15 M  335  ALA THR CYS GLY ASP VAL ASP VAL LEU ILE THR HIS PRO
SEQRES  16 M  335  ASP GLY ARG SER HIS ARG GLY ILE PHE SER ARG LEU LEU
SEQRES  17 M  335  ASP SER LEU ARG GLN GLU GLY PHE LEU THR ASP ASP LEU
SEQRES  18 M  335  VAL SER GLN GLU GLU ASN GLY GLN GLN GLN LYS TYR LEU
SEQRES  19 M  335  GLY VAL CYS ARG LEU PRO GLY PRO GLY ARG ARG HIS ARG
SEQRES  20 M  335  ARG LEU ASP ILE ILE VAL VAL PRO TYR SER GLU PHE ALA
SEQRES  21 M  335  CYS ALA LEU LEU TYR PHE THR GLY SER ALA HIS PHE ASN
SEQRES  22 M  335  ARG SER MET ARG ALA LEU ALA LYS THR LYS GLY MET SER
SEQRES  23 M  335  LEU SER GLU HIS ALA LEU SER THR ALA VAL VAL ARG ASN
SEQRES  24 M  335  THR HIS GLY CYS LYS VAL GLY PRO GLY ARG VAL LEU PRO
SEQRES  25 M  335  THR PRO THR GLU LYS ASP VAL PHE ARG LEU LEU GLY LEU
SEQRES  26 M  335  PRO TYR ARG GLU PRO ALA GLU ARG ASP TRP
HET     NA  A 961       1
HET     NA  E 962       1
HET     NA  I 963       1
HET     NA  M 964       1
HET     NA  J 965       1
HET     NA  N 966       1
HET     MG  B 991       1
HET     MG  F 992       1
HET     MG  H 993       1
HET    CAC  D 950       5
HETNAM      NA SODIUM ION
HETNAM      MG MAGNESIUM ION
HETNAM     CAC CACODYLATE ION
HETSYN     CAC DIMETHYLARSINATE
FORMUL  17   NA    6(NA 1+)
FORMUL  23   MG    3(MG 2+)
FORMUL  26  CAC    C2 H6 AS O2 1-
FORMUL  27  HOH   *843(H2 O)
HELIX    1   1 ASN A  253  GLN A  270  1                                  18
HELIX    2   2 ASP A  272  SER A  288  1                                  17
HELIX    3   3 SER A  295  ILE A  302  1                                   8
HELIX    4   4 GLY A  306  GLY A  320  1                                  15
HELIX    5   5 LEU A  322  HIS A  327  1                                   6
HELIX    6   6 SER A  331  ASN A  340  1                                  10
HELIX    7   7 GLY A  345  GLN A  355  1                                  11
HELIX    8   8 SER A  359  ALA A  367  1                                   9
HELIX    9   9 THR A  370  HIS A  379  1                                  10
HELIX   10  10 HIS A  379  GLU A  385  1                                   7
HELIX   11  11 ARG A  389  ALA A  405  1                                  17
HELIX   12  12 CYS A  415  ARG A  420  1                                   6
HELIX   13  13 ILE A  443  GLU A  454  1                                  12
HELIX   14  14 PRO A  495  SER A  497  5                                   3
HELIX   15  15 GLU A  498  GLY A  508  1                                  11
HELIX   16  16 SER A  509  LYS A  523  1                                  15
HELIX   17  17 THR A  555  LEU A  563  1                                   9
HELIX   18  18 GLU A  569  ARG A  573  5                                   5
HELIX   19  19 ASN E  253  GLN E  270  1                                  18
HELIX   20  20 ASP E  272  SER E  288  1                                  17
HELIX   21  21 SER E  295  SER E  301  1                                   7
HELIX   22  22 GLY E  306  GLY E  320  1                                  15
HELIX   23  23 LEU E  322  HIS E  327  1                                   6
HELIX   24  24 SER E  331  SER E  339  1                                   9
HELIX   25  25 GLY E  345  GLN E  355  1                                  11
HELIX   26  26 SER E  359  ALA E  367  1                                   9
HELIX   27  27 THR E  370  HIS E  379  1                                  10
HELIX   28  28 HIS E  379  GLU E  385  1                                   7
HELIX   29  29 ARG E  389  ALA E  405  1                                  17
HELIX   30  30 CYS E  415  ARG E  420  1                                   6
HELIX   31  31 ILE E  443  GLU E  454  1                                  12
HELIX   32  32 PRO E  495  GLY E  508  1                                  14
HELIX   33  33 SER E  509  LYS E  523  1                                  15
HELIX   34  34 THR E  555  GLY E  564  1                                  10
HELIX   35  35 GLU E  569  ARG E  573  5                                   5
HELIX   36  36 ASN I  253  GLN I  270  1                                  18
HELIX   37  37 ASP I  272  SER I  288  1                                  17
HELIX   38  38 SER I  295  SER I  301  1                                   7
HELIX   39  39 GLY I  306  GLY I  320  1                                  15
HELIX   40  40 LEU I  322  ILE I  328  5                                   7
HELIX   41  41 SER I  331  ASN I  340  1                                  10
HELIX   42  42 GLY I  345  GLN I  355  1                                  11
HELIX   43  43 SER I  359  ALA I  367  1                                   9
HELIX   44  44 THR I  370  HIS I  379  1                                  10
HELIX   45  45 HIS I  379  GLU I  385  1                                   7
HELIX   46  46 ARG I  389  GLN I  404  1                                  16
HELIX   47  47 CYS I  415  ARG I  420  1                                   6
HELIX   48  48 GLY I  442  GLU I  454  1                                  13
HELIX   49  49 PRO I  495  SER I  497  5                                   3
HELIX   50  50 GLU I  498  GLY I  508  1                                  11
HELIX   51  51 SER I  509  LYS I  523  1                                  15
HELIX   52  52 THR I  555  LEU I  563  1                                   9
HELIX   53  53 GLU I  569  ARG I  573  5                                   5
HELIX   54  54 ASN M  253  GLN M  270  1                                  18
HELIX   55  55 ASP M  272  PHE M  289  1                                  18
HELIX   56  56 SER M  295  ILE M  302  1                                   8
HELIX   57  57 GLY M  306  GLY M  320  1                                  15
HELIX   58  58 LEU M  322  HIS M  327  5                                   6
HELIX   59  59 SER M  331  ASN M  340  1                                  10
HELIX   60  60 GLY M  345  GLN M  355  1                                  11
HELIX   61  61 SER M  359  ALA M  367  1                                   9
HELIX   62  62 THR M  370  HIS M  379  1                                  10
HELIX   63  63 HIS M  379  GLU M  385  1                                   7
HELIX   64  64 ARG M  389  ALA M  405  1                                  17
HELIX   65  65 CYS M  415  ARG M  420  1                                   6
HELIX   66  66 ILE M  443  GLU M  454  1                                  12
HELIX   67  67 PRO M  495  SER M  497  5                                   3
HELIX   68  68 GLU M  498  GLY M  508  1                                  11
HELIX   69  69 SER M  509  LYS M  523  1                                  15
HELIX   70  70 THR M  555  LEU M  563  1                                   9
HELIX   71  71 GLU M  569  ARG M  573  5                                   5
SHEET    1   A 2 MET A 387  PRO A 388  0
SHEET    2   A 2 THR A 424  CYS A 425 -1  O  CYS A 425   N  MET A 387
SHEET    1   B 5 LEU A 411  ALA A 414  0
SHEET    2   B 5 VAL A 428  THR A 433 -1  O  THR A 433   N  LEU A 411
SHEET    3   B 5 ARG A 487  VAL A 493  1  O  ILE A 492   N  ILE A 432
SHEET    4   B 5 GLN A 470  CYS A 477 -1  N  CYS A 477   O  ARG A 487
SHEET    5   B 5 LEU A 457  ASN A 467 -1  N  ASN A 467   O  GLN A 470
SHEET    1   C 2 MET A 525  LEU A 527  0
SHEET    2   C 2 LEU A 532  THR A 534 -1  O  SER A 533   N  SER A 526
SHEET    1   D 2 MET E 387  PRO E 388  0
SHEET    2   D 2 THR E 424  CYS E 425 -1  O  CYS E 425   N  MET E 387
SHEET    1   E 5 LEU E 411  ALA E 414  0
SHEET    2   E 5 VAL E 428  THR E 433 -1  O  LEU E 431   N  VAL E 413
SHEET    3   E 5 ARG E 487  VAL E 493  1  O  ILE E 492   N  ILE E 432
SHEET    4   E 5 GLN E 470  CYS E 477 -1  N  GLN E 471   O  VAL E 493
SHEET    5   E 5 LEU E 457  ASN E 467 -1  N  LEU E 461   O  LEU E 474
SHEET    1   F 3 MET E 525  LEU E 527  0
SHEET    2   F 3 LEU E 532  THR E 534 -1  O  SER E 533   N  SER E 526
SHEET    3   F 3 VAL E 550  LEU E 551 -1  O  LEU E 551   N  LEU E 532
SHEET    1   G 2 MET I 387  PRO I 388  0
SHEET    2   G 2 THR I 424  CYS I 425 -1  O  CYS I 425   N  MET I 387
SHEET    1   H 5 LEU I 411  ALA I 414  0
SHEET    2   H 5 VAL I 428  THR I 433 -1  O  THR I 433   N  LEU I 411
SHEET    3   H 5 ARG I 487  VAL I 493  1  O  ILE I 492   N  ILE I 432
SHEET    4   H 5 GLN I 470  CYS I 477 -1  N  GLY I 475   O  LEU I 489
SHEET    5   H 5 LEU I 457  ASN I 467 -1  N  ASP I 459   O  VAL I 476
SHEET    1   I 3 MET I 525  LEU I 527  0
SHEET    2   I 3 LEU I 532  THR I 534 -1  O  SER I 533   N  SER I 526
SHEET    3   I 3 VAL I 550  LEU I 551 -1  O  LEU I 551   N  LEU I 532
SHEET    1   J 2 VAL I 537  ARG I 538  0
SHEET    2   J 2 LYS I 544  GLY I 546 -1  O  VAL I 545   N  VAL I 537
SHEET    1   K 2 MET M 387  PRO M 388  0
SHEET    2   K 2 THR M 424  CYS M 425 -1  O  CYS M 425   N  MET M 387
SHEET    1   L 5 LEU M 411  ALA M 414  0
SHEET    2   L 5 VAL M 428  THR M 433 -1  O  LEU M 431   N  VAL M 413
SHEET    3   L 5 ARG M 487  VAL M 493  1  O  ILE M 492   N  ILE M 432
SHEET    4   L 5 GLN M 470  CYS M 477 -1  N  GLY M 475   O  LEU M 489
SHEET    5   L 5 LEU M 457  ASN M 467 -1  N  VAL M 462   O  LEU M 474
SHEET    1   M 3 MET M 525  LEU M 527  0
SHEET    2   M 3 LEU M 532  THR M 534 -1  O  SER M 533   N  SER M 526
SHEET    3   M 3 VAL M 550  LEU M 551 -1  O  LEU M 551   N  LEU M 532
SHEET    1   N 2 VAL M 537  ARG M 538  0
SHEET    2   N 2 LYS M 544  GLY M 546 -1  O  VAL M 545   N  VAL M 537
SSBOND   1 CYS A  543    CYS M  543                          1555   1555  2.02
LINK        NA    NA A 961                 OP1  DG C   5     1555   1555  2.45
LINK        NA    NA A 961                 O   SER A 339     1555   1555  2.47
LINK        MG    MG B 991                 O   HOH B 702     1555   1555  2.08
LINK        MG    MG B 991                 O   HOH B 703     1555   1555  2.08
LINK        MG    MG B 991                 O   HOH B 704     1555   1555  2.07
LINK        MG    MG B 991                 O   HOH D 701     1555   1555  2.14
LINK        MG    MG B 991                 O   HOH B 700     1555   1555  1.99
LINK        MG    MG B 991                 O   HOH B 705     1555   1555  2.65
LINK        NA    NA E 962                 O   SER E 339     1555   1555  2.60
LINK        NA    NA E 962                 OP1  DG G   5     1555   1555  2.57
LINK        MG    MG F 992                 O   HOH H 855     1555   1555  2.25
LINK        MG    MG F 992                 O   HOH F 858     1555   1555  2.17
LINK        MG    MG F 992                 O   HOH H 856     1555   1555  1.91
LINK        MG    MG F 992                 O   HOH F 859     1555   1555  2.16
LINK        MG    MG F 992                 O   HOH F 857     1555   1555  1.91
LINK        MG    MG F 992                 O   HOH F 854     1555   1555  2.32
LINK        MG    MG H 993                 O   HOH H 868     1555   1555  1.61
LINK        MG    MG H 993                 O   HOH H 872     1555   1555  2.67
LINK        MG    MG H 993                 O   HOH H 873     1555   1555  1.92
LINK        MG    MG H 993                 O   HOH H 874     1555   1555  1.92
LINK        MG    MG H 993                 O   HOH L 870     1555   1555  2.36
LINK        MG    MG H 993                 O   HOH H 871     1555   1555  2.30
LINK        NA    NA I 963                 O   HOH K 303     1555   1555  2.48
LINK        NA    NA I 963                 OP1  DG K   5     1555   1555  2.55
LINK        NA    NA I 963                 O   SER I 339     1555   1555  2.49
LINK        NA    NA J 965                 O   HOH L 645     1555   1555  2.34
LINK        NA    NA J 965                 O   HOH J 642     1555   1555  2.24
LINK        NA    NA J 965                 O   HOH J 643     1555   1555  2.36
LINK        NA    NA J 965                 O   HOH J 641     1555   1555  2.36
LINK        NA    NA M 964                 O   ALA M 344     1555   1555  2.42
LINK        NA    NA M 964                 O   ILE M 341     1555   1555  2.59
LINK        NA    NA M 964                 O   SER M 339     1555   1555  2.41
LINK        NA    NA M 964                 OP1  DG O   5     1555   1555  2.32
LINK        NA    NA N 966                 O   HOH P 940     1555   1555  2.31
LINK        NA    NA N 966                 O   HOH N 945     1555   1555  2.22
LINK        NA    NA N 966                 O   HOH N 944     1555   1555  2.40
LINK        NA    NA N 966                 O   HOH N 943     1555   1555  2.03
LINK         O   ILE A 341                NA    NA A 961     1555   1555  2.67
LINK         O   ALA A 344                NA    NA A 961     1555   1555  2.65
LINK         O   ILE E 341                NA    NA E 962     1555   1555  2.71
LINK         O   ALA E 344                NA    NA E 962     1555   1555  2.79
LINK         O   ILE I 341                NA    NA I 963     1555   1555  2.82
LINK         O   ALA I 344                NA    NA I 963     1555   1555  2.80
LINK        NA    NA A 961                 O   HOH C   8     1555   1555  2.60
LINK        NA    NA A 961                 O   HOH C 156     1555   1555  2.84
LINK        NA    NA E 962                 O   HOH E1016     1555   1555  2.79
LINK        NA    NA E 962                 O   HOH G 508     1555   1555  2.93
LINK        NA    NA I 963                 O   HOH K 875     1555   1555  2.74
LINK        NA    NA M 964                 O   HOH M 978     1555   1555  2.69
LINK        NA    NA M 964                 O   HOH O  39     1555   1555  2.62
LINK        NA    NA J 965                 O   HOH J 644     1555   1555  2.60
LINK        NA    NA J 965                 O   HOH L 640     1555   1555  2.61
CISPEP   1 GLY A  508    SER A  509          0        -0.09
CISPEP   2 GLY E  508    SER E  509          0         0.23
CISPEP   3 GLY I  508    SER I  509          0         0.05
CISPEP   4 GLY M  508    SER M  509          0         0.91
SITE     1 AC1  6 SER A 339  ILE A 341  ALA A 344   DG C   5
SITE     2 AC1  6 HOH C   8  HOH C 156
SITE     1 AC2  6 SER E 339  ILE E 341  ALA E 344  HOH E1016
SITE     2 AC2  6  DG G   5  HOH G 508
SITE     1 AC3  6 SER I 339  ILE I 341  ALA I 344   DG K   5
SITE     2 AC3  6 HOH K 303  HOH K 875
SITE     1 AC4  6 SER M 339  ILE M 341  ALA M 344  HOH M 978
SITE     2 AC4  6  DG O   5  HOH O  39
SITE     1 AC5  6 HOH J 641  HOH J 642  HOH J 643  HOH J 644
SITE     2 AC5  6 HOH L 640  HOH L 645
SITE     1 AC6  4 HOH N 943  HOH N 944  HOH N 945  HOH P 940
SITE     1 AC7  6 HOH B 700  HOH B 702  HOH B 703  HOH B 704
SITE     2 AC7  6 HOH B 705  HOH D 701
SITE     1 AC8  6 HOH F 854  HOH F 857  HOH F 858  HOH F 859
SITE     2 AC8  6 HOH H 855  HOH H 856
SITE     1 AC9  6 HOH H 868  HOH H 871  HOH H 872  HOH H 873
SITE     2 AC9  6 HOH H 874  HOH L 870
SITE     1 BC1  3  DC D   3   DG D   4   DG P   4
CRYST1  191.504   98.812  104.519  90.00  90.00  90.00 P 21 21 2    16
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      0.005222  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010120  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009568        0.00000
      
PROCHECK
Go to PROCHECK summary
 References