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PDBsum entry 3vnn

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Ligase PDB id
3vnn
Jmol
Contents
Protein chain
124 a.a.
Waters ×3
HEADER    LIGASE                                  17-JAN-12   3VNN
TITLE     CRYSTAL STRUCTURE OF A SUB-DOMAIN OF THE NUCLEOTIDYLTRANSFERASE
TITLE    2 (ADENYLATION) DOMAIN OF HUMAN DNA LIGASE IV
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA LIGASE 4;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: A SUB-DOMAIN OF THE NUCLEOTIDYLTRANSFERASE (ADENYLATION)
COMPND   5 DOMAIN, UNP RESIDUES 268-405;
COMPND   6 SYNONYM: DNA LIGASE IV, POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP] 4;
COMPND   7 EC: 6.5.1.1;
COMPND   8 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: LIG4;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHAT5
KEYWDS    DNA LIGASE, NON-HOMOLOGOUS END JOINING, DNA REPAIR, XRCC4, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.OCHI,Q.WU,D.Y.CHIRGADZE,J.G.GROSSMANN,V.M.BOLANOS-GARCIA,
AUTHOR   2 T.L.BLUNDELL
REVDAT   2   24-JUL-13 3VNN    1       JRNL
REVDAT   1   20-JUN-12 3VNN    0
JRNL        AUTH   T.OCHI,Q.WU,D.Y.CHIRGADZE,J.G.GROSSMANN,V.M.BOLANOS-GARCIA,
JRNL        AUTH 2 T.L.BLUNDELL
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE ROLE OF DOMAIN FLEXIBILITY IN
JRNL        TITL 2 HUMAN DNA LIGASE IV
JRNL        REF    STRUCTURE                     V.  20  1212 2012
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   22658747
JRNL        DOI    10.1016/J.STR.2012.04.012
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.64
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9
REMARK   3   NUMBER OF REFLECTIONS             : 3811
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.277
REMARK   3   R VALUE            (WORKING SET) : 0.273
REMARK   3   FREE R VALUE                     : 0.305
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 381
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 30.6413 -  4.1842    0.98     1203   134  0.2742 0.2920
REMARK   3     2  4.1842 -  3.3224    1.00     1127   126  0.2581 0.2978
REMARK   3     3  3.3224 -  2.9028    1.00     1100   121  0.3042 0.3909
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.00
REMARK   3   SHRINKAGE RADIUS   : 0.73
REMARK   3   K_SOL              : 0.32
REMARK   3   B_SOL              : 95.26
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.640
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 89.06
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 109.81
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 8.89710
REMARK   3    B22 (A**2) : 8.89710
REMARK   3    B33 (A**2) : -17.79420
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.014            970
REMARK   3   ANGLE     :  1.971           1319
REMARK   3   CHIRALITY :  0.156            147
REMARK   3   PLANARITY :  0.011            173
REMARK   3   DIHEDRAL  : 18.975            331
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: all
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.1544  12.1520  62.2802
REMARK   3    T TENSOR
REMARK   3      T11:   1.1422 T22:   0.6554
REMARK   3      T33:   0.6698 T12:  -0.5319
REMARK   3      T13:   0.4325 T23:  -0.1712
REMARK   3    L TENSOR
REMARK   3      L11:   3.3707 L22:   1.3123
REMARK   3      L33:   2.7432 L12:  -0.9543
REMARK   3      L13:   1.4246 L23:   0.7508
REMARK   3    S TENSOR
REMARK   3      S11:   0.3848 S12:   0.0965 S13:   0.1399
REMARK   3      S21:  -0.0758 S22:   0.1461 S23:   0.0040
REMARK   3      S31:  -1.1068 S32:   0.6403 S33:  -0.2819
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3VNN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB095271.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765
REMARK 200  MONOCHROMATOR                  : SI (111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 3860
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 11.900
REMARK 200  R MERGE                    (I) : 0.06300
REMARK 200  R SYM                      (I) : 0.06300
REMARK 200   FOR THE DATA SET  : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.54400
REMARK 200  R SYM FOR SHELL            (I) : 0.54400
REMARK 200   FOR SHELL         : 5.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% PEG 6000, 100MM MES, 0.01MG/ML
REMARK 280  PAPAIN, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y,X,Z+1/4
REMARK 290       4555   Y,-X,Z+3/4
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z+1/2
REMARK 290       7555   Y,X,-Z+3/4
REMARK 290       8555   -Y,-X,-Z+1/4
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       98.69650
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.34825
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      148.04475
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       98.69650
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      148.04475
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.34825
REMARK 290
REMARK 290 REMARK: NULL
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. (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     GLY A   309
REMARK 465     SER A   310
REMARK 465     GLY A   346
REMARK 465     THR A   347
REMARK 465     LYS A   348
REMARK 465     PHE A   349
REMARK 465     ASP A   350
REMARK 465     ILE A   351
REMARK 465     LYS A   352
REMARK 465     ARG A   353
REMARK 465     MET A   354
REMARK 465     VAL A   355
REMARK 465     GLU A   356
REMARK 465     ASP A   357
REMARK 465     SER A   358
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 273    CG   CD   CE   NZ
REMARK 470     LYS A 283    CG   CD   CE   NZ
REMARK 470     ASP A 284    CG   OD1  OD2
REMARK 470     LYS A 289    CG   CD   CE   NZ
REMARK 470     SER A 305    OG
REMARK 470     ILE A 315    CG1  CG2  CD1
REMARK 470     LYS A 320    CG   CD   CE   NZ
REMARK 470     MET A 343    CG   SD   CE
REMARK 470     LYS A 345    CG   CD   CE   NZ
REMARK 470     LEU A 360    CG   CD1  CD2
REMARK 470     GLN A 361    CG   CD   OE1  NE2
REMARK 470     ASN A 374    CG   OD1  ND2
REMARK 470     LYS A 375    CG   CD   CE   NZ
REMARK 470     LYS A 376    CG   CD   CE   NZ
REMARK 470     LEU A 377    CG   CD1  CD2
REMARK 470     ARG A 383    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 384    CG   CD   CE   NZ
REMARK 470     GLU A 387    CG   CD   OE1  OE2
REMARK 470     GLN A 404    CG   CD   OE1  NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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   CG1  VAL A   369     CD1  LEU A   389              1.55
REMARK 500   O    GLU A   380     NH1  ARG A   385              2.09
REMARK 500   O    ASP A   322     ND2  ASN A   373              2.18
REMARK 500
REMARK 500 REMARK: NULL
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    TYR A 288   CZ    TYR A 288   CE2    -0.091
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    PHE A 393   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES
REMARK 500    PRO A 397   C   -  N   -  CA  ANGL. DEV. =  -9.4 DEGREES
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    ASP A 286       -7.24     89.52
REMARK 500    TYR A 296      155.12    177.10
REMARK 500    PHE A 302      -74.23    -99.61
REMARK 500    ALA A 321     -110.02     44.03
REMARK 500    GLN A 324      -57.43   -122.79
REMARK 500    ASN A 373       68.66     36.61
REMARK 500    ASN A 374      -17.44     66.76
REMARK 500    PHE A 393      -65.51   -136.77
REMARK 500    THR A 394      125.85     81.34
REMARK 500    ILE A 400       73.26     50.31
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 ASN A  317     ALA A  318                  141.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A 393        15.2      L          L   OUTSIDE RANGE
REMARK 500    ILE A 400        23.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X9N   RELATED DB: PDB
REMARK 900 A HUMAN HOMOLOG
REMARK 900 RELATED ID: 3L2P   RELATED DB: PDB
REMARK 900 A HUMAN HOMOLOG
REMARK 900 RELATED ID: 1IK9   RELATED DB: PDB
REMARK 900 A DIFFERENT POLYPEPTIDE FROM THE SAME PROTEIN
REMARK 900 RELATED ID: 3II6   RELATED DB: PDB
REMARK 900 THE BRCT DOMAINS OF THE SAME PROTEIN
REMARK 900 RELATED ID: 2E2W   RELATED DB: PDB
REMARK 900 THE FIRST BRCT DOMAIN OF THE SAME PROTEIN
DBREF  3VNN A  268   406  UNP    P49917   DNLI4_HUMAN    268    406
SEQRES   1 A  139  PHE TYR ILE GLU THR LYS LEU ASP GLY GLU ARG MET GLN
SEQRES   2 A  139  MET HIS LYS ASP GLY ASP VAL TYR LYS TYR PHE SER ARG
SEQRES   3 A  139  ASN GLY TYR ASN TYR THR ASP GLN PHE GLY ALA SER PRO
SEQRES   4 A  139  THR GLU GLY SER LEU THR PRO PHE ILE HIS ASN ALA PHE
SEQRES   5 A  139  LYS ALA ASP ILE GLN ILE CYS ILE LEU ASP GLY GLU MET
SEQRES   6 A  139  MET ALA TYR ASN PRO ASN THR GLN THR PHE MET GLN LYS
SEQRES   7 A  139  GLY THR LYS PHE ASP ILE LYS ARG MET VAL GLU ASP SER
SEQRES   8 A  139  ASP LEU GLN THR CYS TYR CYS VAL PHE ASP VAL LEU MET
SEQRES   9 A  139  VAL ASN ASN LYS LYS LEU GLY HIS GLU THR LEU ARG LYS
SEQRES  10 A  139  ARG TYR GLU ILE LEU SER SER ILE PHE THR PRO ILE PRO
SEQRES  11 A  139  GLY ARG ILE GLU ILE VAL GLN LYS THR
FORMUL   2  HOH   *3(H2 O)
HELIX    1   1 PRO A  313  ASN A  317  5                                   5
HELIX    2   2 THR A  381  PHE A  393  1                                  13
SHEET    1   A 4 VAL A 287  PHE A 291  0
SHEET    2   A 4 GLU A 277  ASP A 284 -1  N  ASP A 284   O  VAL A 287
SHEET    3   A 4 ILE A 325  ASN A 336 -1  O  MET A 332   N  GLU A 277
SHEET    4   A 4 THR A 341  PHE A 342 -1  O  THR A 341   N  ASN A 336
SHEET    1   B 5 VAL A 287  PHE A 291  0
SHEET    2   B 5 GLU A 277  ASP A 284 -1  N  ASP A 284   O  VAL A 287
SHEET    3   B 5 ILE A 325  ASN A 336 -1  O  MET A 332   N  GLU A 277
SHEET    4   B 5 GLN A 361  VAL A 372 -1  O  MET A 371   N  ILE A 327
SHEET    5   B 5 LYS A 375  LYS A 376 -1  O  LYS A 375   N  VAL A 372
CRYST1   39.086   39.086  197.393  90.00  90.00  90.00 P 41 2 2      8
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      0.025585  0.000000  0.000000        0.00000
SCALE2      0.000000  0.025585  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005066        0.00000
      
PROCHECK
Go to PROCHECK summary
 References