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PDBsum entry 4ic7

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Transferase PDB id
4ic7
Jmol
Contents
Protein chains
355 a.a.
111 a.a.
123 a.a.
Ligands
ANP ×2
Waters ×83
HEADER    TRANSFERASE                             10-DEC-12   4IC7
TITLE     CRYSTAL STRUCTURE OF THE ERK5 KINASE DOMAIN IN COMPLEX WITH AN MKK5
TITLE    2 BINDING FRAGMENT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 7;
COMPND   3 CHAIN: A, D;
COMPND   4 SYNONYM: MAP KINASE 7, MAPK 7, BIG MAP KINASE 1, BMK-1, EXTRACELLULAR
COMPND   5 SIGNAL-REGULATED KINASE 5, ERK-5;
COMPND   6 EC: 2.7.11.24;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5;
COMPND  10 CHAIN: E, B;
COMPND  11 SYNONYM: MAP KINASE KINASE 5, MAPKK 5, MAPK/ERK KINASE 5, MEK 5;
COMPND  12 EC: 2.7.12.2;
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: MAPK7, BMK1, ERK5, PRKM7;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  10 ORGANISM_COMMON: HUMAN;
SOURCE  11 ORGANISM_TAXID: 9606;
SOURCE  12 GENE: MAP2K5, MEK5, MKK5, PRKMK5;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    KINASE DOMAIN, SIGNALING PROTEIN COMPLEX, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.GOGL,A.REMENYI
REVDAT   2   07-AUG-13 4IC7    1       JRNL
REVDAT   1   13-FEB-13 4IC7    0
JRNL        AUTH   G.GLATZ,G.GOGL,A.ALEXA,A.REMENYI
JRNL        TITL   STRUCTURAL MECHANISM FOR THE SPECIFIC ASSEMBLY AND
JRNL        TITL 2 ACTIVATION OF THE EXTRACELLULAR SIGNAL REGULATED KINASE 5
JRNL        TITL 3 (ERK5) MODULE.
JRNL        REF    J.BIOL.CHEM.                  V. 288  8596 2013
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   23382384
JRNL        DOI    10.1074/JBC.M113.452235
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.27
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 39029
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213
REMARK   3   R VALUE            (WORKING SET) : 0.211
REMARK   3   FREE R VALUE                     : 0.258
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010
REMARK   3   FREE R VALUE TEST SET COUNT      : 1955
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 48.2773 -  6.2621    1.00     2667   143  0.1713 0.2022
REMARK   3     2  6.2621 -  4.9721    1.00     2661   135  0.1995 0.2500
REMARK   3     3  4.9721 -  4.3440    1.00     2653   137  0.1699 0.1913
REMARK   3     4  4.3440 -  3.9470    1.00     2665   157  0.1851 0.2475
REMARK   3     5  3.9470 -  3.6642    1.00     2622   145  0.2110 0.2603
REMARK   3     6  3.6642 -  3.4483    1.00     2670   134  0.2210 0.2838
REMARK   3     7  3.4483 -  3.2756    1.00     2659   128  0.2357 0.2576
REMARK   3     8  3.2756 -  3.1331    1.00     2691   120  0.2692 0.3012
REMARK   3     9  3.1331 -  3.0125    1.00     2636   136  0.2630 0.3630
REMARK   3    10  3.0125 -  2.9085    1.00     2658   153  0.2691 0.3324
REMARK   3    11  2.9085 -  2.8176    1.00     2615   148  0.2811 0.3648
REMARK   3    12  2.8176 -  2.7371    0.99     2631   146  0.2868 0.3758
REMARK   3    13  2.7371 -  2.6650    0.99     2622   138  0.2992 0.3322
REMARK   3    14  2.6650 -  2.6000    0.98     2624   135  0.3124 0.4001
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.010
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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      :  0.008           7486
REMARK   3   ANGLE     :  1.584          10209
REMARK   3   CHIRALITY :  0.117           1148
REMARK   3   PLANARITY :  0.011           1327
REMARK   3   DIHEDRAL  : 18.998           2763
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
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 4IC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-12.
REMARK 100 THE RCSB ID CODE IS RCSB076570.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-JUL-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06DA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39147
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.270
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 48% PEG 200, 100MM MIB, PH 6.5, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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+3/4
REMARK 290       4555   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      135.62000
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      203.43000
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       67.81000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     GLU A     3
REMARK 465     PRO A     4
REMARK 465     LEU A     5
REMARK 465     LYS A     6
REMARK 465     GLU A     7
REMARK 465     GLU A     8
REMARK 465     ASP A     9
REMARK 465     GLY A    10
REMARK 465     GLU A    11
REMARK 465     ASP A    12
REMARK 465     GLY A    13
REMARK 465     SER A    14
REMARK 465     ALA A    15
REMARK 465     GLU A    16
REMARK 465     PRO A    17
REMARK 465     PRO A    18
REMARK 465     GLY A    19
REMARK 465     PRO A    20
REMARK 465     VAL A    21
REMARK 465     LYS A    22
REMARK 465     ALA A    23
REMARK 465     GLU A    24
REMARK 465     PRO A    25
REMARK 465     ALA A    26
REMARK 465     HIS A    27
REMARK 465     THR A    28
REMARK 465     ALA A    29
REMARK 465     ALA A    30
REMARK 465     SER A    31
REMARK 465     VAL A    32
REMARK 465     ALA A    33
REMARK 465     ALA A    34
REMARK 465     LYS A    35
REMARK 465     ASN A    36
REMARK 465     LEU A    37
REMARK 465     ALA A    38
REMARK 465     LEU A    39
REMARK 465     LEU A    40
REMARK 465     LYS A    41
REMARK 465     ALA A    42
REMARK 465     ARG A    43
REMARK 465     SER A    44
REMARK 465     PHE A    45
REMARK 465     PHE A   401
REMARK 465     GLN A   402
REMARK 465     PRO A   403
REMARK 465     SER A   404
REMARK 465     LEU A   405
REMARK 465     GLN A   406
REMARK 465     PRO A   407
REMARK 465     VAL A   408
REMARK 465     ALA A   409
REMARK 465     SER A   410
REMARK 465     GLU A   411
REMARK 465     PRO A   412
REMARK 465     GLY A   413
REMARK 465     CYS A   414
REMARK 465     PRO A   415
REMARK 465     ASP A   416
REMARK 465     VAL A   417
REMARK 465     GLU A   418
REMARK 465     MET A   419
REMARK 465     PRO A   420
REMARK 465     SER A   421
REMARK 465     PRO A   422
REMARK 465     TRP A   423
REMARK 465     ALA A   424
REMARK 465     PRO A   425
REMARK 465     SER A   426
REMARK 465     GLY A   427
REMARK 465     ASP A   428
REMARK 465     CYS A   429
REMARK 465     ALA A   430
REMARK 465     MET A   431
REMARK 465     SER A   432
REMARK 465     GLY A   433
REMARK 465     ARG A   434
REMARK 465     HIS A   435
REMARK 465     HIS A   436
REMARK 465     HIS A   437
REMARK 465     HIS A   438
REMARK 465     HIS A   439
REMARK 465     HIS A   440
REMARK 465     GLY D    -1
REMARK 465     SER D     0
REMARK 465     MET D     1
REMARK 465     ALA D     2
REMARK 465     GLU D     3
REMARK 465     PRO D     4
REMARK 465     LEU D     5
REMARK 465     LYS D     6
REMARK 465     GLU D     7
REMARK 465     GLU D     8
REMARK 465     ASP D     9
REMARK 465     GLY D    10
REMARK 465     GLU D    11
REMARK 465     ASP D    12
REMARK 465     GLY D    13
REMARK 465     SER D    14
REMARK 465     ALA D    15
REMARK 465     GLU D    16
REMARK 465     PRO D    17
REMARK 465     PRO D    18
REMARK 465     GLY D    19
REMARK 465     PRO D    20
REMARK 465     VAL D    21
REMARK 465     LYS D    22
REMARK 465     ALA D    23
REMARK 465     GLU D    24
REMARK 465     PRO D    25
REMARK 465     ALA D    26
REMARK 465     HIS D    27
REMARK 465     THR D    28
REMARK 465     ALA D    29
REMARK 465     ALA D    30
REMARK 465     SER D    31
REMARK 465     VAL D    32
REMARK 465     ALA D    33
REMARK 465     ALA D    34
REMARK 465     LYS D    35
REMARK 465     ASN D    36
REMARK 465     LEU D    37
REMARK 465     ALA D    38
REMARK 465     LEU D    39
REMARK 465     LEU D    40
REMARK 465     LYS D    41
REMARK 465     ALA D    42
REMARK 465     ARG D    43
REMARK 465     SER D    44
REMARK 465     PHE D    45
REMARK 465     ASP D    46
REMARK 465     ARG D   400
REMARK 465     PHE D   401
REMARK 465     GLN D   402
REMARK 465     PRO D   403
REMARK 465     SER D   404
REMARK 465     LEU D   405
REMARK 465     GLN D   406
REMARK 465     PRO D   407
REMARK 465     VAL D   408
REMARK 465     ALA D   409
REMARK 465     SER D   410
REMARK 465     GLU D   411
REMARK 465     PRO D   412
REMARK 465     GLY D   413
REMARK 465     CYS D   414
REMARK 465     PRO D   415
REMARK 465     ASP D   416
REMARK 465     VAL D   417
REMARK 465     GLU D   418
REMARK 465     MET D   419
REMARK 465     PRO D   420
REMARK 465     SER D   421
REMARK 465     PRO D   422
REMARK 465     TRP D   423
REMARK 465     ALA D   424
REMARK 465     PRO D   425
REMARK 465     SER D   426
REMARK 465     GLY D   427
REMARK 465     ASP D   428
REMARK 465     CYS D   429
REMARK 465     ALA D   430
REMARK 465     MET D   431
REMARK 465     SER D   432
REMARK 465     GLY D   433
REMARK 465     ARG D   434
REMARK 465     HIS D   435
REMARK 465     HIS D   436
REMARK 465     HIS D   437
REMARK 465     HIS D   438
REMARK 465     HIS D   439
REMARK 465     HIS D   440
REMARK 465     ARG E   125
REMARK 465     ALA E   126
REMARK 465     GLY E   127
REMARK 465     PRO E   128
REMARK 465     SER E   129
REMARK 465     GLN E   130
REMARK 465     SER E   131
REMARK 465     GLY E   132
REMARK 465     ARG E   133
REMARK 465     HIS E   134
REMARK 465     HIS E   135
REMARK 465     HIS E   136
REMARK 465     HIS E   137
REMARK 465     HIS E   138
REMARK 465     HIS E   139
REMARK 465     GLY B    14
REMARK 465     SER B    15
REMARK 465     HIS B   139
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     GLU A  56    CG   CD   OE1  OE2
REMARK 470     LYS A 110    CG   CD   CE   NZ
REMARK 470     ARG A 122    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL A 125    CG1  CG2
REMARK 470     GLU A 129    CG   CD   OE1  OE2
REMARK 470     LYS A 131    CG   CD   CE   NZ
REMARK 470     LEU A 207    CG   CD1  CD2
REMARK 470     THR A 209    OG1  CG2
REMARK 470     SER A 210    OG
REMARK 470     GLN A 215    CG   CD   OE1  NE2
REMARK 470     TYR A 216    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     VAL A 222    CG1  CG2
REMARK 470     ILE A 286    CG1  CG2  CD1
REMARK 470     GLN A 287    CG   CD   OE1  NE2
REMARK 470     GLU A 292    CG   CD   OE1  OE2
REMARK 470     ILE A 298    CG1  CG2  CD1
REMARK 470     LEU A 301    CG   CD1  CD2
REMARK 470     ARG A 304    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 369    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 370    CG   CD   OE1  OE2
REMARK 470     ARG A 376    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 396    NE   CZ   NH1  NH2
REMARK 470     ARG A 400    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL D  47    CG1  CG2
REMARK 470     PHE D  49    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU D  54    CG   CD   OE1  OE2
REMARK 470     GLU D  56    CG   CD   OE1  OE2
REMARK 470     ARG D  73    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D  74    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D  75    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU D  76    CG   CD1  CD2
REMARK 470     LYS D  85    CG   CD   CE   NZ
REMARK 470     ASP D  91    CG   OD1  OD2
REMARK 470     VAL D  93    CG1  CG2
REMARK 470     LYS D 104    CG   CD   CE   NZ
REMARK 470     LYS D 110    CG   CD   CE   NZ
REMARK 470     THR D 124    OG1  CG2
REMARK 470     VAL D 125    CG1  CG2
REMARK 470     TYR D 127    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU D 129    CG   CD   OE1  OE2
REMARK 470     PHE D 130    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS D 131    CG   CD   CE   NZ
REMARK 470     ARG D 205    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU D 207    CG   CD1  CD2
REMARK 470     THR D 209    OG1  CG2
REMARK 470     GLU D 213    CG   CD   OE1  OE2
REMARK 470     GLN D 215    CG   CD   OE1  NE2
REMARK 470     TYR D 216    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     VAL D 222    CG1  CG2
REMARK 470     SER D 235    OG
REMARK 470     GLN D 287    CG   CD   OE1  NE2
REMARK 470     GLU D 292    CG   CD   OE1  OE2
REMARK 470     ARG D 293    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP D 364    CG   OD1  OD2
REMARK 470     ARG D 369    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 370    CG   CD   OE1  OE2
REMARK 470     LEU D 372    CG   CD1  CD2
REMARK 470     THR D 373    OG1  CG2
REMARK 470     ARG D 374    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 375    CG   CD   OE1  OE2
REMARK 470     ARG D 376    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 379    CG   CD   OE1  OE2
REMARK 470     ARG D 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN D 398    CG   CD   OE1  NE2
REMARK 470     ILE D 399    CG1  CG2  CD1
REMARK 470     SER E  15    OG
REMARK 470     LYS E  22    CG   CD   CE   NZ
REMARK 470     SER E  35    OG
REMARK 470     LYS E  79    CG   CD   CE   NZ
REMARK 470     ASN E 123    CG   OD1  ND2
REMARK 470     THR E 124    OG1  CG2
REMARK 470     LYS B  22    CG   CD   CE   NZ
REMARK 470     SER B  35    OG
REMARK 470     GLN B  38    CG   CD   OE1  NE2
REMARK 470     GLU B  54    CG   CD   OE1  OE2
REMARK 470     LYS B  79    CG   CD   CE   NZ
REMARK 470     ASN B 123    CG   OD1  ND2
REMARK 470     SER B 129    OG
REMARK 470     ARG B 133    CG   CD   NE   CZ   NH1  NH2
REMARK 470     HIS B 136    CG   ND1  CD2  CE1  NE2
REMARK 470     HIS B 138    CG   ND1  CD2  CE1  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   O    THR A    48     NZ   LYS A    85              1.99
REMARK 500   O    ALA D    65     O2B  ANP D   501              2.02
REMARK 500   O    HOH A   614     O    HOH B   201              2.09
REMARK 500   OD2  ASP A   355     O    HOH A   612              2.12
REMARK 500   NH2  ARG A   391     OD2  ASP B    46              2.16
REMARK 500   OH   TYR A   350     O    HOH A   605              2.18
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    LEU A 196   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    PRO A 361   C   -  N   -  CA  ANGL. DEV. = -11.1 DEGREES
REMARK 500    PRO D  87   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES
REMARK 500    LEU D 196   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES
REMARK 500    PRO D 361   C   -  N   -  CA  ANGL. DEV. = -11.3 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  53      -20.85     77.27
REMARK 500    GLU A  59     -150.77     48.37
REMARK 500    TYR A  66       16.88     54.78
REMARK 500    LYS A 131      -63.47   -122.66
REMARK 500    ARG A 181      -19.07     75.06
REMARK 500    ASP A 200       71.09     61.60
REMARK 500    LEU A 207     -133.74     65.36
REMARK 500    THR A 209     -158.32    -77.44
REMARK 500    SER A 210      178.28    -58.50
REMARK 500    GLN A 215      -99.41     58.61
REMARK 500    TYR A 216       -4.91    -51.52
REMARK 500    TYR A 221     -166.90     54.81
REMARK 500    VAL A 222      152.54    163.57
REMARK 500    GLU A 292      -22.59     90.42
REMARK 500    TYR A 297      -19.30     82.31
REMARK 500    LEU A 301      148.68     69.00
REMARK 500    GLU A 356       70.59   -118.25
REMARK 500    PHE A 367       -0.25     94.47
REMARK 500    ALA A 371      -78.88   -106.43
REMARK 500    LEU A 372       82.53     42.28
REMARK 500    ILE A 385      -27.37     72.29
REMARK 500    GLU A 393       46.81     70.29
REMARK 500    GLU D  54       -3.42     84.94
REMARK 500    GLU D  56      160.01    177.51
REMARK 500    ILE D  61     -169.78   -113.80
REMARK 500    TYR D  66     -124.20     61.85
REMARK 500    ARG D  75      -75.23    -62.96
REMARK 500    ASN D  88       70.80     62.56
REMARK 500    LYS D  97     -160.63    -78.82
REMARK 500    ARG D  98      -98.67     61.80
REMARK 500    THR D 124      -79.37   -123.17
REMARK 500    LYS D 131      -64.62   -125.04
REMARK 500    ARG D 181      -19.96     75.02
REMARK 500    ASP D 200       75.91     56.73
REMARK 500    LEU D 207      -73.55   -133.80
REMARK 500    THR D 209     -119.16     70.40
REMARK 500    GLN D 215      -25.48     63.34
REMARK 500    TYR D 221       76.03     46.50
REMARK 500    HIS D 237      -17.21     77.13
REMARK 500    GLU D 292     -108.11     57.37
REMARK 500    TYR D 297      -59.73   -143.44
REMARK 500    GLU D 356       72.04   -118.52
REMARK 500    ALA D 360      -70.21    -59.76
REMARK 500    ASP D 364      -71.54    -73.69
REMARK 500    PHE D 365       -2.77     65.51
REMARK 500    PHE D 367      -81.66    -56.22
REMARK 500    ASP D 368     -112.78     30.46
REMARK 500    ALA D 371      -76.02    -56.99
REMARK 500    LEU D 372       -7.66     61.02
REMARK 500    ARG D 374     -139.69     50.92
REMARK 500
REMARK 500 THIS ENTRY HAS      76 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 VAL A   51     GLY A   52                 -143.94
REMARK 500 GLU A  292     ARG A  293                  -32.29
REMARK 500 ALA A  366     PHE A  367                 -144.02
REMARK 500 GLU D  292     ARG D  293                   41.20
REMARK 500 PHE D  367     ASP D  368                  145.02
REMARK 500 ARG D  392     GLU D  393                   32.53
REMARK 500 ILE E  117     HIS E  118                 -148.14
REMARK 500 ILE B  117     HIS B  118                 -144.39
REMARK 500 ALA B  126     GLY B  127                   38.10
REMARK 500 GLN B  130     SER B  131                  138.54
REMARK 500 HIS B  136     HIS B  137                  132.28
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    ARG B 115         0.29    SIDE CHAIN
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    GLU A 292        23.0      L          L   OUTSIDE RANGE
REMARK 500    GLU A 393        25.0      L          L   OUTSIDE RANGE
REMARK 500    GLU D 292        15.2      L          L   OUTSIDE RANGE
REMARK 500    ASP D 368        20.6      L          L   OUTSIDE RANGE
REMARK 500    GLU D 393        23.4      L          L   OUTSIDE RANGE
REMARK 500    ILE E 117        23.9      L          L   OUTSIDE RANGE
REMARK 500    ILE B 117        24.5      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP D 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IC8   RELATED DB: PDB
DBREF  4IC7 A    1   431  UNP    Q13164   MK07_HUMAN       1    431
DBREF  4IC7 D    1   431  UNP    Q13164   MK07_HUMAN       1    431
DBREF  4IC7 E   16   130  UNP    Q13163   MP2K5_HUMAN     16    130
DBREF  4IC7 B   16   130  UNP    Q13163   MP2K5_HUMAN     16    130
SEQADV 4IC7 GLY A   -1  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 SER A    0  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 SER A  432  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 GLY A  433  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 ARG A  434  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS A  435  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS A  436  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS A  437  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS A  438  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS A  439  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS A  440  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 GLY D   -1  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 SER D    0  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 SER D  432  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 GLY D  433  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 ARG D  434  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS D  435  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS D  436  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS D  437  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS D  438  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS D  439  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 HIS D  440  UNP  Q13164              EXPRESSION TAG
SEQADV 4IC7 GLY E   14  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 SER E   15  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 SER E  131  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 GLY E  132  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 ARG E  133  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS E  134  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS E  135  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS E  136  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS E  137  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS E  138  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS E  139  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 GLY B   14  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 SER B   15  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 SER B  131  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 GLY B  132  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 ARG B  133  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS B  134  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS B  135  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS B  136  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS B  137  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS B  138  UNP  Q13163              EXPRESSION TAG
SEQADV 4IC7 HIS B  139  UNP  Q13163              EXPRESSION TAG
SEQRES   1 A  442  GLY SER MET ALA GLU PRO LEU LYS GLU GLU ASP GLY GLU
SEQRES   2 A  442  ASP GLY SER ALA GLU PRO PRO GLY PRO VAL LYS ALA GLU
SEQRES   3 A  442  PRO ALA HIS THR ALA ALA SER VAL ALA ALA LYS ASN LEU
SEQRES   4 A  442  ALA LEU LEU LYS ALA ARG SER PHE ASP VAL THR PHE ASP
SEQRES   5 A  442  VAL GLY ASP GLU TYR GLU ILE ILE GLU THR ILE GLY ASN
SEQRES   6 A  442  GLY ALA TYR GLY VAL VAL SER SER ALA ARG ARG ARG LEU
SEQRES   7 A  442  THR GLY GLN GLN VAL ALA ILE LYS LYS ILE PRO ASN ALA
SEQRES   8 A  442  PHE ASP VAL VAL THR ASN ALA LYS ARG THR LEU ARG GLU
SEQRES   9 A  442  LEU LYS ILE LEU LYS HIS PHE LYS HIS ASP ASN ILE ILE
SEQRES  10 A  442  ALA ILE LYS ASP ILE LEU ARG PRO THR VAL PRO TYR GLY
SEQRES  11 A  442  GLU PHE LYS SER VAL TYR VAL VAL LEU ASP LEU MET GLU
SEQRES  12 A  442  SER ASP LEU HIS GLN ILE ILE HIS SER SER GLN PRO LEU
SEQRES  13 A  442  THR LEU GLU HIS VAL ARG TYR PHE LEU TYR GLN LEU LEU
SEQRES  14 A  442  ARG GLY LEU LYS TYR MET HIS SER ALA GLN VAL ILE HIS
SEQRES  15 A  442  ARG ASP LEU LYS PRO SER ASN LEU LEU VAL ASN GLU ASN
SEQRES  16 A  442  CYS GLU LEU LYS ILE GLY ASP PHE GLY MET ALA ARG GLY
SEQRES  17 A  442  LEU CYS THR SER PRO ALA GLU HIS GLN TYR PHE MET THR
SEQRES  18 A  442  GLU TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU LEU
SEQRES  19 A  442  MET LEU SER LEU HIS GLU TYR THR GLN ALA ILE ASP LEU
SEQRES  20 A  442  TRP SER VAL GLY CYS ILE PHE GLY GLU MET LEU ALA ARG
SEQRES  21 A  442  ARG GLN LEU PHE PRO GLY LYS ASN TYR VAL HIS GLN LEU
SEQRES  22 A  442  GLN LEU ILE MET MET VAL LEU GLY THR PRO SER PRO ALA
SEQRES  23 A  442  VAL ILE GLN ALA VAL GLY ALA GLU ARG VAL ARG ALA TYR
SEQRES  24 A  442  ILE GLN SER LEU PRO PRO ARG GLN PRO VAL PRO TRP GLU
SEQRES  25 A  442  THR VAL TYR PRO GLY ALA ASP ARG GLN ALA LEU SER LEU
SEQRES  26 A  442  LEU GLY ARG MET LEU ARG PHE GLU PRO SER ALA ARG ILE
SEQRES  27 A  442  SER ALA ALA ALA ALA LEU ARG HIS PRO PHE LEU ALA LYS
SEQRES  28 A  442  TYR HIS ASP PRO ASP ASP GLU PRO ASP CYS ALA PRO PRO
SEQRES  29 A  442  PHE ASP PHE ALA PHE ASP ARG GLU ALA LEU THR ARG GLU
SEQRES  30 A  442  ARG ILE LYS GLU ALA ILE VAL ALA GLU ILE GLU ASP PHE
SEQRES  31 A  442  HIS ALA ARG ARG GLU GLY ILE ARG GLN GLN ILE ARG PHE
SEQRES  32 A  442  GLN PRO SER LEU GLN PRO VAL ALA SER GLU PRO GLY CYS
SEQRES  33 A  442  PRO ASP VAL GLU MET PRO SER PRO TRP ALA PRO SER GLY
SEQRES  34 A  442  ASP CYS ALA MET SER GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES   1 D  442  GLY SER MET ALA GLU PRO LEU LYS GLU GLU ASP GLY GLU
SEQRES   2 D  442  ASP GLY SER ALA GLU PRO PRO GLY PRO VAL LYS ALA GLU
SEQRES   3 D  442  PRO ALA HIS THR ALA ALA SER VAL ALA ALA LYS ASN LEU
SEQRES   4 D  442  ALA LEU LEU LYS ALA ARG SER PHE ASP VAL THR PHE ASP
SEQRES   5 D  442  VAL GLY ASP GLU TYR GLU ILE ILE GLU THR ILE GLY ASN
SEQRES   6 D  442  GLY ALA TYR GLY VAL VAL SER SER ALA ARG ARG ARG LEU
SEQRES   7 D  442  THR GLY GLN GLN VAL ALA ILE LYS LYS ILE PRO ASN ALA
SEQRES   8 D  442  PHE ASP VAL VAL THR ASN ALA LYS ARG THR LEU ARG GLU
SEQRES   9 D  442  LEU LYS ILE LEU LYS HIS PHE LYS HIS ASP ASN ILE ILE
SEQRES  10 D  442  ALA ILE LYS ASP ILE LEU ARG PRO THR VAL PRO TYR GLY
SEQRES  11 D  442  GLU PHE LYS SER VAL TYR VAL VAL LEU ASP LEU MET GLU
SEQRES  12 D  442  SER ASP LEU HIS GLN ILE ILE HIS SER SER GLN PRO LEU
SEQRES  13 D  442  THR LEU GLU HIS VAL ARG TYR PHE LEU TYR GLN LEU LEU
SEQRES  14 D  442  ARG GLY LEU LYS TYR MET HIS SER ALA GLN VAL ILE HIS
SEQRES  15 D  442  ARG ASP LEU LYS PRO SER ASN LEU LEU VAL ASN GLU ASN
SEQRES  16 D  442  CYS GLU LEU LYS ILE GLY ASP PHE GLY MET ALA ARG GLY
SEQRES  17 D  442  LEU CYS THR SER PRO ALA GLU HIS GLN TYR PHE MET THR
SEQRES  18 D  442  GLU TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU LEU
SEQRES  19 D  442  MET LEU SER LEU HIS GLU TYR THR GLN ALA ILE ASP LEU
SEQRES  20 D  442  TRP SER VAL GLY CYS ILE PHE GLY GLU MET LEU ALA ARG
SEQRES  21 D  442  ARG GLN LEU PHE PRO GLY LYS ASN TYR VAL HIS GLN LEU
SEQRES  22 D  442  GLN LEU ILE MET MET VAL LEU GLY THR PRO SER PRO ALA
SEQRES  23 D  442  VAL ILE GLN ALA VAL GLY ALA GLU ARG VAL ARG ALA TYR
SEQRES  24 D  442  ILE GLN SER LEU PRO PRO ARG GLN PRO VAL PRO TRP GLU
SEQRES  25 D  442  THR VAL TYR PRO GLY ALA ASP ARG GLN ALA LEU SER LEU
SEQRES  26 D  442  LEU GLY ARG MET LEU ARG PHE GLU PRO SER ALA ARG ILE
SEQRES  27 D  442  SER ALA ALA ALA ALA LEU ARG HIS PRO PHE LEU ALA LYS
SEQRES  28 D  442  TYR HIS ASP PRO ASP ASP GLU PRO ASP CYS ALA PRO PRO
SEQRES  29 D  442  PHE ASP PHE ALA PHE ASP ARG GLU ALA LEU THR ARG GLU
SEQRES  30 D  442  ARG ILE LYS GLU ALA ILE VAL ALA GLU ILE GLU ASP PHE
SEQRES  31 D  442  HIS ALA ARG ARG GLU GLY ILE ARG GLN GLN ILE ARG PHE
SEQRES  32 D  442  GLN PRO SER LEU GLN PRO VAL ALA SER GLU PRO GLY CYS
SEQRES  33 D  442  PRO ASP VAL GLU MET PRO SER PRO TRP ALA PRO SER GLY
SEQRES  34 D  442  ASP CYS ALA MET SER GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES   1 E  126  GLY SER VAL LEU VAL ILE ARG ILE LYS ILE PRO ASN SER
SEQRES   2 E  126  GLY ALA VAL ASP TRP THR VAL HIS SER GLY PRO GLN LEU
SEQRES   3 E  126  LEU PHE ARG ASP VAL LEU ASP VAL ILE GLY GLN VAL LEU
SEQRES   4 E  126  PRO GLU ALA THR THR THR ALA PHE GLU TYR GLU ASP GLU
SEQRES   5 E  126  ASP GLY ASP ARG ILE THR VAL ARG SER ASP GLU GLU MET
SEQRES   6 E  126  LYS ALA MET LEU SER TYR TYR TYR SER THR VAL MET GLU
SEQRES   7 E  126  GLN GLN VAL ASN GLY GLN LEU ILE GLU PRO LEU GLN ILE
SEQRES   8 E  126  PHE PRO ARG ALA CYS LYS PRO PRO GLY GLU ARG ASN ILE
SEQRES   9 E  126  HIS GLY LEU LYS VAL ASN THR ARG ALA GLY PRO SER GLN
SEQRES  10 E  126  SER GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES   1 B  126  GLY SER VAL LEU VAL ILE ARG ILE LYS ILE PRO ASN SER
SEQRES   2 B  126  GLY ALA VAL ASP TRP THR VAL HIS SER GLY PRO GLN LEU
SEQRES   3 B  126  LEU PHE ARG ASP VAL LEU ASP VAL ILE GLY GLN VAL LEU
SEQRES   4 B  126  PRO GLU ALA THR THR THR ALA PHE GLU TYR GLU ASP GLU
SEQRES   5 B  126  ASP GLY ASP ARG ILE THR VAL ARG SER ASP GLU GLU MET
SEQRES   6 B  126  LYS ALA MET LEU SER TYR TYR TYR SER THR VAL MET GLU
SEQRES   7 B  126  GLN GLN VAL ASN GLY GLN LEU ILE GLU PRO LEU GLN ILE
SEQRES   8 B  126  PHE PRO ARG ALA CYS LYS PRO PRO GLY GLU ARG ASN ILE
SEQRES   9 B  126  HIS GLY LEU LYS VAL ASN THR ARG ALA GLY PRO SER GLN
SEQRES  10 B  126  SER GLY ARG HIS HIS HIS HIS HIS HIS
HET    ANP  A 501      31
HET    ANP  D 501      31
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL   5  ANP    2(C10 H17 N6 O12 P3)
FORMUL   7  HOH   *83(H2 O)
HELIX    1   1 VAL A   92  PHE A  109  1                                  18
HELIX    2   2 LEU A  144  HIS A  149  1                                   6
HELIX    3   3 THR A  155  ALA A  176  1                                  22
HELIX    4   4 LYS A  184  SER A  186  5                                   3
HELIX    5   5 GLN A  215  THR A  219  5                                   5
HELIX    6   6 ALA A  229  SER A  235  1                                   7
HELIX    7   7 GLN A  241  ARG A  258  1                                  18
HELIX    8   8 ASN A  266  GLY A  279  1                                  14
HELIX    9   9 SER A  282  GLN A  287  1                                   6
HELIX   10  10 VAL A  294  GLN A  299  1                                   6
HELIX   11  11 PRO A  308  TYR A  313  1                                   6
HELIX   12  12 ASP A  317  LEU A  328  1                                  12
HELIX   13  13 GLU A  331  ARG A  335  5                                   5
HELIX   14  14 SER A  337  LEU A  342  1                                   6
HELIX   15  15 ARG A  343  ALA A  348  5                                   6
HELIX   16  16 ASP A  352  GLU A  356  5                                   5
HELIX   17  17 THR A  373  GLU A  384  1                                  12
HELIX   18  18 ILE A  385  ARG A  391  1                                   7
HELIX   19  19 VAL D   92  LYS D   97  1                                   6
HELIX   20  20 ARG D   98  PHE D  109  1                                  12
HELIX   21  21 LEU D  144  HIS D  149  1                                   6
HELIX   22  22 THR D  155  ALA D  176  1                                  22
HELIX   23  23 LYS D  184  SER D  186  5                                   3
HELIX   24  24 SER D  210  HIS D  214  5                                   5
HELIX   25  25 ALA D  229  LEU D  234  1                                   6
HELIX   26  26 GLN D  241  ARG D  258  1                                  18
HELIX   27  27 ASN D  266  LEU D  278  1                                  13
HELIX   28  28 SER D  282  ALA D  288  1                                   7
HELIX   29  29 VAL D  294  GLN D  299  1                                   6
HELIX   30  30 PRO D  308  TYR D  313  1                                   6
HELIX   31  31 ASP D  317  LEU D  328  1                                  12
HELIX   32  32 GLU D  331  ARG D  335  5                                   5
HELIX   33  33 SER D  337  LEU D  342  1                                   6
HELIX   34  34 HIS D  344  ALA D  348  5                                   5
HELIX   35  35 ASP D  352  GLU D  356  5                                   5
HELIX   36  36 PHE D  365  LEU D  372  1                                   8
HELIX   37  37 ARG D  376  GLU D  384  1                                   9
HELIX   38  38 ILE D  385  ARG D  392  1                                   8
HELIX   39  39 LEU E   40  LEU E   52  1                                  13
HELIX   40  40 GLU E   76  ASN E   95  1                                  20
HELIX   41  41 LEU B   40  LEU B   52  1                                  13
HELIX   42  42 GLU B   76  ASN B   95  1                                  20
SHEET    1   A 5 TYR A  55  ILE A  58  0
SHEET    2   A 5 VAL A  68  ARG A  74 -1  O  ARG A  73   N  GLU A  56
SHEET    3   A 5 GLN A  80  ILE A  86 -1  O  VAL A  81   N  ALA A  72
SHEET    4   A 5 VAL A 133  ASP A 138 -1  O  LEU A 137   N  ALA A  82
SHEET    5   A 5 ILE A 117  ILE A 120 -1  N  ASP A 119   O  VAL A 136
SHEET    1   B 3 SER A 142  ASP A 143  0
SHEET    2   B 3 LEU A 188  VAL A 190 -1  O  VAL A 190   N  SER A 142
SHEET    3   B 3 LEU A 196  ILE A 198 -1  O  LYS A 197   N  LEU A 189
SHEET    1   C 2 VAL A 178  ILE A 179  0
SHEET    2   C 2 ARG A 205  GLY A 206 -1  O  ARG A 205   N  ILE A 179
SHEET    1   D 6 ARG A 396  GLN A 398  0
SHEET    2   D 6 GLY B  27  THR B  32 -1  O  ASP B  30   N  GLN A 397
SHEET    3   D 6 VAL B  18  ILE B  23 -1  N  ILE B  19   O  TRP B  31
SHEET    4   D 6 LEU B 102  PRO B 106  1  O  ILE B 104   N  ARG B  20
SHEET    5   D 6 PHE B  60  GLU B  63 -1  N  GLU B  61   O  PHE B 105
SHEET    6   D 6 ARG B  69  VAL B  72 -1  O  ILE B  70   N  TYR B  62
SHEET    1   E 5 TYR D  55  ILE D  58  0
SHEET    2   E 5 VAL D  68  ARG D  74 -1  O  ARG D  73   N  GLU D  56
SHEET    3   E 5 GLN D  80  PRO D  87 -1  O  ILE D  83   N  SER D  70
SHEET    4   E 5 SER D 132  LEU D 137 -1  O  VAL D 133   N  ILE D  86
SHEET    5   E 5 ILE D 117  ILE D 120 -1  N  ASP D 119   O  VAL D 136
SHEET    1   F 3 SER D 142  ASP D 143  0
SHEET    2   F 3 LEU D 188  VAL D 190 -1  O  VAL D 190   N  SER D 142
SHEET    3   F 3 LEU D 196  ILE D 198 -1  O  LYS D 197   N  LEU D 189
SHEET    1   G 5 GLY E  27  VAL E  33  0
SHEET    2   G 5 LEU E  17  ILE E  23 -1  N  LEU E  17   O  VAL E  33
SHEET    3   G 5 LEU E 102  PRO E 106  1  O  LEU E 102   N  ARG E  20
SHEET    4   G 5 PHE E  60  GLU E  63 -1  N  GLU E  61   O  PHE E 105
SHEET    5   G 5 ARG E  69  VAL E  72 -1  O  VAL E  72   N  PHE E  60
CISPEP   1 VAL A  125    PRO A  126          0       -16.77
CISPEP   2 LEU A  207    CYS A  208          0        -2.04
CISPEP   3 ALA A  212    GLU A  213          0         7.40
CISPEP   4 THR A  219    GLU A  220          0        -2.57
CISPEP   5 ARG A  392    GLU A  393          0        10.37
CISPEP   6 GLU D   56    ILE D   57          0        -7.09
CISPEP   7 PRO D  123    THR D  124          0       -13.50
CISPEP   8 GLY D  128    GLU D  129          0        14.01
CISPEP   9 GLU D  129    PHE D  130          0        -2.67
CISPEP  10 LEU D  207    CYS D  208          0        -4.07
CISPEP  11 THR D  219    GLU D  220          0       -14.23
CISPEP  12 HIS E   34    SER E   35          0        -4.38
CISPEP  13 SER E   35    GLY E   36          0        -4.10
CISPEP  14 GLY E   36    PRO E   37          0         1.82
CISPEP  15 PRO E   37    GLN E   38          0        -9.23
CISPEP  16 PRO E  112    GLY E  113          0       -21.29
CISPEP  17 HIS B   34    SER B   35          0       -16.96
CISPEP  18 SER B   35    GLY B   36          0        17.57
CISPEP  19 GLY B   36    PRO B   37          0         5.26
CISPEP  20 PRO B   37    GLN B   38          0        -6.25
CISPEP  21 PRO B  112    GLY B  113          0        10.72
CISPEP  22 GLY B  132    ARG B  133          0        -3.84
SITE     1 AC1 13 GLY A  62  ALA A  65  TYR A  66  VAL A  69
SITE     2 AC1 13 ALA A  82  LYS A  84  ARG A  98  ILE A 115
SITE     3 AC1 13 ASP A 138  MET A 140  LEU A 189  ASP A 200
SITE     4 AC1 13 HOH A 629
SITE     1 AC2 14 GLY D  62  GLY D  64  ALA D  65  TYR D  66
SITE     2 AC2 14 GLY D  67  VAL D  69  ALA D  82  LYS D  84
SITE     3 AC2 14 ARG D  98  LEU D 137  ASP D 138  MET D 140
SITE     4 AC2 14 LEU D 189  ASP D 200
CRYST1   69.370   69.370  271.240  90.00  90.00  90.00 P 43          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      0.014415  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014415  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003687        0.00000
      
PROCHECK
Go to PROCHECK summary
 References