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PDBsum entry 3gw6

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Top Page protein ligands metals Protein-protein interface(s) links
Chaperone PDB id
3gw6
Jmol
Contents
Protein chains
(+ 0 more) 256 a.a.
Ligands
PEG ×18
TAM ×3
Metals
_CL ×6
_BR ×6
_CA
Waters ×323
HEADER    CHAPERONE                               31-MAR-09   3GW6
TITLE     INTRAMOLECULAR CHAPERONE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ENDO-N-ACETYLNEURAMINIDASE;
COMPND   3 CHAIN: A, B, E, C, D, F;
COMPND   4 FRAGMENT: RESIDUES 790-1064;
COMPND   5 SYNONYM: ENDO-ALPHA-SIALIDASE, GP17 PROTEIN;
COMPND   6 EC: 3.2.1.129;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE K1F;
SOURCE   3 ORGANISM_COMMON: BACTERIOPHAGE K1F;
SOURCE   4 ORGANISM_TAXID: 344021;
SOURCE   5 GENE: SIA, 17, 17.0;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    CHAPERONE, GLYCOSIDASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.C.SCHULZ,A.DICKMANNS,R.FICNER
REVDAT   2   07-APR-10 3GW6    1       JRNL
REVDAT   1   02-FEB-10 3GW6    0
JRNL        AUTH   E.C.SCHULZ,A.DICKMANNS,H.URLAUB,A.SCHMITT,
JRNL        AUTH 2 M.MUHLENHOFF,K.STUMMEYER,D.SCHWARZER,
JRNL        AUTH 3 R.GERARDY-SCHAHN,R.FICNER
JRNL        TITL   CRYSTAL STRUCTURE OF AN INTRAMOLECULAR CHAPERONE
JRNL        TITL 2 MEDIATING TRIPLE-BETA-HELIX FOLDING.
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   210 2010
JRNL        REFN                   ISSN 1545-9993
JRNL        PMID   20118935
JRNL        DOI    10.1038/NSMB.1746
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
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) : 27.63
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4
REMARK   3   NUMBER OF REFLECTIONS             : 59958
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211
REMARK   3   R VALUE            (WORKING SET) : 0.209
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2998
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 27.6342 -  5.5876    0.94     5617   296  0.2189 0.2587
REMARK   3     2  5.5876 -  4.4410    0.94     5626   296  0.1574 0.2064
REMARK   3     3  4.4410 -  3.8814    0.96     5747   302  0.1697 0.2152
REMARK   3     4  3.8814 -  3.5273    0.96     5729   302  0.1975 0.2555
REMARK   3     5  3.5273 -  3.2749    0.96     5745   302  0.2147 0.2375
REMARK   3     6  3.2749 -  3.0821    0.96     5701   300  0.2238 0.2891
REMARK   3     7  3.0821 -  2.9279    0.96     5737   302  0.2314 0.2809
REMARK   3     8  2.9279 -  2.8006    0.96     5712   301  0.2423 0.2867
REMARK   3     9  2.8006 -  2.6929    0.95     5682   299  0.2624 0.3199
REMARK   3    10  2.6929 -  2.6000    0.95     5664   298  0.2970 0.3499
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              : 0.29
REMARK   3   B_SOL              : 40.74
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.100
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.600
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 53.48
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.85
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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      :  0.003          12558
REMARK   3   ANGLE     :  0.727          16957
REMARK   3   CHIRALITY :  0.052           1826
REMARK   3   PLANARITY :  0.002           2229
REMARK   3   DIHEDRAL  : 17.812           4522
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN F AND (RESID 825:835 OR RESID 913:933
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8366  -2.5310  13.2098
REMARK   3    T TENSOR
REMARK   3      T11:   0.6138 T22:   0.4045
REMARK   3      T33:   0.4722 T12:  -0.0458
REMARK   3      T13:   0.0819 T23:   0.0300
REMARK   3    L TENSOR
REMARK   3      L11:   0.1594 L22:  -0.1249
REMARK   3      L33:   0.2874 L12:   0.0396
REMARK   3      L13:  -0.1580 L23:  -0.2770
REMARK   3    S TENSOR
REMARK   3      S11:   0.0884 S12:  -0.0665 S13:  -0.1418
REMARK   3      S21:   0.1803 S22:  -0.2185 S23:  -0.2443
REMARK   3      S31:   0.2469 S32:   0.1139 S33:   0.1126
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 2
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain A and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     SELECTION          : chain B and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     ATOM PAIRS NUMBER  : 996
REMARK   3     RMSD               : 0.068
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain A and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     SELECTION          : chain F and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     ATOM PAIRS NUMBER  : 1008
REMARK   3     RMSD               : 0.073
REMARK   3   NCS GROUP : 2
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain C and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     SELECTION          : chain D and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     ATOM PAIRS NUMBER  : 976
REMARK   3     RMSD               : 0.088
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain C and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     SELECTION          : chain E and (name CA or name N or name
REMARK   3                          C or name O) and (resseq 800:1005 or
REMARK   3                          resseq 1011:1063)
REMARK   3     ATOM PAIRS NUMBER  : 1000
REMARK   3     RMSD               : 0.093
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3GW6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB052382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : X13
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 184838
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.04200
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) : 2.70
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.41100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % PEG 8000, 0.1 M BISTRIS PH
REMARK 280  6.0, 0.15 M CABR2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280  293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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 300 REMARK: ONE OF THE TWO TRIMERS IN THE ASYMMETRIC UNIT IS THE
REMARK 300 BIOLOGICALLY ACTIVE PROTEIN.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 37280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 37390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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     MET A   790
REMARK 465     GLU A   791
REMARK 465     PHE A   792
REMARK 465     THR A   793
REMARK 465     GLY A   794
REMARK 465     ASP A   795
REMARK 465     LEU A   796
REMARK 465     GLY A   797
REMARK 465     LEU A   798
REMARK 465     GLY A   799
REMARK 465     ALA A   805
REMARK 465     SER A   806
REMARK 465     THR A   807
REMARK 465     SER A   808
REMARK 465     SER A   809
REMARK 465     ASN A   810
REMARK 465     THR A   977
REMARK 465     ASN A   978
REMARK 465     LYS A  1064
REMARK 465     MET B   790
REMARK 465     GLU B   791
REMARK 465     PHE B   792
REMARK 465     THR B   793
REMARK 465     GLY B   794
REMARK 465     ASP B   795
REMARK 465     LEU B   796
REMARK 465     GLY B   797
REMARK 465     LEU B   798
REMARK 465     GLY B   799
REMARK 465     SER B   806
REMARK 465     THR B   807
REMARK 465     SER B   808
REMARK 465     SER B   809
REMARK 465     ASN B   810
REMARK 465     GLY B   948
REMARK 465     ASN B   949
REMARK 465     ASP B   950
REMARK 465     ASN B   975
REMARK 465     LYS B  1064
REMARK 465     MET E   790
REMARK 465     GLU E   791
REMARK 465     PHE E   792
REMARK 465     THR E   793
REMARK 465     GLY E   794
REMARK 465     ASP E   795
REMARK 465     LEU E   796
REMARK 465     GLY E   797
REMARK 465     LEU E   798
REMARK 465     GLY E   799
REMARK 465     HIS E   800
REMARK 465     SER E   806
REMARK 465     THR E   807
REMARK 465     SER E   808
REMARK 465     SER E   809
REMARK 465     ASN E   975
REMARK 465     SER E   976
REMARK 465     LYS E  1064
REMARK 465     MET C   790
REMARK 465     GLU C   791
REMARK 465     PHE C   792
REMARK 465     THR C   793
REMARK 465     GLY C   794
REMARK 465     ASP C   795
REMARK 465     LEU C   796
REMARK 465     GLY C   797
REMARK 465     LEU C   798
REMARK 465     GLY C   799
REMARK 465     SER C   806
REMARK 465     THR C   807
REMARK 465     SER C   808
REMARK 465     SER C   809
REMARK 465     ASN C   810
REMARK 465     GLY C   948
REMARK 465     ASN C   949
REMARK 465     ASP C   950
REMARK 465     ASP C   973
REMARK 465     GLU C   974
REMARK 465     LYS C  1064
REMARK 465     MET D   790
REMARK 465     GLU D   791
REMARK 465     PHE D   792
REMARK 465     THR D   793
REMARK 465     GLY D   794
REMARK 465     ASP D   795
REMARK 465     LEU D   796
REMARK 465     GLY D   797
REMARK 465     LEU D   798
REMARK 465     GLY D   799
REMARK 465     ALA D   805
REMARK 465     SER D   806
REMARK 465     THR D   807
REMARK 465     SER D   808
REMARK 465     SER D   809
REMARK 465     ASN D   810
REMARK 465     ASP D   973
REMARK 465     GLU D   974
REMARK 465     ASN D   975
REMARK 465     SER D   976
REMARK 465     THR D   977
REMARK 465     GLN D  1063
REMARK 465     LYS D  1064
REMARK 465     MET F   790
REMARK 465     GLU F   791
REMARK 465     PHE F   792
REMARK 465     THR F   793
REMARK 465     GLY F   794
REMARK 465     ASP F   795
REMARK 465     LEU F   796
REMARK 465     GLY F   797
REMARK 465     LEU F   798
REMARK 465     GLY F   799
REMARK 465     ALA F   805
REMARK 465     SER F   806
REMARK 465     THR F   807
REMARK 465     SER F   808
REMARK 465     SER F   809
REMARK 465     ASN F   810
REMARK 465     ASN F   975
REMARK 465     LYS F  1064
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     HIS A  800   CG   CE1
REMARK 480     ARG A  812   CZ
REMARK 480     ASP A  924   CG
REMARK 480     ASP A  973   C    CG
REMARK 480     GLU A  974   CD
REMARK 480     CYS A  979   CB
REMARK 480     ARG A  980   CZ
REMARK 480     ARG A  991   NH2
REMARK 480     GLU A 1009   O
REMARK 480     GLU A 1017   CD
REMARK 480     GLU A 1022   CD
REMARK 480     GLU A 1028   CD
REMARK 480     GLU A 1052   CD
REMARK 480     LEU A 1058   C
REMARK 480     HIS B  800   CG
REMARK 480     ARG B  915   CZ
REMARK 480     ASP B  923   CG
REMARK 480     ASP B  928   CG
REMARK 480     ARG B  963   CZ
REMARK 480     ASP B  964   CG
REMARK 480     ALA B  968   C
REMARK 480     MET B  972   C
REMARK 480     GLU B  974   CG   CD
REMARK 480     ASN B  978   CG
REMARK 480     ARG B  980   CZ
REMARK 480     GLU B 1008   CB   CD
REMARK 480     GLU B 1009   CD
REMARK 480     VAL B 1012   CA
REMARK 480     THR B 1015   OG1
REMARK 480     GLU B 1016   O
REMARK 480     GLU B 1017   CD
REMARK 480     GLU B 1022   OE1
REMARK 480     GLU B 1028   CD
REMARK 480     GLN B 1047   OE1
REMARK 480     LEU B 1058   C
REMARK 480     GLU B 1062   C
REMARK 480     ALA E  911   C
REMARK 480     ARG E  915   NE   CZ
REMARK 480     GLU E  918   CD
REMARK 480     VAL E  920   O
REMARK 480     ASP E  928   CG
REMARK 480     ARG E  963   CZ
REMARK 480     ILE E  967   C    CB   CD1
REMARK 480     ASP E  973   CG
REMARK 480     ASN E  978   CG
REMARK 480     ARG E  980   CZ
REMARK 480     GLU E 1001   CA
REMARK 480     GLU E 1004   CA
REMARK 480     GLU E 1009   OE1
REMARK 480     THR E 1015   CG2
REMARK 480     GLU E 1016   CD
REMARK 480     GLU E 1017   CD
REMARK 480     GLU E 1022   CD
REMARK 480     ARG E 1049   CZ
REMARK 480     GLU E 1052   CD
REMARK 480     ILE E 1054   CG1  CD1
REMARK 480     ALA E 1056   CB
REMARK 480     GLU E 1062   C
REMARK 480     GLN E 1063   CD
REMARK 480     ASN C  978   CG
REMARK 480     GLU C 1017   CD
REMARK 480     GLU C 1022   CD
REMARK 480     ILE C 1054   CB
REMARK 480     GLU C 1055   CD
REMARK 480     ARG C 1057   CD
REMARK 480     LEU C 1061   C    O
REMARK 480     GLU C 1062   C    CD
REMARK 480     GLN C 1063   C
REMARK 480     ARG D  812   CZ
REMARK 480     ASP D  831   OD2
REMARK 480     LEU D  941   CD1
REMARK 480     ASP D  942   CG
REMARK 480     GLN D  945   CA
REMARK 480     ASN D  949   CG
REMARK 480     ARG D  952   CZ
REMARK 480     GLN D  960   C    CD
REMARK 480     ARG D  963   C    CZ
REMARK 480     PHE D  966   C
REMARK 480     ILE D  967   C
REMARK 480     HIS D  969   CE1
REMARK 480     MET D  972   CB
REMARK 480     CYS D  979   CB
REMARK 480     ARG D  980   CD   CZ
REMARK 480     LYS D  988   CG   CE
REMARK 480     ILE D 1002   CA
REMARK 480     HIS D 1005   C
REMARK 480     GLY D 1010   CA   C
REMARK 480     GLU D 1028   CD
REMARK 480     TRP D 1032   CE2  CH2
REMARK 480     GLN D 1047   CD
REMARK 480     GLU D 1052   C    CD
REMARK 480     GLU D 1055   C    CB
REMARK 480     ALA D 1056   C
REMARK 480     GLU D 1062   CD
REMARK 480     HIS F  800   ND1
REMARK 480     ARG F  915   CZ
REMARK 480     ASP F  942   CG
REMARK 480     VAL F  944   CA
REMARK 480     GLN F  945   CD
REMARK 480     LEU F  946   O    CD2
REMARK 480     LYS F  947   CE
REMARK 480     ASN F  949   CG
REMARK 480     ASP F  950   C
REMARK 480     ARG F  952   CD
REMARK 480     GLN F  961   CG
REMARK 480     ARG F  963   CZ
REMARK 480     GLU F  974   CD
REMARK 480     SER F  976   O
REMARK 480     HIS F 1005   C
REMARK 480     THR F 1014   C
REMARK 480     THR F 1015   OG1
REMARK 480     GLU F 1016   CD
REMARK 480     GLU F 1030   CD
REMARK 480     TRP F 1032   NE1
REMARK 480     GLU F 1052   OE1
REMARK 480     GLU F 1062   C    CD
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    SER A 878       -7.10     80.72
REMARK 500    ASN A 912       48.25     38.02
REMARK 500    THR A 917     -176.49    -65.28
REMARK 500    GLU A 974        2.29    -59.70
REMARK 500    ASN A 975     -161.84    -66.39
REMARK 500    ALA A1060       34.91    -80.50
REMARK 500    ARG B 837      157.20    178.13
REMARK 500    SER B 878       -1.34     83.22
REMARK 500    GLU B1028      157.98    -49.67
REMARK 500    SER E 878        0.00     81.31
REMARK 500    HIS E 999     -176.19   -172.50
REMARK 500    LEU E1061       26.60    -79.40
REMARK 500    ASP C 863       76.58   -100.89
REMARK 500    SER C 878       -8.08     74.47
REMARK 500    ASN C 896       55.21   -142.37
REMARK 500    THR C 900     -177.30   -174.46
REMARK 500    ARG D 837      149.70    177.59
REMARK 500    SER D 878        4.15     83.14
REMARK 500    ASN F 832       73.50   -119.30
REMARK 500    ASN F 912       50.81     36.19
REMARK 500    ASN F 949        1.88    -68.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C SSEQI
REMARK 615     TAM A   32
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 35
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 40
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 38
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 39
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 16
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 33
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR E 36
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 42
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM C 28
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 29
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 41
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG F 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG F 24
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG F 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG F 34
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR F 37
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GUD   RELATED DB: PDB
DBREF  3GW6 A  790  1064  UNP    Q858B1   Q858B1_BPK1F   790   1064
DBREF  3GW6 B  790  1064  UNP    Q858B1   Q858B1_BPK1F   790   1064
DBREF  3GW6 E  790  1064  UNP    Q858B1   Q858B1_BPK1F   790   1064
DBREF  3GW6 C  790  1064  UNP    Q858B1   Q858B1_BPK1F   790   1064
DBREF  3GW6 D  790  1064  UNP    Q858B1   Q858B1_BPK1F   790   1064
DBREF  3GW6 F  790  1064  UNP    Q858B1   Q858B1_BPK1F   790   1064
SEQADV 3GW6 ALA A  911  UNP  Q858B1    SER   911 CONFLICT
SEQADV 3GW6 ALA B  911  UNP  Q858B1    SER   911 CONFLICT
SEQADV 3GW6 ALA E  911  UNP  Q858B1    SER   911 CONFLICT
SEQADV 3GW6 ALA C  911  UNP  Q858B1    SER   911 CONFLICT
SEQADV 3GW6 ALA D  911  UNP  Q858B1    SER   911 CONFLICT
SEQADV 3GW6 ALA F  911  UNP  Q858B1    SER   911 CONFLICT
SEQRES   1 A  275  MET GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR
SEQRES   2 A  275  ILE ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL
SEQRES   3 A  275  LEU MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE
SEQRES   4 A  275  PRO THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS
SEQRES   5 A  275  GLY GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE
SEQRES   6 A  275  THR LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE
SEQRES   7 A  275  VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP
SEQRES   8 A  275  VAL LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY
SEQRES   9 A  275  PRO SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN
SEQRES  10 A  275  PRO ILE VAL THR ALA ASN GLY GLU ARG LYS THR GLU PRO
SEQRES  11 A  275  VAL VAL PHE ASP ASP ALA PHE LEU ASP ALA TRP GLY ASP
SEQRES  12 A  275  VAL HIS TYR ILE MET TYR GLN TRP LEU ASP ALA VAL GLN
SEQRES  13 A  275  LEU LYS GLY ASN ASP ALA ARG ILE HIS PHE GLY VAL ILE
SEQRES  14 A  275  ALA GLN GLN ILE ARG ASP VAL PHE ILE ALA HIS GLY LEU
SEQRES  15 A  275  MET ASP GLU ASN SER THR ASN CYS ARG TYR ALA VAL LEU
SEQRES  16 A  275  CYS TYR ASP LYS TYR PRO ARG MET THR ASP THR VAL PHE
SEQRES  17 A  275  SER HIS ASN GLU ILE VAL GLU HIS THR ASP GLU GLU GLY
SEQRES  18 A  275  ASN VAL THR THR THR GLU GLU PRO VAL TYR THR GLU VAL
SEQRES  19 A  275  VAL ILE HIS GLU GLU GLY GLU GLU TRP GLY VAL ARG PRO
SEQRES  20 A  275  ASP GLY ILE PHE PHE ALA GLU ALA ALA TYR GLN ARG ARG
SEQRES  21 A  275  LYS LEU GLU ARG ILE GLU ALA ARG LEU SER ALA LEU GLU
SEQRES  22 A  275  GLN LYS
SEQRES   1 B  275  MET GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR
SEQRES   2 B  275  ILE ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL
SEQRES   3 B  275  LEU MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE
SEQRES   4 B  275  PRO THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS
SEQRES   5 B  275  GLY GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE
SEQRES   6 B  275  THR LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE
SEQRES   7 B  275  VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP
SEQRES   8 B  275  VAL LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY
SEQRES   9 B  275  PRO SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN
SEQRES  10 B  275  PRO ILE VAL THR ALA ASN GLY GLU ARG LYS THR GLU PRO
SEQRES  11 B  275  VAL VAL PHE ASP ASP ALA PHE LEU ASP ALA TRP GLY ASP
SEQRES  12 B  275  VAL HIS TYR ILE MET TYR GLN TRP LEU ASP ALA VAL GLN
SEQRES  13 B  275  LEU LYS GLY ASN ASP ALA ARG ILE HIS PHE GLY VAL ILE
SEQRES  14 B  275  ALA GLN GLN ILE ARG ASP VAL PHE ILE ALA HIS GLY LEU
SEQRES  15 B  275  MET ASP GLU ASN SER THR ASN CYS ARG TYR ALA VAL LEU
SEQRES  16 B  275  CYS TYR ASP LYS TYR PRO ARG MET THR ASP THR VAL PHE
SEQRES  17 B  275  SER HIS ASN GLU ILE VAL GLU HIS THR ASP GLU GLU GLY
SEQRES  18 B  275  ASN VAL THR THR THR GLU GLU PRO VAL TYR THR GLU VAL
SEQRES  19 B  275  VAL ILE HIS GLU GLU GLY GLU GLU TRP GLY VAL ARG PRO
SEQRES  20 B  275  ASP GLY ILE PHE PHE ALA GLU ALA ALA TYR GLN ARG ARG
SEQRES  21 B  275  LYS LEU GLU ARG ILE GLU ALA ARG LEU SER ALA LEU GLU
SEQRES  22 B  275  GLN LYS
SEQRES   1 E  275  MET GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR
SEQRES   2 E  275  ILE ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL
SEQRES   3 E  275  LEU MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE
SEQRES   4 E  275  PRO THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS
SEQRES   5 E  275  GLY GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE
SEQRES   6 E  275  THR LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE
SEQRES   7 E  275  VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP
SEQRES   8 E  275  VAL LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY
SEQRES   9 E  275  PRO SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN
SEQRES  10 E  275  PRO ILE VAL THR ALA ASN GLY GLU ARG LYS THR GLU PRO
SEQRES  11 E  275  VAL VAL PHE ASP ASP ALA PHE LEU ASP ALA TRP GLY ASP
SEQRES  12 E  275  VAL HIS TYR ILE MET TYR GLN TRP LEU ASP ALA VAL GLN
SEQRES  13 E  275  LEU LYS GLY ASN ASP ALA ARG ILE HIS PHE GLY VAL ILE
SEQRES  14 E  275  ALA GLN GLN ILE ARG ASP VAL PHE ILE ALA HIS GLY LEU
SEQRES  15 E  275  MET ASP GLU ASN SER THR ASN CYS ARG TYR ALA VAL LEU
SEQRES  16 E  275  CYS TYR ASP LYS TYR PRO ARG MET THR ASP THR VAL PHE
SEQRES  17 E  275  SER HIS ASN GLU ILE VAL GLU HIS THR ASP GLU GLU GLY
SEQRES  18 E  275  ASN VAL THR THR THR GLU GLU PRO VAL TYR THR GLU VAL
SEQRES  19 E  275  VAL ILE HIS GLU GLU GLY GLU GLU TRP GLY VAL ARG PRO
SEQRES  20 E  275  ASP GLY ILE PHE PHE ALA GLU ALA ALA TYR GLN ARG ARG
SEQRES  21 E  275  LYS LEU GLU ARG ILE GLU ALA ARG LEU SER ALA LEU GLU
SEQRES  22 E  275  GLN LYS
SEQRES   1 C  275  MET GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR
SEQRES   2 C  275  ILE ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL
SEQRES   3 C  275  LEU MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE
SEQRES   4 C  275  PRO THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS
SEQRES   5 C  275  GLY GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE
SEQRES   6 C  275  THR LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE
SEQRES   7 C  275  VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP
SEQRES   8 C  275  VAL LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY
SEQRES   9 C  275  PRO SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN
SEQRES  10 C  275  PRO ILE VAL THR ALA ASN GLY GLU ARG LYS THR GLU PRO
SEQRES  11 C  275  VAL VAL PHE ASP ASP ALA PHE LEU ASP ALA TRP GLY ASP
SEQRES  12 C  275  VAL HIS TYR ILE MET TYR GLN TRP LEU ASP ALA VAL GLN
SEQRES  13 C  275  LEU LYS GLY ASN ASP ALA ARG ILE HIS PHE GLY VAL ILE
SEQRES  14 C  275  ALA GLN GLN ILE ARG ASP VAL PHE ILE ALA HIS GLY LEU
SEQRES  15 C  275  MET ASP GLU ASN SER THR ASN CYS ARG TYR ALA VAL LEU
SEQRES  16 C  275  CYS TYR ASP LYS TYR PRO ARG MET THR ASP THR VAL PHE
SEQRES  17 C  275  SER HIS ASN GLU ILE VAL GLU HIS THR ASP GLU GLU GLY
SEQRES  18 C  275  ASN VAL THR THR THR GLU GLU PRO VAL TYR THR GLU VAL
SEQRES  19 C  275  VAL ILE HIS GLU GLU GLY GLU GLU TRP GLY VAL ARG PRO
SEQRES  20 C  275  ASP GLY ILE PHE PHE ALA GLU ALA ALA TYR GLN ARG ARG
SEQRES  21 C  275  LYS LEU GLU ARG ILE GLU ALA ARG LEU SER ALA LEU GLU
SEQRES  22 C  275  GLN LYS
SEQRES   1 D  275  MET GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR
SEQRES   2 D  275  ILE ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL
SEQRES   3 D  275  LEU MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE
SEQRES   4 D  275  PRO THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS
SEQRES   5 D  275  GLY GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE
SEQRES   6 D  275  THR LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE
SEQRES   7 D  275  VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP
SEQRES   8 D  275  VAL LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY
SEQRES   9 D  275  PRO SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN
SEQRES  10 D  275  PRO ILE VAL THR ALA ASN GLY GLU ARG LYS THR GLU PRO
SEQRES  11 D  275  VAL VAL PHE ASP ASP ALA PHE LEU ASP ALA TRP GLY ASP
SEQRES  12 D  275  VAL HIS TYR ILE MET TYR GLN TRP LEU ASP ALA VAL GLN
SEQRES  13 D  275  LEU LYS GLY ASN ASP ALA ARG ILE HIS PHE GLY VAL ILE
SEQRES  14 D  275  ALA GLN GLN ILE ARG ASP VAL PHE ILE ALA HIS GLY LEU
SEQRES  15 D  275  MET ASP GLU ASN SER THR ASN CYS ARG TYR ALA VAL LEU
SEQRES  16 D  275  CYS TYR ASP LYS TYR PRO ARG MET THR ASP THR VAL PHE
SEQRES  17 D  275  SER HIS ASN GLU ILE VAL GLU HIS THR ASP GLU GLU GLY
SEQRES  18 D  275  ASN VAL THR THR THR GLU GLU PRO VAL TYR THR GLU VAL
SEQRES  19 D  275  VAL ILE HIS GLU GLU GLY GLU GLU TRP GLY VAL ARG PRO
SEQRES  20 D  275  ASP GLY ILE PHE PHE ALA GLU ALA ALA TYR GLN ARG ARG
SEQRES  21 D  275  LYS LEU GLU ARG ILE GLU ALA ARG LEU SER ALA LEU GLU
SEQRES  22 D  275  GLN LYS
SEQRES   1 F  275  MET GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR
SEQRES   2 F  275  ILE ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL
SEQRES   3 F  275  LEU MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE
SEQRES   4 F  275  PRO THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS
SEQRES   5 F  275  GLY GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE
SEQRES   6 F  275  THR LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE
SEQRES   7 F  275  VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP
SEQRES   8 F  275  VAL LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY
SEQRES   9 F  275  PRO SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN
SEQRES  10 F  275  PRO ILE VAL THR ALA ASN GLY GLU ARG LYS THR GLU PRO
SEQRES  11 F  275  VAL VAL PHE ASP ASP ALA PHE LEU ASP ALA TRP GLY ASP
SEQRES  12 F  275  VAL HIS TYR ILE MET TYR GLN TRP LEU ASP ALA VAL GLN
SEQRES  13 F  275  LEU LYS GLY ASN ASP ALA ARG ILE HIS PHE GLY VAL ILE
SEQRES  14 F  275  ALA GLN GLN ILE ARG ASP VAL PHE ILE ALA HIS GLY LEU
SEQRES  15 F  275  MET ASP GLU ASN SER THR ASN CYS ARG TYR ALA VAL LEU
SEQRES  16 F  275  CYS TYR ASP LYS TYR PRO ARG MET THR ASP THR VAL PHE
SEQRES  17 F  275  SER HIS ASN GLU ILE VAL GLU HIS THR ASP GLU GLU GLY
SEQRES  18 F  275  ASN VAL THR THR THR GLU GLU PRO VAL TYR THR GLU VAL
SEQRES  19 F  275  VAL ILE HIS GLU GLU GLY GLU GLU TRP GLY VAL ARG PRO
SEQRES  20 F  275  ASP GLY ILE PHE PHE ALA GLU ALA ALA TYR GLN ARG ARG
SEQRES  21 F  275  LYS LEU GLU ARG ILE GLU ALA ARG LEU SER ALA LEU GLU
SEQRES  22 F  275  GLN LYS
HET    PEG  A   2       7
HET    PEG  A  17       7
HET    TAM  A  32      11
HET    TAM  A  35      11
HET     CL  A  40       1
HET     BR  B  11       1
HET    PEG  B  13       7
HET     BR  B  38       1
HET     BR  B  39       1
HET    PEG  E   6       7
HET    PEG  E  16       7
HET    PEG  E  18       7
HET    PEG  E  21       7
HET    PEG  E  22       7
HET    PEG  E  27       7
HET    PEG  E  33       7
HET     BR  E  36       1
HET     CL  E  42       1
HET    PEG  C   3       7
HET     BR  C   8       1
HET     CL  C   9       1
HET     CL  C  12       1
HET    PEG  C  14       7
HET    TAM  C  28      11
HET    PEG  C  29       7
HET     CL  D  10       1
HET    PEG  D  15       7
HET     CL  D  41       1
HET     CA  F   1       1
HET    PEG  F   5       7
HET    PEG  F  24       7
HET    PEG  F  30       7
HET    PEG  F  34       7
HET     BR  F  37       1
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE
HETNAM      CL CHLORIDE ION
HETNAM      BR BROMIDE ION
HETNAM      CA CALCIUM ION
FORMUL   7  PEG    18(C4 H10 O3)
FORMUL   9  TAM    3(C7 H17 N O3)
FORMUL  11   CL    6(CL 1-)
FORMUL  12   BR    6(BR 1-)
FORMUL  35   CA    CA 2+
FORMUL  41  HOH   *323(H2 O)
HELIX    1   1 ASN A  832  GLY A  835  5                                   4
HELIX    2   2 ASP A  923  GLY A  931  1                                   9
HELIX    3   3 TRP A  940  GLY A  948  1                                   9
HELIX    4   4 ASN A  949  ALA A  951  5                                   3
HELIX    5   5 ILE A  958  HIS A  969  1                                  12
HELIX    6   6 ARG A 1035  ALA A 1060  1                                  26
HELIX    7   7 ASN B  832  GLY B  835  5                                   4
HELIX    8   8 SER B  847  GLY B  851  5                                   5
HELIX    9   9 ASP B  923  GLY B  931  1                                   9
HELIX   10  10 TRP B  940  LYS B  947  1                                   8
HELIX   11  11 ILE B  958  HIS B  969  1                                  12
HELIX   12  12 ARG B 1035  LEU B 1058  1                                  24
HELIX   13  13 LEU B 1058  GLN B 1063  1                                   6
HELIX   14  14 ASN E  832  GLY E  835  5                                   4
HELIX   15  15 SER E  847  GLY E  851  5                                   5
HELIX   16  16 ASP E  923  GLY E  931  1                                   9
HELIX   17  17 TRP E  940  GLY E  948  1                                   9
HELIX   18  18 ASN E  949  ALA E  951  5                                   3
HELIX   19  19 ILE E  958  HIS E  969  1                                  12
HELIX   20  20 ARG E 1035  LEU E 1061  1                                  27
HELIX   21  21 ASN C  832  GLY C  835  5                                   4
HELIX   22  22 ASP C  923  GLY C  931  1                                   9
HELIX   23  23 TRP C  940  LEU C  946  1                                   7
HELIX   24  24 ILE C  958  ALA C  968  1                                  11
HELIX   25  25 ARG C 1035  GLN C 1063  1                                  29
HELIX   26  26 ASN D  832  GLY D  835  5                                   4
HELIX   27  27 SER D  847  GLY D  851  5                                   5
HELIX   28  28 ASP D  923  GLY D  931  1                                   9
HELIX   29  29 TRP D  940  GLY D  948  1                                   9
HELIX   30  30 ILE D  958  HIS D  969  1                                  12
HELIX   31  31 ARG D 1035  GLU D 1062  1                                  28
HELIX   32  32 ASN F  832  GLY F  835  5                                   4
HELIX   33  33 SER F  847  GLY F  851  5                                   5
HELIX   34  34 ASP F  923  GLY F  931  1                                   9
HELIX   35  35 TRP F  940  GLY F  948  1                                   9
HELIX   36  36 ASN F  949  ALA F  951  5                                   3
HELIX   37  37 ILE F  958  ALA F  968  1                                  11
HELIX   38  38 ARG F 1035  GLU F 1062  1                                  28
SHEET    1   A 8 VAL A 801  ILE A 803  0
SHEET    2   A 8 ARG B 812  MET B 817  1  O  LEU B 816   N  ILE A 803
SHEET    3   A 8 TYR F 821  LYS F 826  1  O  PHE F 823   N  SER B 813
SHEET    4   A 8 ARG A 837  CYS A 841  1  N  ILE A 839   O  GLY F 822
SHEET    5   A 8 GLN A 853  TYR A 857 -1  O  ILE A 854   N  PHE A 840
SHEET    6   A 8 ARG A 866  ASN A 870 -1  O  ASN A 870   N  GLN A 853
SHEET    7   A 8 GLU B 873  GLN B 877  1  O  GLN B 877   N  TYR A 869
SHEET    8   A 8 VAL F 881  PRO F 883  1  O  LYS F 882   N  PHE B 876
SHEET    1   B 8 VAL B 881  PRO B 883  0
SHEET    2   B 8 GLU A 873  GLN A 877  1  N  HIS A 874   O  LYS B 882
SHEET    3   B 8 ARG F 866  ASN F 870  1  O  TYR F 869   N  GLN A 877
SHEET    4   B 8 GLN F 853  TYR F 857 -1  N  GLN F 853   O  ASN F 870
SHEET    5   B 8 ARG F 837  CYS F 841 -1  N  PHE F 840   O  ILE F 854
SHEET    6   B 8 TYR B 821  LYS B 826  1  N  GLY B 822   O  ILE F 839
SHEET    7   B 8 ARG A 812  MET A 817  1  N  VAL A 815   O  PHE B 823
SHEET    8   B 8 VAL F 801  ILE F 803  1  O  ILE F 803   N  LEU A 816
SHEET    1   C 8 VAL A 881  PRO A 883  0
SHEET    2   C 8 GLU F 873  GLN F 877  1  O  PHE F 876   N  LYS A 882
SHEET    3   C 8 ARG B 866  ASN B 870  1  N  TYR B 869   O  GLN F 877
SHEET    4   C 8 GLN B 853  TYR B 857 -1  N  GLN B 853   O  ASN B 870
SHEET    5   C 8 ARG B 837  CYS B 841 -1  N  PHE B 840   O  ILE B 854
SHEET    6   C 8 TYR A 821  LYS A 826  1  N  GLY A 822   O  ILE B 839
SHEET    7   C 8 ARG F 812  MET F 817  1  O  VAL F 815   N  PHE A 823
SHEET    8   C 8 VAL B 801  ILE B 803  1  N  VAL B 801   O  GLU F 814
SHEET    1   D 4 TYR A 902  LEU A 903  0
SHEET    2   D 4 ILE B 908  THR B 910  1  O  ILE B 908   N  LEU A 903
SHEET    3   D 4 GLY F1029  VAL F1034 -1  O  VAL F1034   N  VAL B 909
SHEET    4   D 4 LEU F 984  TYR F 989 -1  N  CYS F 985   O  GLY F1033
SHEET    1   E 2 ILE A 908  VAL A 909  0
SHEET    2   E 2 TYR F 902  LEU F 903  1  O  LEU F 903   N  ILE A 908
SHEET    1   F 2 ILE A 936  TYR A 938  0
SHEET    2   F 2 HIS A 954  GLY A 956 -1  O  HIS A 954   N  TYR A 938
SHEET    1   G 4 LEU A 984  TYR A 989  0
SHEET    2   G 4 GLY A1029  VAL A1034 -1  O  GLY A1029   N  TYR A 989
SHEET    3   G 4 ILE F 908  THR F 910 -1  O  VAL F 909   N  VAL A1034
SHEET    4   G 4 TYR B 902  LEU B 903  1  N  LEU B 903   O  ILE F 908
SHEET    1   H 2 MET A 992  THR A1006  0
SHEET    2   H 2 VAL A1012  HIS A1026 -1  O  GLU A1017   N  GLU A1001
SHEET    1   I 3 VAL B 920  VAL B 921  0
SHEET    2   I 3 ILE F 936  TYR F 938 -1  O  MET F 937   N  VAL B 920
SHEET    3   I 3 HIS F 954  GLY F 956 -1  O  HIS F 954   N  TYR F 938
SHEET    1   J 2 ILE B 936  TYR B 938  0
SHEET    2   J 2 HIS B 954  GLY B 956 -1  O  GLY B 956   N  ILE B 936
SHEET    1   K 2 LEU B 984  TYR B 989  0
SHEET    2   K 2 GLY B1029  VAL B1034 -1  O  GLY B1033   N  CYS B 985
SHEET    1   L 2 MET B 992  THR B1006  0
SHEET    2   L 2 VAL B1012  HIS B1026 -1  O  ILE B1025   N  MET B 992
SHEET    1   M 8 THR E 802  ILE E 803  0
SHEET    2   M 8 ARG D 812  MET D 817  1  O  LEU D 816   N  ILE E 803
SHEET    3   M 8 TYR C 821  LYS C 826  1  N  PHE C 823   O  SER D 813
SHEET    4   M 8 ARG E 837  CYS E 841  1  N  ILE E 839   O  GLY C 822
SHEET    5   M 8 GLN E 853  TYR E 857 -1  O  ILE E 854   N  PHE E 840
SHEET    6   M 8 ARG E 866  ASN E 870 -1  O  ASN E 870   N  GLN E 853
SHEET    7   M 8 GLU D 873  GLN D 877  1  O  GLN D 877   N  TYR E 869
SHEET    8   M 8 VAL C 881  PRO C 883  1  N  LYS C 882   O  HIS D 874
SHEET    1   N 8 VAL C 801  ILE C 803  0
SHEET    2   N 8 ARG E 812  MET E 817  1  N  LEU E 816   O  ILE C 803
SHEET    3   N 8 TYR D 821  LYS D 826  1  O  PHE D 823   N  VAL E 815
SHEET    4   N 8 ARG C 837  CYS C 841  1  N  ILE C 839   O  GLY D 822
SHEET    5   N 8 GLN C 853  TYR C 857 -1  O  ILE C 854   N  PHE C 840
SHEET    6   N 8 ARG C 866  ASN C 870 -1  O  ARG C 866   N  TYR C 857
SHEET    7   N 8 GLU E 873  GLN E 877  1  N  GLN E 877   O  TYR C 869
SHEET    8   N 8 VAL D 881  PRO D 883  1  O  LYS D 882   N  PHE E 876
SHEET    1   O 8 VAL E 881  PRO E 883  0
SHEET    2   O 8 GLU C 873  GLN C 877  1  O  PHE C 876   N  LYS E 882
SHEET    3   O 8 ARG D 866  ASN D 870  1  O  TYR D 869   N  GLN C 877
SHEET    4   O 8 GLN D 853  TYR D 857 -1  N  TYR D 857   O  ARG D 866
SHEET    5   O 8 ARG D 837  CYS D 841 -1  N  PHE D 840   O  ILE D 854
SHEET    6   O 8 TYR E 821  LYS E 826  1  N  ILE E 824   O  ILE D 839
SHEET    7   O 8 ARG C 812  MET C 817  1  O  VAL C 815   N  PHE E 823
SHEET    8   O 8 VAL D 801  ILE D 803  1  O  ILE D 803   N  LEU C 816
SHEET    1   P 2 TYR E 902  LEU E 903  0
SHEET    2   P 2 ILE D 908  VAL D 909  1  O  ILE D 908   N  LEU E 903
SHEET    1   Q 4 TYR C 902  LEU C 903  0
SHEET    2   Q 4 ILE E 908  THR E 910  1  N  ILE E 908   O  LEU C 903
SHEET    3   Q 4 GLY D1029  VAL D1034 -1  O  VAL D1034   N  VAL E 909
SHEET    4   Q 4 LEU D 984  TYR D 989 -1  N  CYS D 985   O  GLY D1033
SHEET    1   R 3 VAL E 920  VAL E 921  0
SHEET    2   R 3 ILE D 936  TYR D 938 -1  O  MET D 937   N  VAL E 920
SHEET    3   R 3 HIS D 954  GLY D 956 -1  O  HIS D 954   N  TYR D 938
SHEET    1   S 2 ILE E 936  TYR E 938  0
SHEET    2   S 2 HIS E 954  GLY E 956 -1  O  HIS E 954   N  TYR E 938
SHEET    1   T 2 LEU E 984  TYR E 989  0
SHEET    2   T 2 GLY E1029  VAL E1034 -1  O  GLY E1029   N  TYR E 989
SHEET    1   U 2 MET E 992  THR E1006  0
SHEET    2   U 2 VAL E1012  HIS E1026 -1  O  VAL E1019   N  HIS E 999
SHEET    1   V 2 ILE C 908  VAL C 909  0
SHEET    2   V 2 TYR D 902  LEU D 903  1  O  LEU D 903   N  ILE C 908
SHEET    1   W 3 HIS C 954  GLY C 956  0
SHEET    2   W 3 ILE C 936  TYR C 938 -1  N  ILE C 936   O  GLY C 956
SHEET    3   W 3 VAL D 920  VAL D 921 -1  O  VAL D 920   N  MET C 937
SHEET    1   X 2 LEU C 984  TYR C 989  0
SHEET    2   X 2 GLY C1029  VAL C1034 -1  O  GLY C1033   N  CYS C 985
SHEET    1   Y 2 MET C 992  THR C1006  0
SHEET    2   Y 2 VAL C1012  HIS C1026 -1  O  ILE C1025   N  MET C 992
SHEET    1   Z 2 MET D 992  THR D1006  0
SHEET    2   Z 2 VAL D1012  HIS D1026 -1  O  THR D1013   N  HIS D1005
SHEET    1  AA 2 MET F 992  THR F1006  0
SHEET    2  AA 2 VAL F1012  HIS F1026 -1  O  VAL F1019   N  HIS F 999
CISPEP   1 SER B  976    THR B  977          0         4.00
CISPEP   2 GLY D  948    ASN D  949          0         1.62
SITE     1 AC1  3 ALA A 943  ARG A 952  HIS A 954
SITE     1 AC2  4 VAL A 921  ARG A1048  VAL B 933  TYR B 935
SITE     1 AC3  4 ASN A 887  GLU A 914   BR B  39  ASP B 942
SITE     1 AC4  6 HOH A 113  HOH A 241  ASP A 942  ASN F 887
SITE     2 AC4  6 VAL F 888  GLU F 914
SITE     1 AC5  3 HOH A 222  THR A 846  SER A 847
SITE     1 AC6  3 HOH B 126  THR B 846  SER B 847
SITE     1 AC7  1 ASN B 887
SITE     1 AC8  3 VAL A 983  PHE B 955  HOH F  62
SITE     1 AC9  3 TAM A  32  HOH B 136  HIS B 954
SITE     1 BC1  3 SER C 878  HOH E 306  VAL E 888
SITE     1 BC2  1 ASP E 831
SITE     1 BC3  8 HOH D 233  PRO D 829  THR D 830  ASP D 831
SITE     2 BC3  8 ASN D 832  GLU E 818  GLY E 819  GLU E 820
SITE     1 BC4  5 TRP E 940  ALA E 943  LYS E 947  ARG E 952
SITE     2 BC4  5 HIS E 954
SITE     1 BC5  7 GLU C 818  GLY C 819  GLU C 820  PRO E 829
SITE     2 BC5  7 THR E 830  ASP E 831  ASN E 832
SITE     1 BC6  1 THR E 849
SITE     1 BC7  3 HOH C 149  HOH E  88  PHE E 955
SITE     1 BC8  2 THR E 846  SER E 847
SITE     1 BC9  3 ILE C 828  PRO C 829  PRO C 833
SITE     1 CC1  2 PHE C 955  VAL D 983
SITE     1 CC2  2 THR C 846  SER C 847
SITE     1 CC3  2 PHE C 997  SER C 998
SITE     1 CC4  5 ASP C 886  ASN C 887  GLU C 914  HOH E 240
SITE     2 CC4  5 ASP E 942
SITE     1 CC5  8 PRO C 829  THR C 830  ASP C 831  ASN C 832
SITE     2 CC5  8 GLU D 818  GLY D 819  GLU D 820  HOH E 127
SITE     1 CC6  2 PHE D 955  VAL E 983
SITE     1 CC7  3 VAL C 888  ASP D 880  THR E 899
SITE     1 CC8  3 HOH C 218  ALA C 959  LYS D 916
SITE     1 CC9  2 VAL B 983  PHE F 955
SITE     1 DC1  9 HOH F  78  ARG F 837  ILE F 839  THR F 846
SITE     2 DC1  9 GLN F 853  THR F 855  THR F 995  PHE F 997
SITE     3 DC1  9 TYR F1020
SITE     1 DC2  5 HOH F 317  ASN F 860  ASN F 861  THR F 862
SITE     2 DC2  5 SER F 864
SITE     1 DC3  2 ASN A 885  SER F 878
SITE     1 DC4  8 GLU B 818  GLY B 819  GLU B 820  HOH F 135
SITE     2 DC4  8 PRO F 829  THR F 830  ASP F 831  ASN F 832
SITE     1 DC5  2 PHE A 955  GLY F1038
CRYST1   62.650   79.950  109.580  81.71  76.53  87.11 P 1           6
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      0.015962 -0.000806 -0.003748        0.00000
SCALE2      0.000000  0.012524 -0.001724        0.00000
SCALE3      0.000000  0.000000  0.009472        0.00000
      
PROCHECK
Go to PROCHECK summary
 References