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PDBsum entry 2wj8

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Top Page protein dna_rna ligands Protein-protein interface(s) links
RNA binding protein/RNA PDB id
2wj8
Jmol
Contents
Protein chains
(+ 14 more) 374 a.a.
DNA/RNA
Ligands
BO4 ×12
Waters ×685
HEADER    RNA BINDING PROTEIN/RNA                 25-MAY-09   2WJ8
TITLE     RESPIRATORY SYNCITIAL VIRUS RIBONUCLEOPROTEIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NUCLEOPROTEIN;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q,
COMPND   4  R, S, T;
COMPND   5 SYNONYM: PROTEIN N, NUCLEOCAPSID PROTEIN;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RNA (5'-R(*CP*CP*CP*CP*CP*C)-3');
COMPND   9 CHAIN: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q,
COMPND  10  r, s, t;
COMPND  11 OTHER_DETAILS: NON SPECIFIC RNA FROM CELLULAR ORIGIN BOUND
COMPND  12  TO THE NUCLEOPROTEIN
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN RESPIRATORY SYNCYTIAL VIRUS A
SOURCE   3  STRAIN LONG;
SOURCE   4 ORGANISM_TAXID: 11260;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET-28B;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE  13 ORGANISM_TAXID: 469008;
SOURCE  14 STRAIN: BL21(DE3);
SOURCE  15 ATCC: BAA-1025
KEYWDS    RNA BINDING PROTEIN RNA COMPLEX, NUCLEOCAPSID (N),
KEYWDS   2 RIBONUCLEOPROTEIN, RESPIRATORY SYNCYTIAL VIRUS (RSV),
KEYWDS   3 VIRAL NUCLEOPROTEIN, TEMPLATE-LIKE ASSEMBLY, RNA, VIRION,
KEYWDS   4 COMPLEX, CYTOPLASM, RNA BINDING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.G.TAWAR,S.DUQUERROY,C.VONRHEIN,P.F.VARELA,L.DAMIER-PIOLLE,
AUTHOR   2 N.CASTAGNE,K.MACLELLAN,H.BEDOUELLE,G.BRICOGNE,D.BHELLA,
AUTHOR   3 J.ELEOUET,F.A.REY
REVDAT   2   17-APR-13 2WJ8    1       JRNL   REMARK VERSN
REVDAT   1   08-DEC-09 2WJ8    0
JRNL        AUTH   R.G.TAWAR,S.DUQUERROY,C.VONRHEIN,P.F.VARELA,
JRNL        AUTH 2 L.DAMIER-PIOLLE,N.CASTAGNE,K.MACLELLAN,H.BEDOUELLE,
JRNL        AUTH 3 G.BRICOGNE,D.BHELLA,J.ELEOUET,F.A.REY
JRNL        TITL   CRYSTAL STRUCTURE OF A NUCLEOCAPSID-LIKE
JRNL        TITL 2 NUCLEOPROTEIN-RNA COMPLEX OF RESPIRATORY SYNCYTIAL
JRNL        TITL 3 VIRUS
JRNL        REF    SCIENCE                       V. 326  1279 2009
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   19965480
JRNL        DOI    10.1126/SCIENCE.1177634
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.MACLELLAN,C.LONEY,R.P.YEO,D.BHELLA
REMARK   1  TITL   THE 24-ANGSTROM STRUCTURE OF RESPIRATORY SYNCYTIAL
REMARK   1  TITL 2 VIRUS NUCLEOCAPSID PROTEIN-RNA DECAMERIC RINGS.
REMARK   1  REF    J.VIROL.                      V.  81  9519 2007
REMARK   1  REFN                   ISSN 0022-538X
REMARK   1  PMID   17567697
REMARK   1  DOI    10.1128/JVI.00526-07
REMARK   2
REMARK   2 RESOLUTION.    3.29 ANGSTROMS.
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : BUSTER-TNT 2.7.0
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.29
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.18
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.65
REMARK   3   NUMBER OF REFLECTIONS             : 150167
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD           : RESOLUTION SHELLS
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.2057
REMARK   3   R VALUE            (WORKING SET)  : 0.2050
REMARK   3   FREE R VALUE                      : 0.2258
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 3.4
REMARK   3   FREE R VALUE TEST SET COUNT       : 5094
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED               : 20
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.29
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.38
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.65
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 10427
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2308
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 10175
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2301
REMARK   3   BIN FREE R VALUE                        : 0.2592
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.42
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 252
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 58383
REMARK   3   NUCLEIC ACID ATOMS       : 2800
REMARK   3   HETEROGEN ATOMS          : 60
REMARK   3   SOLVENT ATOMS            : 685
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 79.61
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.43
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -12.9790
REMARK   3    B22 (A**2) : 26.1085
REMARK   3    B33 (A**2) : -13.1294
REMARK   3    B12 (A**2) : 0.0000
REMARK   3    B13 (A**2) : 2.6224
REMARK   3    B23 (A**2) : 0.0000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL
REMARK   3
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL
REMARK   3
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND LENGTHS                       (A) : NULL
REMARK   3    BOND ANGLES                  (DEGREES) : NULL
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS. RESIDUE TYPES WITHOUT IDEAL-DIST CONTACT DATA, C BO4.
REMARK   3  THE RNA MOLECULE WAS NON SPECIFICALLY INCORPORATED. EACH BASE WAS
REMARK   3  MODELED AS A CYTOSINE BUT CORRESPOND TO AN AVERAGE OF FOUR
REMARK   3  POSSIBLE BASES OF THE GENETIC CODE. C TERMINAL ENDS ARE
REMARK   3  DISORDERED. NCS RESTRAINT LSSR (-AUTONCS)
REMARK   4
REMARK   4 2WJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-09.
REMARK 100 THE PDBE ID CODE IS EBI-39906.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-08
REMARK 200  TEMPERATURE           (KELVIN) : 200
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL
REMARK 200                                   MONOCHROMATOR, SAGITALLY
REMARK 200                                   FOCUSSING
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 384943
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.30
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9
REMARK 200  DATA REDUNDANCY                : 2.6
REMARK 200  R MERGE                    (I) : 0.12
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.47
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3
REMARK 200  R MERGE FOR SHELL          (I) : 0.40
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, MOLREP
REMARK 200 STARTING MODEL: EMDB ENTRY EMD-1622
REMARK 200
REMARK 200 REMARK: STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT USING
REMARK 200  24 ANG EM MAP AND PHASES WERE EXTENDED TO 3.3 ANG BY PHASE
REMARK 200  EXTENSION USING 20-FOLD NCS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12%MPD, 50MM MGCL2, 100MM TRIS
REMARK 280  PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      109.10000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      110.49500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      109.10000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      110.49500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 20MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 20MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 75970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 147400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -455.05 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, N, O, T, S, P, Q, R,
REMARK 350                    AND CHAINS: s, q, l, o, t, n, r, m, p, k
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: 20MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 20MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 75820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 147060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -452.47 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J, H, I, B, C, D, E, F, G,
REMARK 350                    AND CHAINS: f, a, j, i, c, h, g, b, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 B    BO4 D2001  LIES ON A SPECIAL POSITION.
REMARK 375 B    BO4 T2001  LIES ON A SPECIAL POSITION.
REMARK 375 B    BO4 I2001  LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     GLU A   376
REMARK 465     ALA A   377
REMARK 465     ILE A   378
REMARK 465     LYS A   379
REMARK 465     HIS A   380
REMARK 465     GLN A   381
REMARK 465     LEU A   382
REMARK 465     ASN A   383
REMARK 465     PRO A   384
REMARK 465     LYS A   385
REMARK 465     ASP A   386
REMARK 465     ASN A   387
REMARK 465     ASP A   388
REMARK 465     VAL A   389
REMARK 465     GLU A   390
REMARK 465     LEU A   391
REMARK 465     MET B     1
REMARK 465     ALA B   377
REMARK 465     ILE B   378
REMARK 465     LYS B   379
REMARK 465     HIS B   380
REMARK 465     GLN B   381
REMARK 465     LEU B   382
REMARK 465     ASN B   383
REMARK 465     PRO B   384
REMARK 465     LYS B   385
REMARK 465     ASP B   386
REMARK 465     ASN B   387
REMARK 465     ASP B   388
REMARK 465     VAL B   389
REMARK 465     GLU B   390
REMARK 465     LEU B   391
REMARK 465     MET C     1
REMARK 465     LYS C   379
REMARK 465     HIS C   380
REMARK 465     GLN C   381
REMARK 465     LEU C   382
REMARK 465     ASN C   383
REMARK 465     PRO C   384
REMARK 465     LYS C   385
REMARK 465     ASP C   386
REMARK 465     ASN C   387
REMARK 465     ASP C   388
REMARK 465     VAL C   389
REMARK 465     GLU C   390
REMARK 465     LEU C   391
REMARK 465     MET D     1
REMARK 465     GLU D   376
REMARK 465     ALA D   377
REMARK 465     ILE D   378
REMARK 465     LYS D   379
REMARK 465     HIS D   380
REMARK 465     GLN D   381
REMARK 465     LEU D   382
REMARK 465     ASN D   383
REMARK 465     PRO D   384
REMARK 465     LYS D   385
REMARK 465     ASP D   386
REMARK 465     ASN D   387
REMARK 465     ASP D   388
REMARK 465     VAL D   389
REMARK 465     GLU D   390
REMARK 465     LEU D   391
REMARK 465     MET E     1
REMARK 465     GLU E   376
REMARK 465     ALA E   377
REMARK 465     ILE E   378
REMARK 465     LYS E   379
REMARK 465     HIS E   380
REMARK 465     GLN E   381
REMARK 465     LEU E   382
REMARK 465     ASN E   383
REMARK 465     PRO E   384
REMARK 465     LYS E   385
REMARK 465     ASP E   386
REMARK 465     ASN E   387
REMARK 465     ASP E   388
REMARK 465     VAL E   389
REMARK 465     GLU E   390
REMARK 465     LEU E   391
REMARK 465     MET F     1
REMARK 465     LYS F   379
REMARK 465     HIS F   380
REMARK 465     GLN F   381
REMARK 465     LEU F   382
REMARK 465     ASN F   383
REMARK 465     PRO F   384
REMARK 465     LYS F   385
REMARK 465     ASP F   386
REMARK 465     ASN F   387
REMARK 465     ASP F   388
REMARK 465     VAL F   389
REMARK 465     GLU F   390
REMARK 465     LEU F   391
REMARK 465     MET G     1
REMARK 465     LYS G   379
REMARK 465     HIS G   380
REMARK 465     GLN G   381
REMARK 465     LEU G   382
REMARK 465     ASN G   383
REMARK 465     PRO G   384
REMARK 465     LYS G   385
REMARK 465     ASP G   386
REMARK 465     ASN G   387
REMARK 465     ASP G   388
REMARK 465     VAL G   389
REMARK 465     GLU G   390
REMARK 465     LEU G   391
REMARK 465     MET H     1
REMARK 465     ALA H   377
REMARK 465     ILE H   378
REMARK 465     LYS H   379
REMARK 465     HIS H   380
REMARK 465     GLN H   381
REMARK 465     LEU H   382
REMARK 465     ASN H   383
REMARK 465     PRO H   384
REMARK 465     LYS H   385
REMARK 465     ASP H   386
REMARK 465     ASN H   387
REMARK 465     ASP H   388
REMARK 465     VAL H   389
REMARK 465     GLU H   390
REMARK 465     LEU H   391
REMARK 465     MET I     1
REMARK 465     GLU I   376
REMARK 465     ALA I   377
REMARK 465     ILE I   378
REMARK 465     LYS I   379
REMARK 465     HIS I   380
REMARK 465     GLN I   381
REMARK 465     LEU I   382
REMARK 465     ASN I   383
REMARK 465     PRO I   384
REMARK 465     LYS I   385
REMARK 465     ASP I   386
REMARK 465     ASN I   387
REMARK 465     ASP I   388
REMARK 465     VAL I   389
REMARK 465     GLU I   390
REMARK 465     LEU I   391
REMARK 465     MET J     1
REMARK 465     ALA J   372
REMARK 465     GLU J   373
REMARK 465     GLU J   374
REMARK 465     LEU J   375
REMARK 465     GLU J   376
REMARK 465     ALA J   377
REMARK 465     ILE J   378
REMARK 465     LYS J   379
REMARK 465     HIS J   380
REMARK 465     GLN J   381
REMARK 465     LEU J   382
REMARK 465     ASN J   383
REMARK 465     PRO J   384
REMARK 465     LYS J   385
REMARK 465     ASP J   386
REMARK 465     ASN J   387
REMARK 465     ASP J   388
REMARK 465     VAL J   389
REMARK 465     GLU J   390
REMARK 465     LEU J   391
REMARK 465     MET K     1
REMARK 465     GLU K   376
REMARK 465     ALA K   377
REMARK 465     ILE K   378
REMARK 465     LYS K   379
REMARK 465     HIS K   380
REMARK 465     GLN K   381
REMARK 465     LEU K   382
REMARK 465     ASN K   383
REMARK 465     PRO K   384
REMARK 465     LYS K   385
REMARK 465     ASP K   386
REMARK 465     ASN K   387
REMARK 465     ASP K   388
REMARK 465     VAL K   389
REMARK 465     GLU K   390
REMARK 465     LEU K   391
REMARK 465     MET L     1
REMARK 465     LYS L   379
REMARK 465     HIS L   380
REMARK 465     GLN L   381
REMARK 465     LEU L   382
REMARK 465     ASN L   383
REMARK 465     PRO L   384
REMARK 465     LYS L   385
REMARK 465     ASP L   386
REMARK 465     ASN L   387
REMARK 465     ASP L   388
REMARK 465     VAL L   389
REMARK 465     GLU L   390
REMARK 465     LEU L   391
REMARK 465     MET M     1
REMARK 465     GLU M   376
REMARK 465     ALA M   377
REMARK 465     ILE M   378
REMARK 465     LYS M   379
REMARK 465     HIS M   380
REMARK 465     GLN M   381
REMARK 465     LEU M   382
REMARK 465     ASN M   383
REMARK 465     PRO M   384
REMARK 465     LYS M   385
REMARK 465     ASP M   386
REMARK 465     ASN M   387
REMARK 465     ASP M   388
REMARK 465     VAL M   389
REMARK 465     GLU M   390
REMARK 465     LEU M   391
REMARK 465     MET N     1
REMARK 465     HIS N   380
REMARK 465     GLN N   381
REMARK 465     LEU N   382
REMARK 465     ASN N   383
REMARK 465     PRO N   384
REMARK 465     LYS N   385
REMARK 465     ASP N   386
REMARK 465     ASN N   387
REMARK 465     ASP N   388
REMARK 465     VAL N   389
REMARK 465     GLU N   390
REMARK 465     LEU N   391
REMARK 465     MET O     1
REMARK 465     LEU O   375
REMARK 465     GLU O   376
REMARK 465     ALA O   377
REMARK 465     ILE O   378
REMARK 465     LYS O   379
REMARK 465     HIS O   380
REMARK 465     GLN O   381
REMARK 465     LEU O   382
REMARK 465     ASN O   383
REMARK 465     PRO O   384
REMARK 465     LYS O   385
REMARK 465     ASP O   386
REMARK 465     ASN O   387
REMARK 465     ASP O   388
REMARK 465     VAL O   389
REMARK 465     GLU O   390
REMARK 465     LEU O   391
REMARK 465     MET P     1
REMARK 465     GLU P   376
REMARK 465     ALA P   377
REMARK 465     ILE P   378
REMARK 465     LYS P   379
REMARK 465     HIS P   380
REMARK 465     GLN P   381
REMARK 465     LEU P   382
REMARK 465     ASN P   383
REMARK 465     PRO P   384
REMARK 465     LYS P   385
REMARK 465     ASP P   386
REMARK 465     ASN P   387
REMARK 465     ASP P   388
REMARK 465     VAL P   389
REMARK 465     GLU P   390
REMARK 465     LEU P   391
REMARK 465     MET Q     1
REMARK 465     GLU Q   376
REMARK 465     ALA Q   377
REMARK 465     ILE Q   378
REMARK 465     LYS Q   379
REMARK 465     HIS Q   380
REMARK 465     GLN Q   381
REMARK 465     LEU Q   382
REMARK 465     ASN Q   383
REMARK 465     PRO Q   384
REMARK 465     LYS Q   385
REMARK 465     ASP Q   386
REMARK 465     ASN Q   387
REMARK 465     ASP Q   388
REMARK 465     VAL Q   389
REMARK 465     GLU Q   390
REMARK 465     LEU Q   391
REMARK 465     MET R     1
REMARK 465     ILE R   378
REMARK 465     LYS R   379
REMARK 465     HIS R   380
REMARK 465     GLN R   381
REMARK 465     LEU R   382
REMARK 465     ASN R   383
REMARK 465     PRO R   384
REMARK 465     LYS R   385
REMARK 465     ASP R   386
REMARK 465     ASN R   387
REMARK 465     ASP R   388
REMARK 465     VAL R   389
REMARK 465     GLU R   390
REMARK 465     LEU R   391
REMARK 465     MET S     1
REMARK 465     HIS S   380
REMARK 465     GLN S   381
REMARK 465     LEU S   382
REMARK 465     ASN S   383
REMARK 465     PRO S   384
REMARK 465     LYS S   385
REMARK 465     ASP S   386
REMARK 465     ASN S   387
REMARK 465     ASP S   388
REMARK 465     VAL S   389
REMARK 465     GLU S   390
REMARK 465     LEU S   391
REMARK 465     MET T     1
REMARK 465     GLU T   376
REMARK 465     ALA T   377
REMARK 465     ILE T   378
REMARK 465     LYS T   379
REMARK 465     HIS T   380
REMARK 465     GLN T   381
REMARK 465     LEU T   382
REMARK 465     ASN T   383
REMARK 465     PRO T   384
REMARK 465     LYS T   385
REMARK 465     ASP T   386
REMARK 465     ASN T   387
REMARK 465     ASP T   388
REMARK 465     VAL T   389
REMARK 465     GLU T   390
REMARK 465     LEU T   391
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   OD1  ASN D   364     O    GLY E   273              2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OD1  ASN P    93     O2   BO4 N  2001     2656     2.12
REMARK 500   OD1  ASN S    93     O2   BO4 K  2001     2656     2.20
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      C a1002   C2  -  N1  -  C1' ANGL. DEV. = -18.5 DEGREES
REMARK 500      C a1002   C6  -  N1  -  C1' ANGL. DEV. =  18.6 DEGREES
REMARK 500      C a1003   C2  -  N1  -  C1' ANGL. DEV. =   8.2 DEGREES
REMARK 500      C a1003   C6  -  N1  -  C1' ANGL. DEV. =  -8.3 DEGREES
REMARK 500      C a1005   C2  -  N1  -  C1' ANGL. DEV. = -15.9 DEGREES
REMARK 500      C a1005   C6  -  N1  -  C1' ANGL. DEV. =  16.0 DEGREES
REMARK 500      C a1007   C2  -  N1  -  C1' ANGL. DEV. =  -8.8 DEGREES
REMARK 500      C a1007   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500      C b1002   C2  -  N1  -  C1' ANGL. DEV. = -18.6 DEGREES
REMARK 500      C b1002   C6  -  N1  -  C1' ANGL. DEV. =  18.7 DEGREES
REMARK 500      C b1003   C2  -  N1  -  C1' ANGL. DEV. =   8.1 DEGREES
REMARK 500      C b1003   C6  -  N1  -  C1' ANGL. DEV. =  -8.3 DEGREES
REMARK 500      C b1005   C2  -  N1  -  C1' ANGL. DEV. = -16.0 DEGREES
REMARK 500      C b1005   C6  -  N1  -  C1' ANGL. DEV. =  16.0 DEGREES
REMARK 500      C b1007   C2  -  N1  -  C1' ANGL. DEV. =  -8.8 DEGREES
REMARK 500      C b1007   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500      C c1002   C2  -  N1  -  C1' ANGL. DEV. = -18.4 DEGREES
REMARK 500      C c1002   C6  -  N1  -  C1' ANGL. DEV. =  18.6 DEGREES
REMARK 500      C c1003   C2  -  N1  -  C1' ANGL. DEV. =   8.4 DEGREES
REMARK 500      C c1003   C6  -  N1  -  C1' ANGL. DEV. =  -8.3 DEGREES
REMARK 500      C c1005   C2  -  N1  -  C1' ANGL. DEV. = -16.0 DEGREES
REMARK 500      C c1005   C6  -  N1  -  C1' ANGL. DEV. =  16.1 DEGREES
REMARK 500      C c1007   C2  -  N1  -  C1' ANGL. DEV. =  -8.8 DEGREES
REMARK 500      C c1007   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500      C d1002   C2  -  N1  -  C1' ANGL. DEV. = -18.4 DEGREES
REMARK 500      C d1002   C6  -  N1  -  C1' ANGL. DEV. =  18.6 DEGREES
REMARK 500      C d1003   C2  -  N1  -  C1' ANGL. DEV. =   8.2 DEGREES
REMARK 500      C d1003   C6  -  N1  -  C1' ANGL. DEV. =  -8.2 DEGREES
REMARK 500      C d1005   C2  -  N1  -  C1' ANGL. DEV. = -16.1 DEGREES
REMARK 500      C d1005   C6  -  N1  -  C1' ANGL. DEV. =  16.3 DEGREES
REMARK 500      C d1007   C2  -  N1  -  C1' ANGL. DEV. =  -8.8 DEGREES
REMARK 500      C d1007   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500      C e1002   C2  -  N1  -  C1' ANGL. DEV. = -18.4 DEGREES
REMARK 500      C e1002   C6  -  N1  -  C1' ANGL. DEV. =  18.6 DEGREES
REMARK 500      C e1003   C2  -  N1  -  C1' ANGL. DEV. =   8.4 DEGREES
REMARK 500      C e1003   C6  -  N1  -  C1' ANGL. DEV. =  -8.3 DEGREES
REMARK 500      C e1005   C2  -  N1  -  C1' ANGL. DEV. = -16.0 DEGREES
REMARK 500      C e1005   C6  -  N1  -  C1' ANGL. DEV. =  16.0 DEGREES
REMARK 500      C e1007   C2  -  N1  -  C1' ANGL. DEV. =  -8.6 DEGREES
REMARK 500      C e1007   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500      C f1002   C2  -  N1  -  C1' ANGL. DEV. = -18.5 DEGREES
REMARK 500      C f1002   C6  -  N1  -  C1' ANGL. DEV. =  18.6 DEGREES
REMARK 500      C f1003   C2  -  N1  -  C1' ANGL. DEV. =   8.2 DEGREES
REMARK 500      C f1003   C6  -  N1  -  C1' ANGL. DEV. =  -8.4 DEGREES
REMARK 500      C f1005   C2  -  N1  -  C1' ANGL. DEV. = -15.9 DEGREES
REMARK 500      C f1005   C6  -  N1  -  C1' ANGL. DEV. =  16.0 DEGREES
REMARK 500      C f1007   C2  -  N1  -  C1' ANGL. DEV. =  -8.8 DEGREES
REMARK 500      C f1007   C6  -  N1  -  C1' ANGL. DEV. =   9.1 DEGREES
REMARK 500      C g1002   C2  -  N1  -  C1' ANGL. DEV. = -18.4 DEGREES
REMARK 500      C g1002   C6  -  N1  -  C1' ANGL. DEV. =  18.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     160 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  20       42.92   -108.02
REMARK 500    HIS A  59       33.05    -88.83
REMARK 500    ARG A  76      -59.84    -19.79
REMARK 500    ASP A 175       16.32   -154.55
REMARK 500    GLN A 255       43.40   -147.35
REMARK 500    ARG A 338       20.62    -77.48
REMARK 500    ASN A 360     -159.36    -87.43
REMARK 500    THR A 371     -103.97    -94.09
REMARK 500    SER B  20       42.92   -107.89
REMARK 500    HIS B  59       33.02    -88.79
REMARK 500    ARG B  76      -59.72    -19.84
REMARK 500    ASP B 175       16.32   -154.52
REMARK 500    GLN B 255       43.40   -147.35
REMARK 500    ARG B 338       20.56    -77.47
REMARK 500    ASN B 360     -159.90    -87.42
REMARK 500    THR B 371     -103.80    -93.97
REMARK 500    SER C  20       43.14   -108.15
REMARK 500    HIS C  59       32.97    -88.89
REMARK 500    ARG C  76      -59.57    -19.92
REMARK 500    ASP C 175       16.35   -154.29
REMARK 500    GLN C 255       43.38   -147.20
REMARK 500    ARG C 338       20.62    -77.47
REMARK 500    THR C 371     -104.13    -94.29
REMARK 500    SER D  20       43.33   -108.29
REMARK 500    HIS D  59       33.11    -88.86
REMARK 500    ARG D  76      -59.81    -19.74
REMARK 500    ASP D 175       16.40   -154.56
REMARK 500    GLN D 255       43.41   -147.29
REMARK 500    ARG D 338       20.47    -77.41
REMARK 500    ASN D 360     -159.04    -87.80
REMARK 500    THR D 371     -103.58    -93.87
REMARK 500    SER E  20       43.61   -108.49
REMARK 500    HIS E  59       32.98    -88.89
REMARK 500    ARG E  76      -59.64    -19.81
REMARK 500    ASP E 175       16.25   -154.44
REMARK 500    GLN E 255       43.27   -147.29
REMARK 500    ARG E 338       20.64    -77.61
REMARK 500    ASN E 360     -159.73    -87.43
REMARK 500    THR E 371     -104.13    -94.07
REMARK 500    SER F  20       42.80   -107.76
REMARK 500    HIS F  59       33.01    -88.82
REMARK 500    ARG F  76      -59.70    -19.90
REMARK 500    ASP F 175       16.35   -154.50
REMARK 500    GLN F 255       43.36   -147.33
REMARK 500    ARG F 338       20.52    -77.42
REMARK 500    ASN F 360     -159.58    -87.63
REMARK 500    THR F 371     -103.98    -94.07
REMARK 500    SER G  20       42.71   -107.65
REMARK 500    HIS G  59       33.07    -88.80
REMARK 500    ARG G  76      -59.75    -19.85
REMARK 500
REMARK 500 THIS ENTRY HAS     156 RAMACHANDRAN OUTLIERS.
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    THR A  79        24.3      L          L   OUTSIDE RANGE
REMARK 500    VAL A  90        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE A 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR B  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL B  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE B 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR C  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL C  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE C 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR D  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL D  90        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE D 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    LEU D 375        17.0      L          L   OUTSIDE RANGE
REMARK 500    THR E  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL E  90        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE E 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR F  79        24.1      L          L   OUTSIDE RANGE
REMARK 500    VAL F  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE F 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR G  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL G  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE G 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR H  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL H  90        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE H 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR I  79        24.3      L          L   OUTSIDE RANGE
REMARK 500    VAL I  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE I 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR J  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL J  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE J 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR K  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL K  90        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE K 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR L  79        24.1      L          L   OUTSIDE RANGE
REMARK 500    VAL L  90        23.6      L          L   OUTSIDE RANGE
REMARK 500    ILE L 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR M  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL M  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE M 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR N  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL N  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE N 333        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR O  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL O  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE O 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR P  79        24.1      L          L   OUTSIDE RANGE
REMARK 500    VAL P  90        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE P 333        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR Q  79        24.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS      61 CHIRALITY DEVIATIONS.
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 BO4 A2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 B2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 C2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 D2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 H2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 I2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 K2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 L2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 M2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 N2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 O2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 T2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-1622   RELATED DB: EMDB
REMARK 900 HELICAL RECONSTRUCTION OF RESPIRATORY SYNCYTIAL VIRUS
REMARK 900 N-RNA HELICES
DBREF  2WJ8 A    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 B    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 C    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 D    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 E    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 F    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 G    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 H    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 I    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 J    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 K    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 L    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 M    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 N    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 O    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 P    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 Q    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 R    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 S    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 T    1   391  UNP    P03418   NCAP_HRSVA       1    391
DBREF  2WJ8 a 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 b 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 c 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 d 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 e 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 f 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 g 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 h 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 i 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 j 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 k 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 l 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 m 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 n 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 o 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 p 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 q 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 r 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 s 1001  1007  PDB    2WJ8     2WJ8          1001   1007
DBREF  2WJ8 t 1001  1007  PDB    2WJ8     2WJ8          1001   1007
SEQRES   1 A  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 A  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 A  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 A  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 A  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 A  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 A  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 A  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 A  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 A  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 A  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 A  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 A  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 A  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 A  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 A  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 A  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 A  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 A  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 A  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 A  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 A  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 A  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 A  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 A  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 A  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 A  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 A  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 A  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 A  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 A  391  LEU
SEQRES   1 B  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 B  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 B  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 B  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 B  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 B  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 B  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 B  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 B  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 B  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 B  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 B  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 B  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 B  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 B  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 B  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 B  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 B  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 B  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 B  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 B  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 B  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 B  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 B  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 B  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 B  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 B  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 B  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 B  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 B  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 B  391  LEU
SEQRES   1 C  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 C  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 C  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 C  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 C  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 C  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 C  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 C  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 C  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 C  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 C  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 C  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 C  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 C  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 C  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 C  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 C  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 C  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 C  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 C  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 C  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 C  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 C  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 C  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 C  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 C  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 C  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 C  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 C  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 C  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 C  391  LEU
SEQRES   1 D  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 D  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 D  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 D  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 D  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 D  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 D  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 D  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 D  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 D  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 D  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 D  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 D  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 D  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 D  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 D  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 D  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 D  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 D  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 D  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 D  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 D  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 D  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 D  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 D  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 D  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 D  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 D  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 D  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 D  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 D  391  LEU
SEQRES   1 E  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 E  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 E  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 E  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 E  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 E  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 E  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 E  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 E  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 E  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 E  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 E  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 E  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 E  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 E  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 E  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 E  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 E  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 E  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 E  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 E  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 E  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 E  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 E  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 E  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 E  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 E  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 E  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 E  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 E  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 E  391  LEU
SEQRES   1 F  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 F  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 F  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 F  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 F  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 F  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 F  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 F  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 F  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 F  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 F  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 F  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 F  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 F  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 F  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 F  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 F  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 F  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 F  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 F  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 F  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 F  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 F  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 F  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 F  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 F  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 F  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 F  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 F  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 F  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 F  391  LEU
SEQRES   1 G  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 G  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 G  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 G  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 G  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 G  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 G  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 G  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 G  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 G  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 G  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 G  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 G  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 G  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 G  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 G  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 G  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 G  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 G  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 G  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 G  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 G  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 G  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 G  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 G  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 G  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 G  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 G  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 G  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 G  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 G  391  LEU
SEQRES   1 H  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 H  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 H  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 H  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 H  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 H  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 H  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 H  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 H  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 H  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 H  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 H  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 H  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 H  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 H  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 H  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 H  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 H  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 H  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 H  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 H  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 H  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 H  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 H  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 H  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 H  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 H  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 H  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 H  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 H  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 H  391  LEU
SEQRES   1 I  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 I  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 I  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 I  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 I  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 I  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 I  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 I  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 I  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 I  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 I  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 I  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 I  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 I  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 I  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 I  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 I  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 I  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 I  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 I  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 I  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 I  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 I  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 I  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 I  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 I  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 I  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 I  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 I  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 I  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 I  391  LEU
SEQRES   1 J  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 J  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 J  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 J  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 J  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 J  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 J  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 J  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 J  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 J  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 J  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 J  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 J  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 J  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 J  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 J  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 J  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 J  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 J  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 J  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 J  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 J  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 J  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 J  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 J  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 J  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 J  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 J  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 J  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 J  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 J  391  LEU
SEQRES   1 K  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 K  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 K  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 K  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 K  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 K  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 K  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 K  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 K  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 K  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 K  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 K  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 K  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 K  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 K  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 K  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 K  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 K  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 K  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 K  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 K  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 K  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 K  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 K  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 K  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 K  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 K  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 K  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 K  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 K  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 K  391  LEU
SEQRES   1 L  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 L  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 L  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 L  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 L  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 L  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 L  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 L  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 L  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 L  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 L  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 L  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 L  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 L  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 L  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 L  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 L  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 L  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 L  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 L  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 L  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 L  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 L  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 L  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 L  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 L  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 L  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 L  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 L  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 L  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 L  391  LEU
SEQRES   1 M  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 M  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 M  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 M  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 M  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 M  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 M  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 M  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 M  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 M  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 M  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 M  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 M  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 M  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 M  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 M  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 M  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 M  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 M  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 M  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 M  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 M  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 M  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 M  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 M  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 M  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 M  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 M  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 M  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 M  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 M  391  LEU
SEQRES   1 N  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 N  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 N  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 N  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 N  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 N  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 N  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 N  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 N  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 N  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 N  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 N  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 N  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 N  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 N  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 N  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 N  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 N  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 N  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 N  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 N  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 N  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 N  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 N  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 N  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 N  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 N  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 N  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 N  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 N  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 N  391  LEU
SEQRES   1 O  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 O  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 O  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 O  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 O  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 O  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 O  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 O  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 O  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 O  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 O  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 O  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 O  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 O  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 O  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 O  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 O  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 O  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 O  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 O  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 O  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 O  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 O  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 O  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 O  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 O  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 O  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 O  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 O  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 O  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 O  391  LEU
SEQRES   1 P  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 P  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 P  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 P  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 P  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 P  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 P  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 P  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 P  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 P  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 P  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 P  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 P  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 P  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 P  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 P  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 P  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 P  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 P  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 P  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 P  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 P  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 P  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 P  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 P  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 P  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 P  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 P  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 P  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 P  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 P  391  LEU
SEQRES   1 Q  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 Q  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 Q  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 Q  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 Q  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 Q  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 Q  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 Q  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 Q  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 Q  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 Q  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 Q  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 Q  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 Q  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 Q  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 Q  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 Q  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 Q  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 Q  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 Q  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 Q  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 Q  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 Q  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 Q  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 Q  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 Q  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 Q  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 Q  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 Q  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 Q  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 Q  391  LEU
SEQRES   1 R  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 R  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 R  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 R  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 R  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 R  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 R  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 R  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 R  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 R  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 R  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 R  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 R  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 R  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 R  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 R  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 R  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 R  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 R  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 R  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 R  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 R  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 R  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 R  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 R  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 R  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 R  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 R  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 R  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 R  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 R  391  LEU
SEQRES   1 S  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 S  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 S  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 S  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 S  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 S  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 S  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 S  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 S  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 S  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 S  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 S  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 S  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 S  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 S  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 S  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 S  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 S  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 S  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 S  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 S  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 S  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 S  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 S  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 S  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 S  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 S  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 S  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 S  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 S  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 S  391  LEU
SEQRES   1 T  391  MET ALA LEU SER LYS VAL LYS LEU ASN ASP THR LEU ASN
SEQRES   2 T  391  LYS ASP GLN LEU LEU SER SER SER LYS TYR THR ILE GLN
SEQRES   3 T  391  ARG SER THR GLY ASP SER ILE ASP THR PRO ASN TYR ASP
SEQRES   4 T  391  VAL GLN LYS HIS ILE ASN LYS LEU CYS GLY MET LEU LEU
SEQRES   5 T  391  ILE THR GLU ASP ALA ASN HIS LYS PHE THR GLY LEU ILE
SEQRES   6 T  391  GLY MET LEU TYR ALA MET SER ARG LEU GLY ARG GLU ASP
SEQRES   7 T  391  THR ILE LYS ILE LEU ARG ASP ALA GLY TYR HIS VAL LYS
SEQRES   8 T  391  ALA ASN GLY VAL ASP VAL THR THR HIS ARG GLN ASP ILE
SEQRES   9 T  391  ASN GLY LYS GLU MET LYS PHE GLU VAL LEU THR LEU ALA
SEQRES  10 T  391  SER LEU THR THR GLU ILE GLN ILE ASN ILE GLU ILE GLU
SEQRES  11 T  391  SER ARG LYS SER TYR LYS LYS MET LEU LYS GLU MET GLY
SEQRES  12 T  391  GLU VAL ALA PRO GLU TYR ARG HIS ASP SER PRO ASP CYS
SEQRES  13 T  391  GLY MET ILE ILE LEU CYS ILE ALA ALA LEU VAL ILE THR
SEQRES  14 T  391  LYS LEU ALA ALA GLY ASP ARG SER GLY LEU THR ALA VAL
SEQRES  15 T  391  ILE ARG ARG ALA ASN ASN VAL LEU LYS ASN GLU MET LYS
SEQRES  16 T  391  ARG TYR LYS GLY LEU LEU PRO LYS ASP ILE ALA ASN SER
SEQRES  17 T  391  PHE TYR GLU VAL PHE GLU LYS HIS PRO HIS PHE ILE ASP
SEQRES  18 T  391  VAL PHE VAL HIS PHE GLY ILE ALA GLN SER SER THR ARG
SEQRES  19 T  391  GLY GLY SER ARG VAL GLU GLY ILE PHE ALA GLY LEU PHE
SEQRES  20 T  391  MET ASN ALA TYR GLY ALA GLY GLN VAL MET LEU ARG TRP
SEQRES  21 T  391  GLY VAL LEU ALA LYS SER VAL LYS ASN ILE MET LEU GLY
SEQRES  22 T  391  HIS ALA SER VAL GLN ALA GLU MET GLU GLN VAL VAL GLU
SEQRES  23 T  391  VAL TYR GLU TYR ALA GLN LYS LEU GLY GLY GLU ALA GLY
SEQRES  24 T  391  PHE TYR HIS ILE LEU ASN ASN PRO LYS ALA SER LEU LEU
SEQRES  25 T  391  SER LEU THR GLN PHE PRO HIS PHE SER SER VAL VAL LEU
SEQRES  26 T  391  GLY ASN ALA ALA GLY LEU GLY ILE MET GLY GLU TYR ARG
SEQRES  27 T  391  GLY THR PRO ARG ASN GLN ASP LEU TYR ASP ALA ALA LYS
SEQRES  28 T  391  ALA TYR ALA GLU GLN LEU LYS GLU ASN GLY VAL ILE ASN
SEQRES  29 T  391  TYR SER VAL LEU ASP LEU THR ALA GLU GLU LEU GLU ALA
SEQRES  30 T  391  ILE LYS HIS GLN LEU ASN PRO LYS ASP ASN ASP VAL GLU
SEQRES  31 T  391  LEU
SEQRES   1 a    7    C   C   C   C   C   C   C
SEQRES   1 b    7    C   C   C   C   C   C   C
SEQRES   1 c    7    C   C   C   C   C   C   C
SEQRES   1 d    7    C   C   C   C   C   C   C
SEQRES   1 e    7    C   C   C   C   C   C   C
SEQRES   1 f    7    C   C   C   C   C   C   C
SEQRES   1 g    7    C   C   C   C   C   C   C
SEQRES   1 h    7    C   C   C   C   C   C   C
SEQRES   1 i    7    C   C   C   C   C   C   C
SEQRES   1 j    7    C   C   C   C   C   C   C
SEQRES   1 k    7    C   C   C   C   C   C   C
SEQRES   1 l    7    C   C   C   C   C   C   C
SEQRES   1 m    7    C   C   C   C   C   C   C
SEQRES   1 n    7    C   C   C   C   C   C   C
SEQRES   1 o    7    C   C   C   C   C   C   C
SEQRES   1 p    7    C   C   C   C   C   C   C
SEQRES   1 q    7    C   C   C   C   C   C   C
SEQRES   1 r    7    C   C   C   C   C   C   C
SEQRES   1 s    7    C   C   C   C   C   C   C
SEQRES   1 t    7    C   C   C   C   C   C   C
HET    BO4  A2001       5
HET    BO4  B2001       5
HET    BO4  C2001       5
HET    BO4  D2001       5
HET    BO4  H2001       5
HET    BO4  I2001       5
HET    BO4  K2001       5
HET    BO4  L2001       5
HET    BO4  M2001       5
HET    BO4  N2001       5
HET    BO4  O2001       5
HET    BO4  T2001       5
HETNAM     BO4 BORATE ION
FORMUL  41  BO4    12(B H4 O4 1-)
FORMUL  42  HOH   *685(H2 O1)
HELIX    1   1 ASN A    9  SER A   20  1                                  12
HELIX    2   2 ASN A   37  ASP A   39  5                                   3
HELIX    3   3 VAL A   40  THR A   54  1                                  15
HELIX    4   4 PHE A   61  GLY A   75  1                                  15
HELIX    5   5 GLY A   75  GLY A   87  1                                  13
HELIX    6   6 THR A  120  GLY A  143  1                                  24
HELIX    7   7 PRO A  154  LYS A  170  1                                  17
HELIX    8   8 LEU A  171  GLY A  174  5                                   4
HELIX    9   9 GLY A  178  VAL A  189  1                                  12
HELIX   10  10 LEU A  190  TYR A  197  1                                   8
HELIX   11  11 LEU A  201  HIS A  216  1                                  16
HELIX   12  12 HIS A  216  SER A  231  1                                  16
HELIX   13  13 SER A  237  ASN A  249  1                                  13
HELIX   14  14 GLN A  255  VAL A  267  1                                  13
HELIX   15  15 ASN A  269  GLY A  273  5                                   5
HELIX   16  16 HIS A  274  GLY A  295  1                                  22
HELIX   17  17 GLY A  296  TYR A  301  5                                   6
HELIX   18  18 ASN A  306  SER A  313  5                                   8
HELIX   19  19 PHE A  317  LEU A  331  1                                  15
HELIX   20  20 ASN A  343  LYS A  358  1                                  16
HELIX   21  21 ASN B    9  SER B   20  1                                  12
HELIX   22  22 ASN B   37  ASP B   39  5                                   3
HELIX   23  23 VAL B   40  THR B   54  1                                  15
HELIX   24  24 PHE B   61  GLY B   75  1                                  15
HELIX   25  25 GLY B   75  GLY B   87  1                                  13
HELIX   26  26 THR B  120  GLY B  143  1                                  24
HELIX   27  27 PRO B  154  LYS B  170  1                                  17
HELIX   28  28 LEU B  171  GLY B  174  5                                   4
HELIX   29  29 GLY B  178  VAL B  189  1                                  12
HELIX   30  30 LEU B  190  TYR B  197  1                                   8
HELIX   31  31 LEU B  201  HIS B  216  1                                  16
HELIX   32  32 HIS B  216  SER B  231  1                                  16
HELIX   33  33 SER B  237  ASN B  249  1                                  13
HELIX   34  34 GLN B  255  VAL B  267  1                                  13
HELIX   35  35 ASN B  269  GLY B  273  5                                   5
HELIX   36  36 HIS B  274  GLY B  295  1                                  22
HELIX   37  37 GLY B  296  TYR B  301  5                                   6
HELIX   38  38 ASN B  306  SER B  313  5                                   8
HELIX   39  39 PHE B  317  LEU B  331  1                                  15
HELIX   40  40 ASN B  343  LYS B  358  1                                  16
HELIX   41  41 ASN C    9  SER C   20  1                                  12
HELIX   42  42 ASN C   37  ASP C   39  5                                   3
HELIX   43  43 VAL C   40  THR C   54  1                                  15
HELIX   44  44 PHE C   61  GLY C   75  1                                  15
HELIX   45  45 GLY C   75  GLY C   87  1                                  13
HELIX   46  46 THR C  120  GLY C  143  1                                  24
HELIX   47  47 PRO C  154  LYS C  170  1                                  17
HELIX   48  48 LEU C  171  GLY C  174  5                                   4
HELIX   49  49 GLY C  178  VAL C  189  1                                  12
HELIX   50  50 LEU C  190  TYR C  197  1                                   8
HELIX   51  51 LEU C  201  HIS C  216  1                                  16
HELIX   52  52 HIS C  216  SER C  231  1                                  16
HELIX   53  53 SER C  237  ASN C  249  1                                  13
HELIX   54  54 GLN C  255  VAL C  267  1                                  13
HELIX   55  55 ASN C  269  GLY C  273  5                                   5
HELIX   56  56 HIS C  274  GLY C  295  1                                  22
HELIX   57  57 GLY C  296  TYR C  301  5                                   6
HELIX   58  58 ASN C  306  SER C  313  5                                   8
HELIX   59  59 PHE C  317  LEU C  331  1                                  15
HELIX   60  60 ASN C  343  LYS C  358  1                                  16
HELIX   61  61 ASN D    9  SER D   20  1                                  12
HELIX   62  62 ASN D   37  ASP D   39  5                                   3
HELIX   63  63 VAL D   40  THR D   54  1                                  15
HELIX   64  64 PHE D   61  GLY D   75  1                                  15
HELIX   65  65 GLY D   75  GLY D   87  1                                  13
HELIX   66  66 THR D  120  GLY D  143  1                                  24
HELIX   67  67 PRO D  154  LYS D  170  1                                  17
HELIX   68  68 LEU D  171  GLY D  174  5                                   4
HELIX   69  69 GLY D  178  VAL D  189  1                                  12
HELIX   70  70 LEU D  190  TYR D  197  1                                   8
HELIX   71  71 LEU D  201  HIS D  216  1                                  16
HELIX   72  72 HIS D  216  SER D  231  1                                  16
HELIX   73  73 SER D  237  ASN D  249  1                                  13
HELIX   74  74 GLN D  255  VAL D  267  1                                  13
HELIX   75  75 ASN D  269  GLY D  273  5                                   5
HELIX   76  76 HIS D  274  GLY D  295  1                                  22
HELIX   77  77 GLY D  296  TYR D  301  5                                   6
HELIX   78  78 ASN D  306  SER D  313  5                                   8
HELIX   79  79 PHE D  317  LEU D  331  1                                  15
HELIX   80  80 ASN D  343  LYS D  358  1                                  16
HELIX   81  81 ASN E    9  SER E   20  1                                  12
HELIX   82  82 ASN E   37  ASP E   39  5                                   3
HELIX   83  83 VAL E   40  THR E   54  1                                  15
HELIX   84  84 PHE E   61  GLY E   75  1                                  15
HELIX   85  85 GLY E   75  GLY E   87  1                                  13
HELIX   86  86 THR E  120  GLY E  143  1                                  24
HELIX   87  87 PRO E  154  LYS E  170  1                                  17
HELIX   88  88 LEU E  171  GLY E  174  5                                   4
HELIX   89  89 GLY E  178  VAL E  189  1                                  12
HELIX   90  90 LEU E  190  TYR E  197  1                                   8
HELIX   91  91 LEU E  201  HIS E  216  1                                  16
HELIX   92  92 HIS E  216  SER E  231  1                                  16
HELIX   93  93 SER E  237  ASN E  249  1                                  13
HELIX   94  94 GLN E  255  VAL E  267  1                                  13
HELIX   95  95 ASN E  269  GLY E  273  5                                   5
HELIX   96  96 HIS E  274  GLY E  295  1                                  22
HELIX   97  97 GLY E  296  TYR E  301  5                                   6
HELIX   98  98 ASN E  306  SER E  313  5                                   8
HELIX   99  99 PHE E  317  LEU E  331  1                                  15
HELIX  100 100 ASN E  343  LYS E  358  1                                  16
HELIX  101 101 ASN F    9  SER F   20  1                                  12
HELIX  102 102 ASN F   37  ASP F   39  5                                   3
HELIX  103 103 VAL F   40  THR F   54  1                                  15
HELIX  104 104 PHE F   61  GLY F   75  1                                  15
HELIX  105 105 GLY F   75  GLY F   87  1                                  13
HELIX  106 106 THR F  120  GLY F  143  1                                  24
HELIX  107 107 PRO F  154  LYS F  170  1                                  17
HELIX  108 108 LEU F  171  GLY F  174  5                                   4
HELIX  109 109 GLY F  178  VAL F  189  1                                  12
HELIX  110 110 LEU F  190  TYR F  197  1                                   8
HELIX  111 111 LEU F  201  HIS F  216  1                                  16
HELIX  112 112 HIS F  216  SER F  231  1                                  16
HELIX  113 113 SER F  237  ASN F  249  1                                  13
HELIX  114 114 GLN F  255  VAL F  267  1                                  13
HELIX  115 115 ASN F  269  GLY F  273  5                                   5
HELIX  116 116 HIS F  274  GLY F  295  1                                  22
HELIX  117 117 GLY F  296  TYR F  301  5                                   6
HELIX  118 118 ASN F  306  SER F  313  5                                   8
HELIX  119 119 PHE F  317  LEU F  331  1                                  15
HELIX  120 120 ASN F  343  LYS F  358  1                                  16
HELIX  121 121 ASN G    9  SER G   20  1                                  12
HELIX  122 122 ASN G   37  ASP G   39  5                                   3
HELIX  123 123 VAL G   40  THR G   54  1                                  15
HELIX  124 124 PHE G   61  GLY G   75  1                                  15
HELIX  125 125 GLY G   75  GLY G   87  1                                  13
HELIX  126 126 THR G  120  GLY G  143  1                                  24
HELIX  127 127 PRO G  154  LYS G  170  1                                  17
HELIX  128 128 LEU G  171  GLY G  174  5                                   4
HELIX  129 129 GLY G  178  VAL G  189  1                                  12
HELIX  130 130 LEU G  190  TYR G  197  1                                   8
HELIX  131 131 LEU G  201  HIS G  216  1                                  16
HELIX  132 132 HIS G  216  SER G  231  1                                  16
HELIX  133 133 SER G  237  ASN G  249  1                                  13
HELIX  134 134 GLN G  255  VAL G  267  1                                  13
HELIX  135 135 ASN G  269  GLY G  273  5                                   5
HELIX  136 136 HIS G  274  GLY G  295  1                                  22
HELIX  137 137 GLY G  296  TYR G  301  5                                   6
HELIX  138 138 ASN G  306  SER G  313  5                                   8
HELIX  139 139 PHE G  317  LEU G  331  1                                  15
HELIX  140 140 ASN G  343  LYS G  358  1                                  16
HELIX  141 141 ASN H    9  SER H   20  1                                  12
HELIX  142 142 ASN H   37  ASP H   39  5                                   3
HELIX  143 143 VAL H   40  THR H   54  1                                  15
HELIX  144 144 PHE H   61  GLY H   75  1                                  15
HELIX  145 145 GLY H   75  GLY H   87  1                                  13
HELIX  146 146 THR H  120  GLY H  143  1                                  24
HELIX  147 147 PRO H  154  LYS H  170  1                                  17
HELIX  148 148 LEU H  171  GLY H  174  5                                   4
HELIX  149 149 GLY H  178  VAL H  189  1                                  12
HELIX  150 150 LEU H  190  TYR H  197  1                                   8
HELIX  151 151 LEU H  201  HIS H  216  1                                  16
HELIX  152 152 HIS H  216  SER H  231  1                                  16
HELIX  153 153 SER H  237  ASN H  249  1                                  13
HELIX  154 154 GLN H  255  VAL H  267  1                                  13
HELIX  155 155 ASN H  269  GLY H  273  5                                   5
HELIX  156 156 HIS H  274  GLY H  295  1                                  22
HELIX  157 157 GLY H  296  TYR H  301  5                                   6
HELIX  158 158 ASN H  306  SER H  313  5                                   8
HELIX  159 159 PHE H  317  LEU H  331  1                                  15
HELIX  160 160 ASN H  343  LYS H  358  1                                  16
HELIX  161 161 ASN I    9  SER I   20  1                                  12
HELIX  162 162 ASN I   37  ASP I   39  5                                   3
HELIX  163 163 VAL I   40  THR I   54  1                                  15
HELIX  164 164 PHE I   61  GLY I   75  1                                  15
HELIX  165 165 GLY I   75  GLY I   87  1                                  13
HELIX  166 166 THR I  120  GLY I  143  1                                  24
HELIX  167 167 PRO I  154  LYS I  170  1                                  17
HELIX  168 168 LEU I  171  GLY I  174  5                                   4
HELIX  169 169 GLY I  178  VAL I  189  1                                  12
HELIX  170 170 LEU I  190  TYR I  197  1                                   8
HELIX  171 171 LEU I  201  HIS I  216  1                                  16
HELIX  172 172 HIS I  216  SER I  231  1                                  16
HELIX  173 173 SER I  237  ASN I  249  1                                  13
HELIX  174 174 GLN I  255  VAL I  267  1                                  13
HELIX  175 175 ASN I  269  GLY I  273  5                                   5
HELIX  176 176 HIS I  274  GLY I  295  1                                  22
HELIX  177 177 GLY I  296  TYR I  301  5                                   6
HELIX  178 178 ASN I  306  SER I  313  5                                   8
HELIX  179 179 PHE I  317  LEU I  331  1                                  15
HELIX  180 180 ASN I  343  LYS I  358  1                                  16
HELIX  181 181 ASN J    9  SER J   20  1                                  12
HELIX  182 182 ASN J   37  ASP J   39  5                                   3
HELIX  183 183 VAL J   40  THR J   54  1                                  15
HELIX  184 184 PHE J   61  GLY J   75  1                                  15
HELIX  185 185 GLY J   75  GLY J   87  1                                  13
HELIX  186 186 THR J  120  GLY J  143  1                                  24
HELIX  187 187 PRO J  154  LYS J  170  1                                  17
HELIX  188 188 LEU J  171  GLY J  174  5                                   4
HELIX  189 189 GLY J  178  VAL J  189  1                                  12
HELIX  190 190 LEU J  190  TYR J  197  1                                   8
HELIX  191 191 LEU J  201  HIS J  216  1                                  16
HELIX  192 192 HIS J  216  SER J  231  1                                  16
HELIX  193 193 SER J  237  ASN J  249  1                                  13
HELIX  194 194 GLN J  255  VAL J  267  1                                  13
HELIX  195 195 ASN J  269  GLY J  273  5                                   5
HELIX  196 196 HIS J  274  GLY J  295  1                                  22
HELIX  197 197 GLY J  296  TYR J  301  5                                   6
HELIX  198 198 ASN J  306  SER J  313  5                                   8
HELIX  199 199 PHE J  317  LEU J  331  1                                  15
HELIX  200 200 ASN J  343  LYS J  358  1                                  16
HELIX  201 201 ASN K    9  SER K   20  1                                  12
HELIX  202 202 ASN K   37  ASP K   39  5                                   3
HELIX  203 203 VAL K   40  THR K   54  1                                  15
HELIX  204 204 PHE K   61  GLY K   75  1                                  15
HELIX  205 205 GLY K   75  GLY K   87  1                                  13
HELIX  206 206 THR K  120  GLY K  143  1                                  24
HELIX  207 207 PRO K  154  LYS K  170  1                                  17
HELIX  208 208 LEU K  171  GLY K  174  5                                   4
HELIX  209 209 GLY K  178  VAL K  189  1                                  12
HELIX  210 210 LEU K  190  TYR K  197  1                                   8
HELIX  211 211 LEU K  201  HIS K  216  1                                  16
HELIX  212 212 HIS K  216  SER K  231  1                                  16
HELIX  213 213 SER K  237  ASN K  249  1                                  13
HELIX  214 214 GLN K  255  VAL K  267  1                                  13
HELIX  215 215 ASN K  269  GLY K  273  5                                   5
HELIX  216 216 HIS K  274  GLY K  295  1                                  22
HELIX  217 217 GLY K  296  TYR K  301  5                                   6
HELIX  218 218 ASN K  306  SER K  313  5                                   8
HELIX  219 219 PHE K  317  LEU K  331  1                                  15
HELIX  220 220 ASN K  343  LYS K  358  1                                  16
HELIX  221 221 ASN L    9  SER L   20  1                                  12
HELIX  222 222 ASN L   37  ASP L   39  5                                   3
HELIX  223 223 VAL L   40  THR L   54  1                                  15
HELIX  224 224 PHE L   61  GLY L   75  1                                  15
HELIX  225 225 GLY L   75  GLY L   87  1                                  13
HELIX  226 226 THR L  120  GLY L  143  1                                  24
HELIX  227 227 PRO L  154  LYS L  170  1                                  17
HELIX  228 228 LEU L  171  GLY L  174  5                                   4
HELIX  229 229 GLY L  178  VAL L  189  1                                  12
HELIX  230 230 LEU L  190  TYR L  197  1                                   8
HELIX  231 231 LEU L  201  HIS L  216  1                                  16
HELIX  232 232 HIS L  216  SER L  231  1                                  16
HELIX  233 233 SER L  237  ASN L  249  1                                  13
HELIX  234 234 GLN L  255  VAL L  267  1                                  13
HELIX  235 235 ASN L  269  GLY L  273  5                                   5
HELIX  236 236 HIS L  274  GLY L  295  1                                  22
HELIX  237 237 GLY L  296  TYR L  301  5                                   6
HELIX  238 238 ASN L  306  SER L  313  5                                   8
HELIX  239 239 PHE L  317  LEU L  331  1                                  15
HELIX  240 240 ASN L  343  LYS L  358  1                                  16
HELIX  241 241 ASN M    9  SER M   20  1                                  12
HELIX  242 242 ASN M   37  ASP M   39  5                                   3
HELIX  243 243 VAL M   40  THR M   54  1                                  15
HELIX  244 244 PHE M   61  GLY M   75  1                                  15
HELIX  245 245 GLY M   75  GLY M   87  1                                  13
HELIX  246 246 THR M  120  GLY M  143  1                                  24
HELIX  247 247 PRO M  154  LYS M  170  1                                  17
HELIX  248 248 LEU M  171  GLY M  174  5                                   4
HELIX  249 249 GLY M  178  VAL M  189  1                                  12
HELIX  250 250 LEU M  190  TYR M  197  1                                   8
HELIX  251 251 LEU M  201  HIS M  216  1                                  16
HELIX  252 252 HIS M  216  SER M  231  1                                  16
HELIX  253 253 SER M  237  ASN M  249  1                                  13
HELIX  254 254 GLN M  255  VAL M  267  1                                  13
HELIX  255 255 ASN M  269  GLY M  273  5                                   5
HELIX  256 256 HIS M  274  GLY M  295  1                                  22
HELIX  257 257 GLY M  296  TYR M  301  5                                   6
HELIX  258 258 ASN M  306  SER M  313  5                                   8
HELIX  259 259 PHE M  317  LEU M  331  1                                  15
HELIX  260 260 ASN M  343  LYS M  358  1                                  16
HELIX  261 261 ASN N    9  SER N   20  1                                  12
HELIX  262 262 ASN N   37  ASP N   39  5                                   3
HELIX  263 263 VAL N   40  THR N   54  1                                  15
HELIX  264 264 PHE N   61  GLY N   75  1                                  15
HELIX  265 265 GLY N   75  GLY N   87  1                                  13
HELIX  266 266 THR N  120  GLY N  143  1                                  24
HELIX  267 267 PRO N  154  LYS N  170  1                                  17
HELIX  268 268 LEU N  171  GLY N  174  5                                   4
HELIX  269 269 GLY N  178  VAL N  189  1                                  12
HELIX  270 270 LEU N  190  TYR N  197  1                                   8
HELIX  271 271 LEU N  201  HIS N  216  1                                  16
HELIX  272 272 HIS N  216  SER N  231  1                                  16
HELIX  273 273 SER N  237  ASN N  249  1                                  13
HELIX  274 274 GLN N  255  VAL N  267  1                                  13
HELIX  275 275 ASN N  269  GLY N  273  5                                   5
HELIX  276 276 HIS N  274  GLY N  295  1                                  22
HELIX  277 277 GLY N  296  TYR N  301  5                                   6
HELIX  278 278 ASN N  306  SER N  313  5                                   8
HELIX  279 279 PHE N  317  LEU N  331  1                                  15
HELIX  280 280 ASN N  343  LYS N  358  1                                  16
HELIX  281 281 GLU N  374  LYS N  379  1                                   6
HELIX  282 282 ASN O    9  SER O   20  1                                  12
HELIX  283 283 ASN O   37  ASP O   39  5                                   3
HELIX  284 284 VAL O   40  THR O   54  1                                  15
HELIX  285 285 PHE O   61  GLY O   75  1                                  15
HELIX  286 286 GLY O   75  GLY O   87  1                                  13
HELIX  287 287 THR O  120  GLY O  143  1                                  24
HELIX  288 288 PRO O  154  LYS O  170  1                                  17
HELIX  289 289 LEU O  171  GLY O  174  5                                   4
HELIX  290 290 GLY O  178  VAL O  189  1                                  12
HELIX  291 291 LEU O  190  TYR O  197  1                                   8
HELIX  292 292 LEU O  201  HIS O  216  1                                  16
HELIX  293 293 HIS O  216  SER O  231  1                                  16
HELIX  294 294 SER O  237  ASN O  249  1                                  13
HELIX  295 295 GLN O  255  VAL O  267  1                                  13
HELIX  296 296 ASN O  269  GLY O  273  5                                   5
HELIX  297 297 HIS O  274  GLY O  295  1                                  22
HELIX  298 298 GLY O  296  TYR O  301  5                                   6
HELIX  299 299 ASN O  306  SER O  313  5                                   8
HELIX  300 300 PHE O  317  LEU O  331  1                                  15
HELIX  301 301 ASN O  343  LYS O  358  1                                  16
HELIX  302 302 ASN P    9  SER P   20  1                                  12
HELIX  303 303 ASN P   37  ASP P   39  5                                   3
HELIX  304 304 VAL P   40  THR P   54  1                                  15
HELIX  305 305 PHE P   61  GLY P   75  1                                  15
HELIX  306 306 GLY P   75  GLY P   87  1                                  13
HELIX  307 307 THR P  120  GLY P  143  1                                  24
HELIX  308 308 PRO P  154  LYS P  170  1                                  17
HELIX  309 309 LEU P  171  GLY P  174  5                                   4
HELIX  310 310 GLY P  178  VAL P  189  1                                  12
HELIX  311 311 LEU P  190  TYR P  197  1                                   8
HELIX  312 312 LEU P  201  HIS P  216  1                                  16
HELIX  313 313 HIS P  216  SER P  231  1                                  16
HELIX  314 314 SER P  237  ASN P  249  1                                  13
HELIX  315 315 GLN P  255  VAL P  267  1                                  13
HELIX  316 316 ASN P  269  GLY P  273  5                                   5
HELIX  317 317 HIS P  274  GLY P  295  1                                  22
HELIX  318 318 GLY P  296  TYR P  301  5                                   6
HELIX  319 319 ASN P  306  SER P  313  5                                   8
HELIX  320 320 PHE P  317  LEU P  331  1                                  15
HELIX  321 321 ASN P  343  LYS P  358  1                                  16
HELIX  322 322 ASN Q    9  SER Q   20  1                                  12
HELIX  323 323 ASN Q   37  ASP Q   39  5                                   3
HELIX  324 324 VAL Q   40  THR Q   54  1                                  15
HELIX  325 325 PHE Q   61  GLY Q   75  1                                  15
HELIX  326 326 GLY Q   75  GLY Q   87  1                                  13
HELIX  327 327 THR Q  120  GLY Q  143  1                                  24
HELIX  328 328 PRO Q  154  LYS Q  170  1                                  17
HELIX  329 329 LEU Q  171  GLY Q  174  5                                   4
HELIX  330 330 GLY Q  178  VAL Q  189  1                                  12
HELIX  331 331 LEU Q  190  TYR Q  197  1                                   8
HELIX  332 332 LEU Q  201  HIS Q  216  1                                  16
HELIX  333 333 HIS Q  216  SER Q  231  1                                  16
HELIX  334 334 SER Q  237  ASN Q  249  1                                  13
HELIX  335 335 GLN Q  255  VAL Q  267  1                                  13
HELIX  336 336 ASN Q  269  GLY Q  273  5                                   5
HELIX  337 337 HIS Q  274  GLY Q  295  1                                  22
HELIX  338 338 GLY Q  296  TYR Q  301  5                                   6
HELIX  339 339 ASN Q  306  SER Q  313  5                                   8
HELIX  340 340 PHE Q  317  LEU Q  331  1                                  15
HELIX  341 341 ASN Q  343  LYS Q  358  1                                  16
HELIX  342 342 ASN R    9  SER R   20  1                                  12
HELIX  343 343 ASN R   37  ASP R   39  5                                   3
HELIX  344 344 VAL R   40  THR R   54  1                                  15
HELIX  345 345 PHE R   61  GLY R   75  1                                  15
HELIX  346 346 GLY R   75  GLY R   87  1                                  13
HELIX  347 347 THR R  120  GLY R  143  1                                  24
HELIX  348 348 PRO R  154  LYS R  170  1                                  17
HELIX  349 349 LEU R  171  GLY R  174  5                                   4
HELIX  350 350 GLY R  178  VAL R  189  1                                  12
HELIX  351 351 LEU R  190  TYR R  197  1                                   8
HELIX  352 352 LEU R  201  HIS R  216  1                                  16
HELIX  353 353 HIS R  216  SER R  231  1                                  16
HELIX  354 354 SER R  237  ASN R  249  1                                  13
HELIX  355 355 GLN R  255  VAL R  267  1                                  13
HELIX  356 356 ASN R  269  GLY R  273  5                                   5
HELIX  357 357 HIS R  274  GLY R  295  1                                  22
HELIX  358 358 GLY R  296  TYR R  301  5                                   6
HELIX  359 359 ASN R  306  SER R  313  5                                   8
HELIX  360 360 PHE R  317  LEU R  331  1                                  15
HELIX  361 361 ASN R  343  LYS R  358  1                                  16
HELIX  362 362 ASN S    9  SER S   20  1                                  12
HELIX  363 363 ASN S   37  ASP S   39  5                                   3
HELIX  364 364 VAL S   40  THR S   54  1                                  15
HELIX  365 365 PHE S   61  GLY S   75  1                                  15
HELIX  366 366 GLY S   75  GLY S   87  1                                  13
HELIX  367 367 THR S  120  GLY S  143  1                                  24
HELIX  368 368 PRO S  154  LYS S  170  1                                  17
HELIX  369 369 LEU S  171  GLY S  174  5                                   4
HELIX  370 370 GLY S  178  VAL S  189  1                                  12
HELIX  371 371 LEU S  190  TYR S  197  1                                   8
HELIX  372 372 LEU S  201  HIS S  216  1                                  16
HELIX  373 373 HIS S  216  SER S  231  1                                  16
HELIX  374 374 SER S  237  ASN S  249  1                                  13
HELIX  375 375 GLN S  255  VAL S  267  1                                  13
HELIX  376 376 ASN S  269  GLY S  273  5                                   5
HELIX  377 377 HIS S  274  GLY S  295  1                                  22
HELIX  378 378 GLY S  296  TYR S  301  5                                   6
HELIX  379 379 ASN S  306  SER S  313  5                                   8
HELIX  380 380 PHE S  317  LEU S  331  1                                  15
HELIX  381 381 ASN S  343  LYS S  358  1                                  16
HELIX  382 382 GLU S  374  LYS S  379  1                                   6
HELIX  383 383 ASN T    9  SER T   20  1                                  12
HELIX  384 384 ASN T   37  ASP T   39  5                                   3
HELIX  385 385 VAL T   40  THR T   54  1                                  15
HELIX  386 386 PHE T   61  GLY T   75  1                                  15
HELIX  387 387 GLY T   75  GLY T   87  1                                  13
HELIX  388 388 THR T  120  GLY T  143  1                                  24
HELIX  389 389 PRO T  154  LYS T  170  1                                  17
HELIX  390 390 LEU T  171  GLY T  174  5                                   4
HELIX  391 391 GLY T  178  VAL T  189  1                                  12
HELIX  392 392 LEU T  190  TYR T  197  1                                   8
HELIX  393 393 LEU T  201  HIS T  216  1                                  16
HELIX  394 394 HIS T  216  SER T  231  1                                  16
HELIX  395 395 SER T  237  ASN T  249  1                                  13
HELIX  396 396 GLN T  255  VAL T  267  1                                  13
HELIX  397 397 ASN T  269  GLY T  273  5                                   5
HELIX  398 398 HIS T  274  GLY T  295  1                                  22
HELIX  399 399 GLY T  296  TYR T  301  5                                   6
HELIX  400 400 ASN T  306  SER T  313  5                                   8
HELIX  401 401 PHE T  317  LEU T  331  1                                  15
HELIX  402 402 ASN T  343  LYS T  358  1                                  16
SHEET    1  AA 2 ARG A  27  SER A  28  0
SHEET    2  AA 2 TYR A  88  HIS A  89  1  N  HIS A  89   O  ARG A  27
SHEET    1  AB 2 ILE A  33  THR A  35  0
SHEET    2  AB 2 ALA A  92  GLY A  94  1  O  ASN A  93   N  THR A  35
SHEET    1  AC 2 VAL A  97  ILE A 104  0
SHEET    2  AC 2 LYS A 107  LEU A 114 -1  O  LYS A 107   N  ILE A 104
SHEET    1  BA 2 ARG B  27  SER B  28  0
SHEET    2  BA 2 TYR B  88  HIS B  89  1  N  HIS B  89   O  ARG B  27
SHEET    1  BB 2 ILE B  33  THR B  35  0
SHEET    2  BB 2 ALA B  92  GLY B  94  1  O  ASN B  93   N  THR B  35
SHEET    1  BC 2 VAL B  97  ILE B 104  0
SHEET    2  BC 2 LYS B 107  LEU B 114 -1  O  LYS B 107   N  ILE B 104
SHEET    1  CA 2 ARG C  27  SER C  28  0
SHEET    2  CA 2 TYR C  88  HIS C  89  1  N  HIS C  89   O  ARG C  27
SHEET    1  CB 2 ILE C  33  THR C  35  0
SHEET    2  CB 2 ALA C  92  GLY C  94  1  O  ASN C  93   N  THR C  35
SHEET    1  CC 2 VAL C  97  ILE C 104  0
SHEET    2  CC 2 LYS C 107  LEU C 114 -1  O  LYS C 107   N  ILE C 104
SHEET    1  DA 2 ARG D  27  SER D  28  0
SHEET    2  DA 2 TYR D  88  HIS D  89  1  N  HIS D  89   O  ARG D  27
SHEET    1  DB 2 ILE D  33  THR D  35  0
SHEET    2  DB 2 ALA D  92  GLY D  94  1  O  ASN D  93   N  THR D  35
SHEET    1  DC 2 VAL D  97  ILE D 104  0
SHEET    2  DC 2 LYS D 107  LEU D 114 -1  O  LYS D 107   N  ILE D 104
SHEET    1  EA 2 ARG E  27  SER E  28  0
SHEET    2  EA 2 TYR E  88  HIS E  89  1  N  HIS E  89   O  ARG E  27
SHEET    1  EB 2 ILE E  33  THR E  35  0
SHEET    2  EB 2 ALA E  92  GLY E  94  1  O  ASN E  93   N  THR E  35
SHEET    1  EC 2 VAL E  97  ILE E 104  0
SHEET    2  EC 2 LYS E 107  LEU E 114 -1  O  LYS E 107   N  ILE E 104
SHEET    1  FA 2 ARG F  27  SER F  28  0
SHEET    2  FA 2 TYR F  88  HIS F  89  1  N  HIS F  89   O  ARG F  27
SHEET    1  FB 2 ILE F  33  THR F  35  0
SHEET    2  FB 2 ALA F  92  GLY F  94  1  O  ASN F  93   N  THR F  35
SHEET    1  FC 2 VAL F  97  ILE F 104  0
SHEET    2  FC 2 LYS F 107  LEU F 114 -1  O  LYS F 107   N  ILE F 104
SHEET    1  GA 2 ARG G  27  SER G  28  0
SHEET    2  GA 2 TYR G  88  HIS G  89  1  N  HIS G  89   O  ARG G  27
SHEET    1  GB 2 ILE G  33  THR G  35  0
SHEET    2  GB 2 ALA G  92  GLY G  94  1  O  ASN G  93   N  THR G  35
SHEET    1  GC 2 VAL G  97  ILE G 104  0
SHEET    2  GC 2 LYS G 107  LEU G 114 -1  O  LYS G 107   N  ILE G 104
SHEET    1  HA 2 ARG H  27  SER H  28  0
SHEET    2  HA 2 TYR H  88  HIS H  89  1  N  HIS H  89   O  ARG H  27
SHEET    1  HB 2 ILE H  33  THR H  35  0
SHEET    2  HB 2 ALA H  92  GLY H  94  1  O  ASN H  93   N  THR H  35
SHEET    1  HC 2 VAL H  97  ILE H 104  0
SHEET    2  HC 2 LYS H 107  LEU H 114 -1  O  LYS H 107   N  ILE H 104
SHEET    1  IA 2 ARG I  27  SER I  28  0
SHEET    2  IA 2 TYR I  88  HIS I  89  1  N  HIS I  89   O  ARG I  27
SHEET    1  IB 2 ILE I  33  THR I  35  0
SHEET    2  IB 2 ALA I  92  GLY I  94  1  O  ASN I  93   N  THR I  35
SHEET    1  IC 2 VAL I  97  ILE I 104  0
SHEET    2  IC 2 LYS I 107  LEU I 114 -1  O  LYS I 107   N  ILE I 104
SHEET    1  JA 2 ARG J  27  SER J  28  0
SHEET    2  JA 2 TYR J  88  HIS J  89  1  N  HIS J  89   O  ARG J  27
SHEET    1  JB 2 ILE J  33  THR J  35  0
SHEET    2  JB 2 ALA J  92  GLY J  94  1  O  ASN J  93   N  THR J  35
SHEET    1  JC 2 VAL J  97  ILE J 104  0
SHEET    2  JC 2 LYS J 107  LEU J 114 -1  O  LYS J 107   N  ILE J 104
SHEET    1  KA 2 ARG K  27  SER K  28  0
SHEET    2  KA 2 TYR K  88  HIS K  89  1  N  HIS K  89   O  ARG K  27
SHEET    1  KB 2 ILE K  33  THR K  35  0
SHEET    2  KB 2 ALA K  92  GLY K  94  1  O  ASN K  93   N  THR K  35
SHEET    1  KC 2 VAL K  97  ILE K 104  0
SHEET    2  KC 2 LYS K 107  LEU K 114 -1  O  LYS K 107   N  ILE K 104
SHEET    1  LA 2 ARG L  27  SER L  28  0
SHEET    2  LA 2 TYR L  88  HIS L  89  1  N  HIS L  89   O  ARG L  27
SHEET    1  LB 2 ILE L  33  THR L  35  0
SHEET    2  LB 2 ALA L  92  GLY L  94  1  O  ASN L  93   N  THR L  35
SHEET    1  LC 2 VAL L  97  ILE L 104  0
SHEET    2  LC 2 LYS L 107  LEU L 114 -1  O  LYS L 107   N  ILE L 104
SHEET    1  MA 2 ARG M  27  SER M  28  0
SHEET    2  MA 2 TYR M  88  HIS M  89  1  N  HIS M  89   O  ARG M  27
SHEET    1  MB 2 ILE M  33  THR M  35  0
SHEET    2  MB 2 ALA M  92  GLY M  94  1  O  ASN M  93   N  THR M  35
SHEET    1  MC 2 VAL M  97  ILE M 104  0
SHEET    2  MC 2 LYS M 107  LEU M 114 -1  O  LYS M 107   N  ILE M 104
SHEET    1  NA 2 ARG N  27  SER N  28  0
SHEET    2  NA 2 TYR N  88  HIS N  89  1  N  HIS N  89   O  ARG N  27
SHEET    1  NB 2 ILE N  33  THR N  35  0
SHEET    2  NB 2 ALA N  92  GLY N  94  1  O  ASN N  93   N  THR N  35
SHEET    1  NC 2 VAL N  97  ILE N 104  0
SHEET    2  NC 2 LYS N 107  LEU N 114 -1  O  LYS N 107   N  ILE N 104
SHEET    1  OA 2 ARG O  27  SER O  28  0
SHEET    2  OA 2 TYR O  88  HIS O  89  1  N  HIS O  89   O  ARG O  27
SHEET    1  OB 2 ILE O  33  THR O  35  0
SHEET    2  OB 2 ALA O  92  GLY O  94  1  O  ASN O  93   N  THR O  35
SHEET    1  OC 2 VAL O  97  ILE O 104  0
SHEET    2  OC 2 LYS O 107  LEU O 114 -1  O  LYS O 107   N  ILE O 104
SHEET    1  PA 2 ARG P  27  SER P  28  0
SHEET    2  PA 2 TYR P  88  HIS P  89  1  N  HIS P  89   O  ARG P  27
SHEET    1  PB 2 ILE P  33  THR P  35  0
SHEET    2  PB 2 ALA P  92  GLY P  94  1  O  ASN P  93   N  THR P  35
SHEET    1  PC 2 VAL P  97  ILE P 104  0
SHEET    2  PC 2 LYS P 107  LEU P 114 -1  O  LYS P 107   N  ILE P 104
SHEET    1  QA 2 ARG Q  27  SER Q  28  0
SHEET    2  QA 2 TYR Q  88  HIS Q  89  1  N  HIS Q  89   O  ARG Q  27
SHEET    1  QB 2 ILE Q  33  THR Q  35  0
SHEET    2  QB 2 ALA Q  92  GLY Q  94  1  O  ASN Q  93   N  THR Q  35
SHEET    1  QC 2 VAL Q  97  ILE Q 104  0
SHEET    2  QC 2 LYS Q 107  LEU Q 114 -1  O  LYS Q 107   N  ILE Q 104
SHEET    1  RA 2 ARG R  27  SER R  28  0
SHEET    2  RA 2 TYR R  88  HIS R  89  1  N  HIS R  89   O  ARG R  27
SHEET    1  RB 2 ILE R  33  THR R  35  0
SHEET    2  RB 2 ALA R  92  GLY R  94  1  O  ASN R  93   N  THR R  35
SHEET    1  RC 2 VAL R  97  ILE R 104  0
SHEET    2  RC 2 LYS R 107  LEU R 114 -1  O  LYS R 107   N  ILE R 104
SHEET    1  SA 2 ARG S  27  SER S  28  0
SHEET    2  SA 2 TYR S  88  HIS S  89  1  N  HIS S  89   O  ARG S  27
SHEET    1  SB 2 ILE S  33  THR S  35  0
SHEET    2  SB 2 ALA S  92  GLY S  94  1  O  ASN S  93   N  THR S  35
SHEET    1  SC 2 VAL S  97  ILE S 104  0
SHEET    2  SC 2 LYS S 107  LEU S 114 -1  O  LYS S 107   N  ILE S 104
SHEET    1  TA 2 ARG T  27  SER T  28  0
SHEET    2  TA 2 TYR T  88  HIS T  89  1  N  HIS T  89   O  ARG T  27
SHEET    1  TB 2 ILE T  33  THR T  35  0
SHEET    2  TB 2 ALA T  92  GLY T  94  1  O  ASN T  93   N  THR T  35
SHEET    1  TC 2 VAL T  97  ILE T 104  0
SHEET    2  TC 2 LYS T 107  LEU T 114 -1  O  LYS T 107   N  ILE T 104
LINK         P     C a1001                 O3'   C j1007     1555   1555  1.61
LINK         O3'   C a1007                 P     C b1001     1555   1555  1.61
LINK         O3'   C b1007                 P     C c1001     1555   1555  1.61
LINK         O3'   C c1007                 P     C d1001     1555   1555  1.59
LINK         O3'   C d1007                 P     C e1001     1555   1555  1.62
LINK         O3'   C e1007                 P     C f1001     1555   1555  1.61
LINK         O3'   C f1007                 P     C g1001     1555   1555  1.60
LINK         O3'   C g1007                 P     C h1001     1555   1555  1.59
LINK         O3'   C h1007                 P     C i1001     1555   1555  1.60
LINK         O3'   C i1007                 P     C j1001     1555   1555  1.62
LINK         P     C k1001                 O3'   C t1007     1555   1555  1.62
LINK         O3'   C k1007                 P     C l1001     1555   1555  1.59
LINK         O3'   C l1007                 P     C m1001     1555   1555  1.60
LINK         O3'   C m1007                 P     C n1001     1555   1555  1.61
LINK         O3'   C n1007                 P     C o1001     1555   1555  1.60
LINK         O3'   C o1007                 P     C p1001     1555   1555  1.61
LINK         O3'   C p1007                 P     C q1001     1555   1555  1.60
LINK         O3'   C q1007                 P     C r1001     1555   1555  1.59
LINK         O3'   C r1007                 P     C s1001     1555   1555  1.59
LINK         O3'   C s1007                 P     C t1001     1555   1555  1.62
CISPEP   1 GLY A  335    GLU A  336          0         0.43
CISPEP   2 GLY B  335    GLU B  336          0         0.35
CISPEP   3 GLY C  335    GLU C  336          0         0.39
CISPEP   4 GLY D  335    GLU D  336          0         0.41
CISPEP   5 GLY E  335    GLU E  336          0         0.41
CISPEP   6 GLY F  335    GLU F  336          0         0.40
CISPEP   7 GLY G  335    GLU G  336          0         0.39
CISPEP   8 GLY H  335    GLU H  336          0         0.46
CISPEP   9 GLY I  335    GLU I  336          0         0.41
CISPEP  10 GLY J  335    GLU J  336          0         0.35
CISPEP  11 GLY K  335    GLU K  336          0         0.48
CISPEP  12 GLY L  335    GLU L  336          0         0.42
CISPEP  13 GLY M  335    GLU M  336          0         0.36
CISPEP  14 GLY N  335    GLU N  336          0         0.45
CISPEP  15 GLY O  335    GLU O  336          0         0.35
CISPEP  16 GLY P  335    GLU P  336          0         0.35
CISPEP  17 GLY Q  335    GLU Q  336          0         0.35
CISPEP  18 GLY R  335    GLU R  336          0         0.34
CISPEP  19 GLY S  335    GLU S  336          0         0.35
CISPEP  20 GLY T  335    GLU T  336          0         0.34
SITE     1 AC1  6 ASN A  93  GLY A  94  HOH A3029  ASN G  93
SITE     2 AC1  6 GLY G  94  THR G 115
SITE     1 AC2  5 ASN B  93  GLY B  94  ASN F  93  GLY F  94
SITE     2 AC2  5 THR F 115
SITE     1 AC3  5 ASN C  93  GLY C  94  ASN E  93  GLY E  94
SITE     2 AC3  5 THR E 115
SITE     1 AC4  3 ASN D  93  GLY D  94  THR D 115
SITE     1 AC5  5 ASN H  93  GLY H  94  ASN J  93  GLY J  94
SITE     2 AC5  5 THR J 115
SITE     1 AC6  3 ASN I  93  GLY I  94  THR I 115
SITE     1 AC7  5 ASN K  93  GLY K  94  ASN S  93  GLY S  94
SITE     2 AC7  5 THR S 115
SITE     1 AC8  5 ASN L  93  GLY L  94  ASN R  93  GLY R  94
SITE     2 AC8  5 THR R 115
SITE     1 AC9  5 ASN M  93  GLY M  94  ASN Q  93  GLY Q  94
SITE     2 AC9  5 THR Q 115
SITE     1 BC1  5 ASN N  93  GLY N  94  ASN P  93  GLY P  94
SITE     2 BC1  5 THR P 115
SITE     1 BC2  2 ASN O  93  GLY O  94
SITE     1 BC3  3 ASN T  93  GLY T  94  THR T 115
CRYST1  218.200  220.990  218.100  90.00  93.09  90.00 C 1 2 1      80
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      0.004583  0.000000  0.000247        0.00000
SCALE2      0.000000  0.004525  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004592        0.00000
MTRIX1   1  0.898076 -0.428888  0.097529       25.02422    1
MTRIX2   1  0.428709  0.804014 -0.412026      115.41074    1
MTRIX3   1  0.098295  0.411854  0.905939      -24.10942    1
MTRIX1   2  0.634794 -0.692750  0.342254       -2.36447    1
MTRIX2   2  0.693488  0.315450 -0.647746      224.13570    1
MTRIX3   2  0.340764  0.648534  0.680651        2.21694    1
MTRIX1   3  0.316302 -0.702916  0.637077      -69.76667    1
MTRIX2   3  0.694719 -0.285672 -0.660121      292.71124    1
MTRIX3   3  0.646003  0.651381  0.397972       67.24315    1
MTRIX1   4  0.038770 -0.436650  0.898795     -158.91490    1
MTRIX2   4  0.435356 -0.802233 -0.408518      292.79144    1
MTRIX3   4  0.899421  0.407140  0.158999      148.95276    1
MTRIX1   5 -0.066286  0.005566  0.997782     -230.47574    1
MTRIX2   5 -0.002468 -0.999981  0.005415      220.53116    1
MTRIX3   5  0.997794 -0.002103  0.066298      215.34981    1
MTRIX1   6  0.036404  0.434608  0.899884     -255.35376    1
MTRIX2   6 -0.426183 -0.807737  0.407343      107.21156    1
MTRIX3   6  0.903904 -0.398349  0.155815      238.38187    1
MTRIX1   7  0.304546  0.692706  0.653766     -226.97728    1
MTRIX2   7 -0.686417 -0.316251  0.654836       -3.92357    1
MTRIX3   7  0.660364 -0.648187  0.379173      214.13055    1
MTRIX1   8  0.630712  0.695352  0.344505     -156.30705    1
MTRIX2   8 -0.688620  0.296833  0.661582      -72.93071    1
MTRIX3   8  0.357768 -0.654505  0.666052      148.82530    1
MTRIX1   9  0.895024  0.435361  0.096972      -70.47168    1
MTRIX2   9 -0.434082  0.800233  0.413760      -71.99734    1
MTRIX3   9  0.102533 -0.412414  0.905211       67.31360    1
MTRIX1  10  0.034091 -0.433687  0.900421      -44.26447    1
MTRIX2  10 -0.428210  0.807723  0.405245      -72.44729    1
MTRIX3  10 -0.903040 -0.399381 -0.158172      177.26276    1
MTRIX1  11 -0.070460  0.004435  0.997499     -114.93875    1
MTRIX2  11  0.001253  0.999986 -0.004358       -0.20702    1
MTRIX3  11 -0.997514  0.000943 -0.070466      112.92480    1
MTRIX1  12  0.031241  0.423956  0.905148     -139.70630    1
MTRIX2  12  0.416584  0.817658 -0.397358      110.68253    1
MTRIX3  12 -0.908557  0.389482 -0.151062       89.05310    1
MTRIX1  13  0.295733  0.695397  0.654952     -112.38541    1
MTRIX2  13  0.690991  0.317683 -0.649313      224.03156    1
MTRIX3  13 -0.659596  0.644593 -0.386569      114.49227    1
MTRIX1  14  0.633852  0.698281  0.332615      -39.53724    1
MTRIX2  14  0.688383 -0.313223 -0.654236      294.67053    1
MTRIX3  14 -0.352652  0.643658 -0.679224      181.32082    1
MTRIX1  15  0.897091  0.432754  0.089134       46.16614    1
MTRIX2  15  0.429288 -0.805968 -0.407576      292.36072    1
MTRIX3  15 -0.104541  0.403902 -0.908809      260.64883    1
MTRIX1  16  0.999990 -0.001009 -0.004393      115.73892    1
MTRIX2  16 -0.001009 -1.000004  0.000039      220.71881    1
MTRIX3  16 -0.004393 -0.000035 -0.999994      326.21722    1
MTRIX1  17  0.900408 -0.424800  0.093920      140.13438    1
MTRIX2  17 -0.426053 -0.817292  0.387961      110.65357    1
MTRIX3  17 -0.088048 -0.389338 -0.916879      349.66214    1
MTRIX1  18  0.632746 -0.696889  0.337594      113.98705    1
MTRIX2  18 -0.695018 -0.318878  0.644411       -3.07732    1
MTRIX3  18 -0.341442 -0.642389 -0.686120      324.70236    1
MTRIX1  19  0.309955 -0.700310  0.643033       44.05276    1
MTRIX2  19 -0.690662  0.298950  0.658494      -73.81007    1
MTRIX3  19 -0.653395 -0.648222 -0.391014      258.21420    1
      
PROCHECK
Go to PROCHECK summary
 References