longtext: 2HRQ-pdb

content
HEADER    HYDROLASE                               20-JUL-06   2HRQ
TITLE     CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1 (HCE1)
TITLE    2 IN COVALENT COMPLEX WITH THE NERVE AGENT SOMAN (GD)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 SYNONYM: ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE, ACAT,
COMPND   5 MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE ESTERASE
COMPND   6 1, BRAIN CARBOXYLESTERASE HBR1, TRIACYLGLYCEROL HYDROLASE,
COMPND   7 TGH, EGASYN;
COMPND   8 EC: 3.1.1.1.;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 GENE: CES1;
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM
KEYWDS    HYDROLASE, CARBOXYLESTERASE, SOMAN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.D.FLEMING,M.R.REDINBO
REVDAT   1   01-MAY-07 2HRQ    0
JRNL        AUTH   C.D.FLEMING,C.C.EDWARDS,S.D.KIRBY,D.M.MAXWELL,
JRNL        AUTH 2 P.M.POTTER,D.M.CERASOLI,M.R.REDINBO
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CARBOXYLESTERASE 1 IN
JRNL        TITL 2 COVALENT COMPLEXES WITH THE CHEMICAL WARFARE
JRNL        TITL 3 AGENTS SOMAN AND TABUN.
JRNL        REF    BIOCHEMISTRY                               2007
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 2.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 86030.230
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.5
REMARK   3   NUMBER OF REFLECTIONS             : 108029
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.170
REMARK   3   FREE R VALUE                     : 0.225
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 7595
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.80
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 16109
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150
REMARK   3   BIN FREE R VALUE                    : 0.2850
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1199
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 24757
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 468
REMARK   3   SOLVENT ATOMS            : 1115
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.00
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.35000
REMARK   3    B22 (A**2) : 3.85000
REMARK   3    B33 (A**2) : -0.50000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25
REMARK   3   ESD FROM SIGMAA              (A) : 0.25
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.350 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.310 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.060 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.180 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 31.03
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  5  : SUC.PAR
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  5   : SUC.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2HRQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038684.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-2005
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 109291
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10200
REMARK 200   FOR THE DATA SET  : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.21600
REMARK 200   FOR SHELL         : 7.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE PH 5.5, 8-11% PEG
REMARK 280  3350, 0.1-0.4M LITHIUM SULFATE, 0.1M LITHIUM CHLORIDE, 0.1M
REMARK 280  SODIUM CHLORIDE, 5% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,1/2+Y,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       90.59650
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H, I
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J, K, L
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     SER B  2021
REMARK 465     SER C  3021
REMARK 465     SER E  5021
REMARK 465     SER F  6021
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
REMARK 500   ND2  ASN A  1079     O5   NAG G   179              1.81
REMARK 500   ND2  ASN F  6079     O5   NAG L   679              1.84
REMARK 500   CG   ASN A  1079     O5   NAG G   179              1.89
REMARK 500   ND2  ASN D  4079     O5   NAG J   479              1.95
REMARK 500   ND2  ASN F  6079     C2   NAG L   679              2.02
REMARK 500   C8   NAG G   179     O    HOH    8924              2.04
REMARK 500   ND2  ASN D  4079     C2   NAG J   479              2.13
REMARK 500   CG   ASN D  4079     O5   NAG J   479              2.14
REMARK 500   N2   NAG G   179     O    HOH    8924              2.14
REMARK 500   O7   SIA I   382     O    HOH    8364              2.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    LYS A1092   CD    LYS A1092   CE    -0.054
REMARK 500    LYS A1092   CE    LYS A1092   NZ    -0.155
REMARK 500    MET A1446   SD    MET A1446   CE     0.079
REMARK 500    LYS B2092   CD    LYS B2092   CE    -0.057
REMARK 500    LYS B2092   CE    LYS B2092   NZ    -0.156
REMARK 500    MET B2459   SD    MET B2459   CE     0.045
REMARK 500    LYS C3092   CD    LYS C3092   CE    -0.054
REMARK 500    LYS C3092   CE    LYS C3092   NZ    -0.158
REMARK 500    GLU C3292   CB    GLU C3292   CG     0.050
REMARK 500    GLU C3292   CG    GLU C3292   CD     0.051
REMARK 500    MET C3364   SD    MET C3364   CE     0.049
REMARK 500    LYS D4092   CD    LYS D4092   CE    -0.055
REMARK 500    LYS D4092   CE    LYS D4092   NZ    -0.154
REMARK 500    MET D4136   SD    MET D4136   CE     0.055
REMARK 500    MET D4446   SD    MET D4446   CE     0.040
REMARK 500    MET D4459   SD    MET D4459   CE     0.043
REMARK 500    LYS E5092   CD    LYS E5092   CE    -0.058
REMARK 500    LYS E5092   CE    LYS E5092   NZ    -0.155
REMARK 500    MET E5459   SD    MET E5459   CE     0.053
REMARK 500    LYS F6092   CD    LYS F6092   CE    -0.060
REMARK 500    LYS F6092   CE    LYS F6092   NZ    -0.158
REMARK 500    MET F6364   CG    MET F6364   SD    -0.041
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LYS A1092   CD  -  CE  -  NZ  ANGL. DEV. = 12.6 DEGREES
REMARK 500    ASP A1115   N   -  CA  -  C   ANGL. DEV. = -8.0 DEGREES
REMARK 500    ASP A1126   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES
REMARK 500    PHE A1177   N   -  CA  -  C   ANGL. DEV. =  8.3 DEGREES
REMARK 500    THR A1252   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES
REMARK 500    SER A1253   N   -  CA  -  C   ANGL. DEV. =  8.0 DEGREES
REMARK 500    ILE A1323   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES
REMARK 500    GLY A1484   N   -  CA  -  C   ANGL. DEV. =  9.8 DEGREES
REMARK 500    LEU B2034   CA  -  CB  -  CG  ANGL. DEV. = 10.4 DEGREES
REMARK 500    ASP B2090   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES
REMARK 500    LYS B2092   CD  -  CE  -  NZ  ANGL. DEV. = 11.9 DEGREES
REMARK 500    ASP B2115   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES
REMARK 500    GLU B2183   N   -  CA  -  C   ANGL. DEV. =  7.8 DEGREES
REMARK 500    ASN B2204   N   -  CA  -  C   ANGL. DEV. =  8.3 DEGREES
REMARK 500    SER B2253   N   -  CA  -  C   ANGL. DEV. =  9.1 DEGREES
REMARK 500    LEU B2319   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES
REMARK 500    GLY B2484   N   -  CA  -  C   ANGL. DEV. =  9.7 DEGREES
REMARK 500    ASN B2506   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES
REMARK 500    SER C3075   N   -  CA  -  C   ANGL. DEV. =  8.5 DEGREES
REMARK 500    MET C3086   N   -  CA  -  C   ANGL. DEV. = -8.3 DEGREES
REMARK 500    LYS C3092   CD  -  CE  -  NZ  ANGL. DEV. = 12.6 DEGREES
REMARK 500    ASP C3126   N   -  CA  -  C   ANGL. DEV. = -8.5 DEGREES
REMARK 500    GLU C3183   N   -  CA  -  C   ANGL. DEV. =  7.9 DEGREES
REMARK 500    THR C3252   N   -  CA  -  C   ANGL. DEV. =-11.3 DEGREES
REMARK 500    SER C3253   N   -  CA  -  C   ANGL. DEV. =  9.6 DEGREES
REMARK 500    GLY C3320   N   -  CA  -  C   ANGL. DEV. =  8.8 DEGREES
REMARK 500    LEU C3420   CA  -  CB  -  CG  ANGL. DEV. = 10.2 DEGREES
REMARK 500    GLY C3484   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES
REMARK 500    GLN C3528   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES
REMARK 500    LYS C3538   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES
REMARK 500    LYS D4092   CD  -  CE  -  NZ  ANGL. DEV. = 12.6 DEGREES
REMARK 500    ASP D4115   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES
REMARK 500    ASP D4126   N   -  CA  -  C   ANGL. DEV. = -8.9 DEGREES
REMARK 500    ASN D4204   N   -  CA  -  C   ANGL. DEV. =  7.8 DEGREES
REMARK 500    SER D4253   N   -  CA  -  C   ANGL. DEV. =  8.0 DEGREES
REMARK 500    LEU D4319   N   -  CA  -  C   ANGL. DEV. = -8.4 DEGREES
REMARK 500    GLU D4448   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES
REMARK 500    GLY D4484   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES
REMARK 500    LEU E5034   CA  -  CB  -  CG  ANGL. DEV. =  7.8 DEGREES
REMARK 500    SER E5075   N   -  CA  -  C   ANGL. DEV. =  8.9 DEGREES
REMARK 500    THR E5081   N   -  CA  -  C   ANGL. DEV. =  9.1 DEGREES
REMARK 500    MET E5086   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES
REMARK 500    LYS E5092   CD  -  CE  -  NZ  ANGL. DEV. = 12.1 DEGREES
REMARK 500    ASP E5115   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES
REMARK 500    ASN E5204   N   -  CA  -  C   ANGL. DEV. =  8.1 DEGREES
REMARK 500    SER E5253   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES
REMARK 500    LEU E5319   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES
REMARK 500    ASN E5506   N   -  CA  -  C   ANGL. DEV. = 10.1 DEGREES
REMARK 500    LEU F6034   CA  -  CB  -  CG  ANGL. DEV. =  8.2 DEGREES
REMARK 500    SER F6075   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES
REMARK 500    LYS F6092   CD  -  CE  -  NZ  ANGL. DEV. = 12.5 DEGREES
REMARK 500    ASP F6126   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES
REMARK 500    GLU F6183   N   -  CA  -  C   ANGL. DEV. =  7.7 DEGREES
REMARK 500    ASN F6204   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES
REMARK 500    THR F6252   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES
REMARK 500    SER F6253   N   -  CA  -  C   ANGL. DEV. =  9.9 DEGREES
REMARK 500    GLY F6320   N   -  CA  -  C   ANGL. DEV. =  7.8 DEGREES
REMARK 500    LEU F6420   CA  -  CB  -  CG  ANGL. DEV. = 10.2 DEGREES
REMARK 500    GLY F6484   N   -  CA  -  C   ANGL. DEV. =  8.9 DEGREES
REMARK 500    GLN F6528   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES
REMARK 500    LYS F6538   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    SER A1221     -118.31     73.00
REMARK 500    SER C3221     -117.08     64.16
REMARK 500    SER D4221     -119.98     68.71
REMARK 500    ASN E5238        9.14    142.29
REMARK 500    SER F6221     -116.32     60.38
DBREF  2HRQ A 1021  1553  UNP    Q9UK77   EST1_HUMAN      21    553
DBREF  2HRQ B 2021  2553  UNP    Q9UK77   EST1_HUMAN      21    553
DBREF  2HRQ C 3021  3553  UNP    Q9UK77   EST1_HUMAN      21    553
DBREF  2HRQ D 4021  4553  UNP    Q9UK77   EST1_HUMAN      21    553
DBREF  2HRQ E 5021  5553  UNP    Q9UK77   EST1_HUMAN      21    553
DBREF  2HRQ F 6021  6553  UNP    Q9UK77   EST1_HUMAN      21    553
SEQADV 2HRQ     A       UNP  Q9UK77    GLN   362 DELETION
SEQADV 2HRQ     B       UNP  Q9UK77    GLN   362 DELETION
SEQADV 2HRQ     C       UNP  Q9UK77    GLN   362 DELETION
SEQADV 2HRQ     D       UNP  Q9UK77    GLN   362 DELETION
SEQADV 2HRQ     E       UNP  Q9UK77    GLN   362 DELETION
SEQADV 2HRQ     F       UNP  Q9UK77    GLN   362 DELETION
SEQRES   1 A  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES   2 A  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES   3 A  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES   4 A  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES   5 A  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES   6 A  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES   7 A  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES   8 A  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES   9 A  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES  10 A  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES  11 A  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES  12 A  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES  13 A  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES  14 A  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES  15 A  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES  16 A  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES  17 A  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES  18 A  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES  19 A  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES  20 A  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES  21 A  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES  22 A  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES  23 A  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES  24 A  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES  25 A  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES  26 A  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES  27 A  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES  28 A  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES  29 A  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES  30 A  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES  31 A  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES  32 A  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES  33 A  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES  34 A  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES  35 A  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES  36 A  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES  37 A  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES  38 A  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES  39 A  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES  40 A  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES  41 A  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES   1 B  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES   2 B  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES   3 B  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES   4 B  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES   5 B  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES   6 B  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES   7 B  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES   8 B  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES   9 B  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES  10 B  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES  11 B  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES  12 B  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES  13 B  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES  14 B  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES  15 B  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES  16 B  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES  17 B  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES  18 B  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES  19 B  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES  20 B  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES  21 B  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES  22 B  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES  23 B  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES  24 B  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES  25 B  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES  26 B  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES  27 B  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES  28 B  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES  29 B  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES  30 B  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES  31 B  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES  32 B  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES  33 B  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES  34 B  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES  35 B  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES  36 B  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES  37 B  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES  38 B  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES  39 B  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES  40 B  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES  41 B  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES   1 C  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES   2 C  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES   3 C  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES   4 C  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES   5 C  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES   6 C  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES   7 C  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES   8 C  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES   9 C  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES  10 C  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES  11 C  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES  12 C  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES  13 C  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES  14 C  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES  15 C  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES  16 C  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES  17 C  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES  18 C  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES  19 C  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES  20 C  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES  21 C  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES  22 C  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES  23 C  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES  24 C  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES  25 C  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES  26 C  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES  27 C  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES  28 C  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES  29 C  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES  30 C  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES  31 C  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES  32 C  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES  33 C  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES  34 C  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES  35 C  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES  36 C  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES  37 C  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES  38 C  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES  39 C  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES  40 C  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES  41 C  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES   1 D  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES   2 D  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES   3 D  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES   4 D  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES   5 D  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES   6 D  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES   7 D  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES   8 D  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES   9 D  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES  10 D  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES  11 D  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES  12 D  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES  13 D  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES  14 D  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES  15 D  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES  16 D  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES  17 D  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES  18 D  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES  19 D  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES  20 D  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES  21 D  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES  22 D  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES  23 D  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES  24 D  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES  25 D  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES  26 D  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES  27 D  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES  28 D  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES  29 D  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES  30 D  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES  31 D  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES  32 D  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES  33 D  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES  34 D  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES  35 D  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES  36 D  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES  37 D  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES  38 D  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES  39 D  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES  40 D  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES  41 D  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES   1 E  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES   2 E  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES   3 E  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES   4 E  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES   5 E  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES   6 E  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES   7 E  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES   8 E  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES   9 E  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES  10 E  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES  11 E  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES  12 E  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES  13 E  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES  14 E  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES  15 E  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES  16 E  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES  17 E  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES  18 E  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES  19 E  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES  20 E  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES  21 E  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES  22 E  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES  23 E  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES  24 E  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES  25 E  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES  26 E  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES  27 E  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES  28 E  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES  29 E  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES  30 E  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES  31 E  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES  32 E  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES  33 E  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES  34 E  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES  35 E  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES  36 E  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES  37 E  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES  38 E  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES  39 E  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES  40 E  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES  41 E  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES   1 F  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES   2 F  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES   3 F  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES   4 F  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES   5 F  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES   6 F  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES   7 F  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES   8 F  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES   9 F  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES  10 F  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES  11 F  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES  12 F  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES  13 F  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES  14 F  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES  15 F  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES  16 F  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES  17 F  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES  18 F  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES  19 F  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES  20 F  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES  21 F  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES  22 F  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES  23 F  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES  24 F  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES  25 F  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES  26 F  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES  27 F  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES  28 F  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES  29 F  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES  30 F  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES  31 F  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES  32 F  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES  33 F  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES  34 F  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES  35 F  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES  36 F  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES  37 F  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES  38 F  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES  39 F  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES  40 F  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES  41 F  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
MODRES 2HRQ ASN A 1079  ASN  GLYCOSYLATION SITE
MODRES 2HRQ ASN B 2079  ASN  GLYCOSYLATION SITE
MODRES 2HRQ ASN C 3079  ASN  GLYCOSYLATION SITE
MODRES 2HRQ ASN D 4079  ASN  GLYCOSYLATION SITE
MODRES 2HRQ ASN E 5079  ASN  GLYCOSYLATION SITE
MODRES 2HRQ ASN F 6079  ASN  GLYCOSYLATION SITE
HET    NAG  G 179      14
HET    SIA  G 182      21
HET    NAG  H 279      14
HET    SIA  H 282      21
HET    NAG  I 379      14
HET    SIA  I 382      21
HET    NAG  J 479      14
HET    SIA  J 482      21
HET    NAG  K 579      14
HET    SIA  K 582      21
HET    NAG  L 679      14
HET    SIA  L 682      21
HET    SUC     11      23
HET    SUC     22      23
HET    SUC     33      23
HET    SUC     44      23
HET    SUC     55      23
HET    SUC     66      23
HET    SO4    184       5
HET    SO4    185       5
HET    SO4    284       5
HET    SO4    285       5
HET    SO4    384       5
HET    SO4    385       5
HET    SO4    484       5
HET    SO4    485       5
HET    SO4    584       5
HET    SO4    585       5
HET    SO4    684       5
HET    SO4    685       5
HET    GD7  A   1      10
HET    GD7  B   1      10
HET    GD7  C   1      10
HET    GD7  D   1      10
HET    GD7  E   1      10
HET    GD7  F   1      10
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     SIA O-SIALIC ACID
HETNAM     SUC SUCROSE
HETNAM     SO4 SULFATE ION
HETNAM     GD7 (1R)-1,2,2-TRIMETHYLPROPYL (R)-METHYLPHOSPHINATE
HETSYN     NAG NAG
FORMUL   7  NAG    6(C8 H15 N1 O6)
FORMUL   8  SIA    6(C11 H19 N1 O9)
FORMUL  19  SUC    6(C12 H22 O11)
FORMUL  25  SO4    12(O4 S1 2-)
FORMUL  37  GD7    6(C7 H17 O2 P1)
FORMUL  43  HOH   *1115(H2 O1)
HELIX    1   1 LEU A 1060  ARG A 1064  5                                   5
HELIX    2   2 ASP A 1090  THR A 1102  1                                  13
HELIX    3   3 GLY A 1154  ASN A 1162  1                                   9
HELIX    4   4 LEU A 1172  PHE A 1178  1                                   7
HELIX    5   5 ASP A 1182  ARG A 1186  5                                   5
HELIX    6   6 ASN A 1188  ILE A 1205  1                                  18
HELIX    7   7 ALA A 1206  PHE A 1208  5                                   3
HELIX    8   8 SER A 1221  LEU A 1232  1                                  12
HELIX    9   9 THR A 1252  VAL A 1256  5                                   5
HELIX   10  10 VAL A 1261  GLY A 1273  1                                  13
HELIX   11  11 THR A 1278  GLN A 1288  1                                  11
HELIX   12  12 THR A 1290  LYS A 1302  1                                  13
HELIX   13  13 ASP A 1311  SER A 1315  5                                   5
HELIX   14  14 THR A 1331  GLU A 1338  1                                   8
HELIX   15  15 TRP A 1357  SER A 1365  1                                   8
HELIX   16  16 ASP A 1374  SER A 1385  1                                  12
HELIX   17  17 SER A 1385  CYS A 1390  1                                   6
HELIX   18  18 LEU A 1395  GLY A 1405  1                                  11
HELIX   19  19 ASP A 1409  PHE A 1426  1                                  18
HELIX   20  20 PHE A 1426  ALA A 1440  1                                  15
HELIX   21  21 GLU A 1471  PHE A 1476  1                                   6
HELIX   22  22 GLY A 1477  LEU A 1481  5                                   5
HELIX   23  23 SER A 1486  GLY A 1507  1                                  22
HELIX   24  24 LYS A 1540  PHE A 1551  1                                  12
HELIX   25  25 LEU B 2060  ARG B 2064  5                                   5
HELIX   26  26 ASP B 2090  THR B 2102  1                                  13
HELIX   27  27 GLY B 2154  ASN B 2162  1                                   9
HELIX   28  28 LEU B 2172  PHE B 2178  1                                   7
HELIX   29  29 ASN B 2188  ILE B 2205  1                                  18
HELIX   30  30 ALA B 2206  PHE B 2208  5                                   3
HELIX   31  31 SER B 2221  SER B 2233  1                                  13
HELIX   32  32 THR B 2252  VAL B 2256  5                                   5
HELIX   33  33 VAL B 2261  ALA B 2272  1                                  12
HELIX   34  34 THR B 2278  ARG B 2287  1                                  10
HELIX   35  35 THR B 2290  MET B 2301  1                                  12
HELIX   36  36 THR B 2331  ALA B 2337  1                                   7
HELIX   37  37 TRP B 2357  MET B 2364  1                                   7
HELIX   38  38 ASP B 2374  SER B 2385  1                                  12
HELIX   39  39 SER B 2385  CYS B 2390  1                                   6
HELIX   40  40 ALA B 2392  GLU B 2394  5                                   3
HELIX   41  41 LEU B 2395  GLY B 2405  1                                  11
HELIX   42  42 ASP B 2409  PHE B 2426  1                                  18
HELIX   43  43 PHE B 2426  ALA B 2440  1                                  15
HELIX   44  44 GLU B 2471  PHE B 2476  1                                   6
HELIX   45  45 GLY B 2477  LEU B 2481  5                                   5
HELIX   46  46 SER B 2486  GLY B 2507  1                                  22
HELIX   47  47 LYS B 2540  ALA B 2552  1                                  13
HELIX   48  48 LEU C 3060  ARG C 3064  5                                   5
HELIX   49  49 ASP C 3090  THR C 3102  1                                  13
HELIX   50  50 GLY C 3154  ASN C 3162  1                                   9
HELIX   51  51 LEU C 3172  PHE C 3178  1                                   7
HELIX   52  52 ASN C 3188  ILE C 3205  1                                  18
HELIX   53  53 ALA C 3206  PHE C 3208  5                                   3
HELIX   54  54 SER C 3221  SER C 3233  1                                  13
HELIX   55  55 THR C 3252  VAL C 3256  5                                   5
HELIX   56  56 VAL C 3261  ALA C 3272  1                                  12
HELIX   57  57 THR C 3278  GLN C 3288  1                                  11
HELIX   58  58 THR C 3290  LYS C 3302  1                                  13
HELIX   59  59 ASP C 3311  SER C 3315  5                                   5
HELIX   60  60 THR C 3331  ALA C 3337  1                                   7
HELIX   61  61 TRP C 3357  MET C 3364  1                                   7
HELIX   62  62 ASP C 3374  SER C 3385  1                                  12
HELIX   63  63 SER C 3385  CYS C 3390  1                                   6
HELIX   64  64 LEU C 3395  GLY C 3405  1                                  11
HELIX   65  65 ASP C 3409  PHE C 3426  1                                  18
HELIX   66  66 PHE C 3426  ALA C 3440  1                                  15
HELIX   67  67 GLU C 3471  PHE C 3476  1                                   6
HELIX   68  68 GLY C 3477  LEU C 3481  5                                   5
HELIX   69  69 SER C 3486  GLY C 3507  1                                  22
HELIX   70  70 LYS C 3540  PHE C 3551  1                                  12
HELIX   71  71 LEU D 4060  ARG D 4064  5                                   5
HELIX   72  72 ASP D 4090  THR D 4102  1                                  13
HELIX   73  73 GLY D 4154  ASN D 4162  1                                   9
HELIX   74  74 LEU D 4172  PHE D 4178  1                                   7
HELIX   75  75 ASN D 4188  ILE D 4205  1                                  18
HELIX   76  76 ALA D 4206  PHE D 4208  5                                   3
HELIX   77  77 SER D 4221  SER D 4233  1                                  13
HELIX   78  78 THR D 4252  VAL D 4256  5                                   5
HELIX   79  79 VAL D 4261  GLY D 4273  1                                  13
HELIX   80  80 THR D 4278  ARG D 4287  1                                  10
HELIX   81  81 THR D 4290  LYS D 4302  1                                  13
HELIX   82  82 ASP D 4311  SER D 4315  5                                   5
HELIX   83  83 THR D 4331  GLU D 4338  1                                   8
HELIX   84  84 TRP D 4357  SER D 4365  1                                   8
HELIX   85  85 ASP D 4374  SER D 4385  1                                  12
HELIX   86  86 SER D 4385  CYS D 4390  1                                   6
HELIX   87  87 LEU D 4395  GLY D 4405  1                                  11
HELIX   88  88 ASP D 4409  PHE D 4426  1                                  18
HELIX   89  89 PHE D 4426  ALA D 4440  1                                  15
HELIX   90  90 GLU D 4471  PHE D 4476  1                                   6
HELIX   91  91 GLY D 4477  LEU D 4481  5                                   5
HELIX   92  92 SER D 4486  GLY D 4507  1                                  22
HELIX   93  93 LYS D 4540  PHE D 4551  1                                  12
HELIX   94  94 LEU E 5060  ARG E 5064  5                                   5
HELIX   95  95 ASP E 5090  THR E 5102  1                                  13
HELIX   96  96 GLY E 5154  ASN E 5162  1                                   9
HELIX   97  97 LEU E 5172  PHE E 5178  1                                   7
HELIX   98  98 ASN E 5188  ILE E 5205  1                                  18
HELIX   99  99 ALA E 5206  PHE E 5208  5                                   3
HELIX  100 100 SER E 5221  SER E 5233  1                                  13
HELIX  101 101 PRO E 5234  LYS E 5237  5                                   4
HELIX  102 102 THR E 5252  VAL E 5256  5                                   5
HELIX  103 103 VAL E 5261  GLY E 5273  1                                  13
HELIX  104 104 THR E 5278  GLN E 5288  1                                  11
HELIX  105 105 THR E 5290  LYS E 5302  1                                  13
HELIX  106 106 ASP E 5311  SER E 5315  5                                   5
HELIX  107 107 THR E 5331  ALA E 5337  1                                   7
HELIX  108 108 TRP E 5357  MET E 5364  1                                   7
HELIX  109 109 ASP E 5374  SER E 5385  1                                  12
HELIX  110 110 SER E 5385  CYS E 5390  1                                   6
HELIX  111 111 LEU E 5395  GLY E 5405  1                                  11
HELIX  112 112 ASP E 5409  PHE E 5426  1                                  18
HELIX  113 113 PHE E 5426  ALA E 5440  1                                  15
HELIX  114 114 GLU E 5471  PHE E 5476  1                                   6
HELIX  115 115 GLY E 5477  LEU E 5481  5                                   5
HELIX  116 116 SER E 5486  GLY E 5507  1                                  22
HELIX  117 117 LYS E 5540  ALA E 5552  1                                  13
HELIX  118 118 LEU F 6060  ARG F 6064  5                                   5
HELIX  119 119 ASP F 6090  THR F 6102  1                                  13
HELIX  120 120 GLY F 6154  ASN F 6162  1                                   9
HELIX  121 121 LEU F 6172  PHE F 6178  1                                   7
HELIX  122 122 ASN F 6188  ILE F 6205  1                                  18
HELIX  123 123 ALA F 6206  PHE F 6208  5                                   3
HELIX  124 124 SER F 6221  SER F 6233  1                                  13
HELIX  125 125 THR F 6252  VAL F 6256  5                                   5
HELIX  126 126 VAL F 6261  ALA F 6272  1                                  12
HELIX  127 127 THR F 6278  LYS F 6289  1                                  12
HELIX  128 128 THR F 6290  LYS F 6302  1                                  13
HELIX  129 129 THR F 6331  ALA F 6337  1                                   7
HELIX  130 130 TRP F 6357  MET F 6364  1                                   7
HELIX  131 131 ASP F 6374  SER F 6385  1                                  12
HELIX  132 132 SER F 6385  CYS F 6390  1                                   6
HELIX  133 133 LEU F 6395  GLY F 6405  1                                  11
HELIX  134 134 ASP F 6409  PHE F 6426  1                                  18
HELIX  135 135 PHE F 6426  ALA F 6440  1                                  15
HELIX  136 136 ASP F 6470  PHE F 6476  1                                   7
HELIX  137 137 GLY F 6477  LYS F 6482  1                                   6
HELIX  138 138 SER F 6486  GLY F 6507  1                                  22
HELIX  139 139 LYS F 6540  PHE F 6551  1                                  12
SHEET    1   A 3 VAL A1025  THR A1028  0
SHEET    2   A 3 GLY A1031  LEU A1034 -1  O  VAL A1033   N  VAL A1026
SHEET    3   A 3 VAL A1077  ASN A1079  1  O  LYS A1078   N  LEU A1034
SHEET    1   B11 LYS A1036  VAL A1038  0
SHEET    2   B11 VAL A1047  PRO A1054 -1  O  ILE A1049   N  LYS A1036
SHEET    3   B11 TYR A1118  THR A1123 -1  O  THR A1123   N  ALA A1048
SHEET    4   B11 VAL A1164  ILE A1168 -1  O  VAL A1165   N  TYR A1122
SHEET    5   B11 LEU A1133  ILE A1139  1  N  MET A1136   O  VAL A1164
SHEET    6   B11 GLY A1210  GLU A1220  1  O  THR A1216   N  VAL A1135
SHEET    7   B11 ARG A1242  GLU A1246  1  O  GLU A1246   N  GLY A1219
SHEET    8   B11 TYR A1346  ASN A1351  1  O  MET A1347   N  SER A1245
SHEET    9   B11 THR A1444  PHE A1449  1  O  TYR A1445   N  VAL A1348
SHEET   10   B11 GLY A1525  ILE A1529  1  O  LEU A1527   N  GLU A1448
SHEET   11   B11 GLN A1534  GLN A1537 -1  O  GLN A1534   N  GLN A1528
SHEET    1   C 2 MET A1086  CYS A1087  0
SHEET    2   C 2 LEU A1112  SER A1113  1  O  SER A1113   N  MET A1086
SHEET    1   D 3 VAL B2025  THR B2028  0
SHEET    2   D 3 GLY B2031  LEU B2034 -1  O  VAL B2033   N  VAL B2026
SHEET    3   D 3 VAL B2077  ASN B2079  1  O  LYS B2078   N  LEU B2034
SHEET    1   E11 LYS B2036  LEU B2040  0
SHEET    2   E11 PHE B2043  PRO B2054 -1  O  VAL B2047   N  VAL B2038
SHEET    3   E11 TYR B2118  THR B2123 -1  O  THR B2123   N  ALA B2048
SHEET    4   E11 VAL B2164  ILE B2168 -1  O  THR B2167   N  ASN B2120
SHEET    5   E11 LEU B2133  ILE B2139  1  N  MET B2136   O  VAL B2166
SHEET    6   E11 GLY B2210  GLU B2220  1  O  THR B2216   N  VAL B2135
SHEET    7   E11 ARG B2242  GLU B2246  1  O  GLU B2246   N  GLY B2219
SHEET    8   E11 TYR B2346  ASN B2351  1  O  MET B2347   N  SER B2245
SHEET    9   E11 THR B2444  GLN B2450  1  O  TYR B2445   N  VAL B2348
SHEET   10   E11 GLY B2525  GLY B2530  1  O  ILE B2529   N  GLN B2450
SHEET   11   E11 GLN B2534  GLN B2537 -1  O  GLN B2534   N  GLN B2528
SHEET    1   F 2 MET B2086  CYS B2087  0
SHEET    2   F 2 LEU B2112  SER B2113  1  O  SER B2113   N  MET B2086
SHEET    1   G 3 VAL C3025  THR C3028  0
SHEET    2   G 3 GLY C3031  LEU C3034 -1  O  VAL C3033   N  VAL C3026
SHEET    3   G 3 VAL C3077  ASN C3079  1  O  LYS C3078   N  LEU C3034
SHEET    1   H11 LYS C3036  VAL C3038  0
SHEET    2   H11 VAL C3047  PRO C3054 -1  O  ILE C3049   N  LYS C3036
SHEET    3   H11 TYR C3118  THR C3123 -1  O  ILE C3121   N  PHE C3050
SHEET    4   H11 VAL C3164  ILE C3168 -1  O  VAL C3165   N  TYR C3122
SHEET    5   H11 LEU C3133  ILE C3139  1  N  MET C3136   O  VAL C3164
SHEET    6   H11 GLY C3210  GLU C3220  1  O  THR C3216   N  VAL C3135
SHEET    7   H11 ARG C3242  GLU C3246  1  O  GLU C3246   N  GLY C3219
SHEET    8   H11 TYR C3346  ASN C3351  1  O  MET C3347   N  ALA C3243
SHEET    9   H11 THR C3444  PHE C3449  1  O  TYR C3445   N  VAL C3348
SHEET   10   H11 TYR C3526  ILE C3529  1  O  LEU C3527   N  MET C3446
SHEET   11   H11 GLN C3534  ALA C3536 -1  O  ALA C3536   N  TYR C3526
SHEET    1   I 2 MET C3086  CYS C3087  0
SHEET    2   I 2 LEU C3112  SER C3113  1  O  SER C3113   N  MET C3086
SHEET    1   J 3 VAL D4025  THR D4028  0
SHEET    2   J 3 GLY D4031  LEU D4034 -1  O  VAL D4033   N  VAL D4026
SHEET    3   J 3 VAL D4077  ASN D4079  1  O  LYS D4078   N  LEU D4034
SHEET    1   K11 LYS D4036  VAL D4038  0
SHEET    2   K11 VAL D4047  PRO D4054 -1  O  ILE D4049   N  LYS D4036
SHEET    3   K11 TYR D4118  THR D4123 -1  O  THR D4123   N  ALA D4048
SHEET    4   K11 VAL D4164  ILE D4168 -1  O  THR D4167   N  ASN D4120
SHEET    5   K11 LEU D4133  ILE D4139  1  N  MET D4136   O  VAL D4164
SHEET    6   K11 GLY D4210  GLU D4220  1  O  THR D4216   N  VAL D4137
SHEET    7   K11 ARG D4242  GLU D4246  1  O  GLU D4246   N  GLY D4219
SHEET    8   K11 TYR D4346  ASN D4351  1  O  MET D4347   N  ALA D4243
SHEET    9   K11 THR D4444  PHE D4449  1  O  PHE D4449   N  ILE D4350
SHEET   10   K11 GLY D4525  ILE D4529  1  O  LEU D4527   N  GLU D4448
SHEET   11   K11 GLN D4534  GLN D4537 -1  O  GLN D4534   N  GLN D4528
SHEET    1   L 2 MET D4086  CYS D4087  0
SHEET    2   L 2 LEU D4112  SER D4113  1  O  SER D4113   N  MET D4086
SHEET    1   M 3 VAL E5025  THR E5028  0
SHEET    2   M 3 GLY E5031  LEU E5034 -1  O  VAL E5033   N  VAL E5026
SHEET    3   M 3 VAL E5077  ASN E5079  1  O  LYS E5078   N  LEU E5034
SHEET    1   N11 LYS E5036  LEU E5040  0
SHEET    2   N11 PHE E5043  PRO E5054 -1  O  VAL E5047   N  VAL E5038
SHEET    3   N11 TYR E5118  THR E5123 -1  O  THR E5123   N  ALA E5048
SHEET    4   N11 VAL E5164  ILE E5168 -1  O  VAL E5165   N  TYR E5122
SHEET    5   N11 LEU E5133  ILE E5139  1  N  MET E5136   O  VAL E5166
SHEET    6   N11 GLY E5210  GLU E5220  1  O  THR E5216   N  VAL E5137
SHEET    7   N11 ARG E5242  GLU E5246  1  O  GLU E5246   N  GLY E5219
SHEET    8   N11 TYR E5346  ASN E5351  1  O  MET E5347   N  ALA E5243
SHEET    9   N11 THR E5444  PHE E5449  1  O  TYR E5445   N  VAL E5348
SHEET   10   N11 GLY E5525  ILE E5529  1  O  ILE E5529   N  GLU E5448
SHEET   11   N11 GLN E5534  GLN E5537 -1  O  GLN E5534   N  GLN E5528
SHEET    1   O 2 MET E5086  CYS E5087  0
SHEET    2   O 2 LEU E5112  SER E5113  1  O  SER E5113   N  MET E5086
SHEET    1   P 3 VAL F6025  THR F6028  0
SHEET    2   P 3 GLY F6031  LEU F6034 -1  O  VAL F6033   N  VAL F6026
SHEET    3   P 3 VAL F6077  ASN F6079  1  O  LYS F6078   N  LEU F6034
SHEET    1   Q11 LYS F6036  VAL F6038  0
SHEET    2   Q11 VAL F6047  PRO F6054 -1  O  ILE F6049   N  LYS F6036
SHEET    3   Q11 TYR F6118  THR F6123 -1  O  ILE F6121   N  PHE F6050
SHEET    4   Q11 VAL F6164  ILE F6168 -1  O  THR F6167   N  ASN F6120
SHEET    5   Q11 LEU F6133  ILE F6139  1  N  MET F6136   O  VAL F6164
SHEET    6   Q11 GLY F6210  GLU F6220  1  O  THR F6216   N  VAL F6135
SHEET    7   Q11 ARG F6242  GLU F6246  1  O  ILE F6244   N  ILE F6217
SHEET    8   Q11 TYR F6346  ASN F6351  1  O  MET F6347   N  ALA F6243
SHEET    9   Q11 THR F6444  PHE F6449  1  O  TYR F6445   N  VAL F6348
SHEET   10   Q11 TYR F6526  ILE F6529  1  O  LEU F6527   N  MET F6446
SHEET   11   Q11 GLN F6534  ALA F6536 -1  O  ALA F6536   N  TYR F6526
SHEET    1   R 2 MET F6086  CYS F6087  0
SHEET    2   R 2 LEU F6112  SER F6113  1  O  SER F6113   N  MET F6086
SSBOND   1 CYS A 1087    CYS A 1116
SSBOND   2 CYS A 1274    CYS A 1285
SSBOND   3 CYS B 2087    CYS B 2116
SSBOND   4 CYS B 2274    CYS B 2285
SSBOND   5 CYS C 3087    CYS C 3116
SSBOND   6 CYS C 3274    CYS C 3285
SSBOND   7 CYS D 4087    CYS D 4116
SSBOND   8 CYS D 4274    CYS D 4285
SSBOND   9 CYS E 5087    CYS E 5116
SSBOND  10 CYS E 5274    CYS E 5285
SSBOND  11 CYS F 6087    CYS F 6116
SSBOND  12 CYS F 6274    CYS F 6285
LINK         ND2 ASN B2079                 C1  NAG H 279
LINK         ND2 ASN C3079                 C1  NAG I 379
LINK         ND2 ASN E5079                 C1  NAG K 579
LINK         OG  SER A1221                 P1  GD7 A   1
LINK         OG  SER B2221                 P1  GD7 B   1
LINK         OG  SER C3221                 P1  GD7 C   1
LINK         OG  SER D4221                 P1  GD7 D   1
LINK         OG  SER E5221                 P1  GD7 E   1
LINK         OG  SER F6221                 P1  GD7 F   1
LINK         ND2 ASN A1079                 C1  NAG G 179
LINK         ND2 ASN D4079                 C1  NAG J 479
LINK         ND2 ASN F6079                 C1  NAG L 679
CRYST1   55.463  181.193  203.051  90.00  89.99  90.00 P 1 21 1     12
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      0.018030  0.000000 -0.000003        0.00000
SCALE2      0.000000  0.005519  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004925        0.00000
TER    4131      LYS A1553
TER    8256      LYS B2553
TER   12381      LYS C3553
TER   16512      LYS D4553
TER   20637      LYS E5553
TER   24763      LYS F6553
MASTER      374    0   36  139   96    0    0    626340    6  504  246
END