HEADER TOXIN 16-APR-13 3W9T
TITLE PORE-FORMING CEL-III
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOLYTIC LECTIN CEL-III;
COMPND 3 CHAIN: A, C, G, B, F, E, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUCUMARIA ECHINATA;
SOURCE 3 ORGANISM_COMMON: SEA CUCUMBER;
SOURCE 4 ORGANISM_TAXID: 40245
KEYWDS HEMOLYTIC LECTIN, PORE FORMING TOXIN, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.UNNO,S.GODA,T.HATAKEYAMA
REVDAT 5 29-JUL-20 3W9T 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 FORMUL SSBOND LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 25-DEC-19 3W9T 1 SEQRES LINK
REVDAT 3 25-JUL-18 3W9T 1 COMPND SOURCE REMARK DBREF
REVDAT 3 2 1 SEQADV HET HETNAM FORMUL
REVDAT 2 21-MAY-14 3W9T 1 SEQADV
REVDAT 1 19-MAR-14 3W9T 0
JRNL AUTH H.UNNO,S.GODA,T.HATAKEYAMA
JRNL TITL HEMOLYTIC LECTIN CEL-III HEPTAMER REVEALS ITS TRANSMEMBRANE
JRNL TITL 2 PORE-FORMATION MECHANISM
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 107985
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 + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5691
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7991
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 420
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23191
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 909
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.64000
REMARK 3 B22 (A**2) : 0.39000
REMARK 3 B33 (A**2) : -0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.039
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.412
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24590 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33546 ; 1.595 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3017 ; 8.651 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1162 ;40.536 ;25.482
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3836 ;18.109 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 126 ;17.854 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3812 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18368 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 432
REMARK 3 RESIDUE RANGE : A 1001 A 1013
REMARK 3 ORIGIN FOR THE GROUP (A): 83.3228 105.9592 -14.6935
REMARK 3 T TENSOR
REMARK 3 T11: 0.1589 T22: 0.2735
REMARK 3 T33: 0.1067 T12: 0.0919
REMARK 3 T13: 0.0353 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.3767 L22: 0.7594
REMARK 3 L33: 0.3207 L12: -0.4276
REMARK 3 L13: -0.1285 L23: 0.1571
REMARK 3 S TENSOR
REMARK 3 S11: -0.1173 S12: -0.0377 S13: 0.0945
REMARK 3 S21: 0.1632 S22: 0.1254 S23: -0.0032
REMARK 3 S31: 0.0948 S32: -0.0952 S33: -0.0081
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 432
REMARK 3 RESIDUE RANGE : C 1001 C 1013
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5039 33.6309 -5.4994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2179 T22: 0.2801
REMARK 3 T33: 0.1492 T12: -0.1217
REMARK 3 T13: 0.0900 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 0.3327 L22: 0.2799
REMARK 3 L33: 0.3092 L12: 0.0288
REMARK 3 L13: -0.2082 L23: -0.0883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0592 S12: 0.0121 S13: -0.1527
REMARK 3 S21: -0.0268 S22: -0.0052 S23: 0.0620
REMARK 3 S31: 0.1365 S32: -0.1624 S33: 0.0643
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 432
REMARK 3 RESIDUE RANGE : G 501 G 513
REMARK 3 ORIGIN FOR THE GROUP (A): 121.2997 103.2956 -32.6771
REMARK 3 T TENSOR
REMARK 3 T11: 0.2826 T22: 0.1393
REMARK 3 T33: 0.2150 T12: 0.0023
REMARK 3 T13: -0.0326 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.8053 L22: 0.7223
REMARK 3 L33: 0.3595 L12: 0.1472
REMARK 3 L13: 0.0587 L23: 0.3712
REMARK 3 S TENSOR
REMARK 3 S11: -0.1253 S12: 0.0038 S13: 0.3946
REMARK 3 S21: -0.2151 S22: 0.0610 S23: 0.1487
REMARK 3 S31: -0.1191 S32: 0.0175 S33: 0.0643
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 432
REMARK 3 RESIDUE RANGE : B 501 B 514
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4567 75.2413 -2.7634
REMARK 3 T TENSOR
REMARK 3 T11: 0.1856 T22: 0.2614
REMARK 3 T33: 0.1656 T12: -0.0098
REMARK 3 T13: 0.1060 T23: 0.0942
REMARK 3 L TENSOR
REMARK 3 L11: 0.3954 L22: 0.3858
REMARK 3 L33: 0.1665 L12: -0.2585
REMARK 3 L13: 0.0244 L23: 0.0530
REMARK 3 S TENSOR
REMARK 3 S11: -0.1538 S12: -0.0434 S13: -0.1726
REMARK 3 S21: 0.0415 S22: 0.0868 S23: 0.2042
REMARK 3 S31: 0.0800 S32: -0.0059 S33: 0.0670
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 432
REMARK 3 RESIDUE RANGE : F 501 F 513
REMARK 3 ORIGIN FOR THE GROUP (A): 142.7005 68.4932 -42.0606
REMARK 3 T TENSOR
REMARK 3 T11: 0.4533 T22: 0.3752
REMARK 3 T33: 0.0524 T12: -0.0345
REMARK 3 T13: 0.0821 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 0.9454 L22: 0.5944
REMARK 3 L33: 0.2088 L12: 0.3261
REMARK 3 L13: -0.1134 L23: 0.2411
REMARK 3 S TENSOR
REMARK 3 S11: -0.2568 S12: 0.0522 S13: 0.0782
REMARK 3 S21: -0.2165 S22: 0.2213 S23: 0.0646
REMARK 3 S31: -0.0059 S32: 0.0395 S33: 0.0355
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 432
REMARK 3 RESIDUE RANGE : E 501 E 514
REMARK 3 ORIGIN FOR THE GROUP (A): 131.8473 28.1256 -37.2260
REMARK 3 T TENSOR
REMARK 3 T11: 0.3346 T22: 0.3376
REMARK 3 T33: 0.0600 T12: 0.0881
REMARK 3 T13: 0.0990 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.8101 L22: 0.3502
REMARK 3 L33: 0.0884 L12: -0.0995
REMARK 3 L13: -0.1035 L23: 0.0242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: 0.0975 S13: -0.1468
REMARK 3 S21: -0.0622 S22: -0.0265 S23: 0.0219
REMARK 3 S31: 0.0967 S32: 0.0786 S33: 0.0592
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 432
REMARK 3 RESIDUE RANGE : D 501 D 513
REMARK 3 ORIGIN FOR THE GROUP (A): 96.5089 12.8579 -21.0730
REMARK 3 T TENSOR
REMARK 3 T11: 0.3005 T22: 0.0999
REMARK 3 T33: 0.0512 T12: 0.0016
REMARK 3 T13: 0.0788 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.2349 L22: 0.5040
REMARK 3 L33: 0.2574 L12: 0.1665
REMARK 3 L13: -0.0821 L23: -0.0254
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: 0.0083 S13: -0.0877
REMARK 3 S21: -0.0639 S22: -0.0633 S23: -0.0956
REMARK 3 S31: 0.2347 S32: 0.0306 S33: 0.0819
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3W9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000096066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113863
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 53.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.41100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M CDCL2, 0.1M SODIUM
REMARK 280 ACETATE, 10MM CACL2, 0.1M LACTULOSE, PH 4.2, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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 109.90000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 114.32500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 109.90000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 114.32500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 36080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, G, B, F, E, D, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,
REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l,
REMARK 350 AND CHAINS: m, n, o, p, q, r
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 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 OG1 THR G 35 O THR G 128 2.01
REMARK 500 O4 FRU g 1 O5 GAL g 2 2.19
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 C GLY A 127 CA CA C 1014 4555 1.19
REMARK 500 CA GLY A 127 CA CA C 1014 4555 1.68
REMARK 500 OE2 GLU E 211 OE2 GLU E 211 2654 1.69
REMARK 500 O GLY B 127 OE2 GLU D 123 4555 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 126 CG ASP A 126 OD2 -0.164
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 ASP A 126 OD1 - CG - OD2 ANGL. DEV. = -15.9 DEGREES
REMARK 500 ASP A 126 CB - CG - OD1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 THR C 128 N - CA - C ANGL. DEV. = -28.6 DEGREES
REMARK 500 LEU C 349 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 LEU C 349 CB - CG - CD1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG B 378 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG B 378 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 GLY B 379 C - N - CA ANGL. DEV. = 20.4 DEGREES
REMARK 500 GLY E 129 N - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 66 41.51 -85.07
REMARK 500 SER A 125 53.33 -118.31
REMARK 500 ASP A 126 70.87 80.11
REMARK 500 THR A 128 -107.30 -82.73
REMARK 500 ASN A 138 16.09 52.12
REMARK 500 ASP A 140 3.53 -69.55
REMARK 500 GLU A 152 111.25 -26.01
REMARK 500 SER A 172 15.25 -145.95
REMARK 500 ASP A 225 40.36 -104.48
REMARK 500 ASP A 226 27.25 41.96
REMARK 500 PHE A 336 -49.84 126.07
REMARK 500 ASP A 373 4.07 82.79
REMARK 500 ASP C 66 42.28 -83.83
REMARK 500 ASP C 126 65.38 161.92
REMARK 500 THR C 128 -129.57 169.75
REMARK 500 ASN C 138 18.47 48.61
REMARK 500 ASP C 140 1.99 -66.12
REMARK 500 GLU C 152 106.53 -20.71
REMARK 500 SER C 172 14.33 -148.73
REMARK 500 ASP C 225 42.00 -103.16
REMARK 500 ASP C 226 26.29 40.68
REMARK 500 ASN C 252 29.98 45.84
REMARK 500 ILE C 335 72.32 36.82
REMARK 500 PHE C 336 -30.29 159.01
REMARK 500 ASP G 66 41.02 -83.11
REMARK 500 ASP G 126 82.96 151.46
REMARK 500 THR G 128 54.96 -146.26
REMARK 500 ASN G 138 16.75 52.39
REMARK 500 ASP G 140 3.49 -67.76
REMARK 500 GLU G 152 78.54 33.96
REMARK 500 SER G 172 15.79 -145.43
REMARK 500 ASP G 225 41.14 -102.03
REMARK 500 ASP G 226 27.13 40.98
REMARK 500 ILE G 335 72.79 35.72
REMARK 500 PHE G 336 -30.03 160.68
REMARK 500 ARG B 55 -168.70 -129.56
REMARK 500 ASP B 66 40.69 -86.60
REMARK 500 ASP B 126 81.40 127.44
REMARK 500 ASN B 138 17.23 51.41
REMARK 500 ASP B 140 1.01 -67.45
REMARK 500 GLU B 152 79.39 32.15
REMARK 500 SER B 172 13.69 -145.26
REMARK 500 ASP B 225 40.67 -100.99
REMARK 500 ASP B 226 26.70 39.90
REMARK 500 ASN B 252 29.58 44.23
REMARK 500 PHE B 336 -48.57 125.12
REMARK 500 ARG B 378 168.16 177.72
REMARK 500 ASP F 66 39.75 -83.27
REMARK 500 ASP F 126 79.25 164.96
REMARK 500 THR F 128 96.52 128.72
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 151 GLU A 152 131.94
REMARK 500 ILE A 335 PHE A 336 127.44
REMARK 500 SER C 125 ASP C 126 146.44
REMARK 500 GLY C 127 THR C 128 142.71
REMARK 500 PRO C 151 GLU C 152 127.30
REMARK 500 ILE C 335 PHE C 336 72.00
REMARK 500 GLY G 127 THR G 128 53.44
REMARK 500 PRO G 151 GLU G 152 72.58
REMARK 500 LYS G 332 GLY G 333 -85.80
REMARK 500 ILE G 335 PHE G 336 71.13
REMARK 500 ASP B 126 GLY B 127 59.86
REMARK 500 GLY B 127 THR B 128 51.92
REMARK 500 PRO B 151 GLU B 152 74.04
REMARK 500 ILE B 335 PHE B 336 127.73
REMARK 500 GLY F 127 THR F 128 147.27
REMARK 500 PRO F 151 GLU F 152 75.94
REMARK 500 ILE F 335 PHE F 336 71.60
REMARK 500 ASP E 126 GLY E 127 148.44
REMARK 500 GLY E 127 THR E 128 53.75
REMARK 500 PRO E 151 GLU E 152 75.21
REMARK 500 ILE E 335 PHE E 336 127.44
REMARK 500 ASP D 126 GLY D 127 64.74
REMARK 500 GLY D 127 THR D 128 47.10
REMARK 500 PRO D 151 GLU D 152 128.50
REMARK 500 ILE D 335 PHE D 336 127.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 601 DISTANCE = 10.02 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 23 OD1
REMARK 620 2 ILE A 24 O 76.7
REMARK 620 3 GLY A 26 O 152.3 76.3
REMARK 620 4 ASP A 43 OD2 105.7 72.7 71.9
REMARK 620 5 GAL H 2 O3 96.1 125.4 94.3 154.9
REMARK 620 6 GAL H 2 O4 80.0 67.8 84.1 137.5 57.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1011 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 33 O
REMARK 620 2 ASN A 72 OD1 164.7
REMARK 620 3 VAL A 73 O 88.1 93.9
REMARK 620 4 ILE A 131 O 101.3 94.0 85.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 121 OD1
REMARK 620 2 ILE A 122 O 83.6
REMARK 620 3 GLY A 124 O 170.4 103.2
REMARK 620 4 ASP A 141 OD2 98.4 81.4 76.3
REMARK 620 5 GAL I 2 O3 92.8 119.3 89.7 157.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1008 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 168 OD1
REMARK 620 2 VAL A 169 O 70.8
REMARK 620 3 GLY A 171 O 152.7 81.9
REMARK 620 4 ASP A 188 OD2 99.7 74.3 70.7
REMARK 620 5 GAL J 2 O3 96.0 126.9 101.5 157.3
REMARK 620 6 GAL J 2 O4 82.7 64.1 86.6 134.9 63.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1010 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 177 OD1
REMARK 620 2 VAL A 178 O 94.1
REMARK 620 3 ASN A 218 OD1 102.1 144.4
REMARK 620 4 VAL A 219 O 88.0 95.4 116.4
REMARK 620 5 ASP A 265 OD1 90.5 68.7 79.6 163.9
REMARK 620 6 VAL A 266 O 175.0 90.1 73.0 94.2 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1009 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 209 OD1
REMARK 620 2 VAL A 210 O 65.3
REMARK 620 3 GLY A 212 O 130.6 73.5
REMARK 620 4 ASP A 229 OD2 108.2 69.9 80.4
REMARK 620 5 ASP A 229 OD1 118.0 114.6 102.9 46.1
REMARK 620 6 GAL K 2 O3 85.8 112.7 86.1 164.9 132.5
REMARK 620 7 GAL K 2 O4 59.5 53.5 74.6 122.3 168.1 59.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 256 OD1
REMARK 620 2 VAL A 257 O 64.0
REMARK 620 3 GLY A 259 O 133.1 70.0
REMARK 620 4 ASP A 276 OD2 96.3 69.0 75.1
REMARK 620 5 GAL L 2 O3 94.9 120.9 100.8 167.8
REMARK 620 6 GAL L 2 O4 66.8 62.1 84.2 130.9 58.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1008 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 23 OD1
REMARK 620 2 ILE C 24 O 70.1
REMARK 620 3 GLY C 26 O 138.4 69.0
REMARK 620 4 ASP C 43 OD2 99.3 67.4 71.5
REMARK 620 5 ASP C 43 OD1 104.0 109.3 96.2 43.4
REMARK 620 6 GAL M 2 O6 81.8 60.2 71.8 123.6 166.0
REMARK 620 7 GAL M 2 O4 89.3 111.9 99.0 170.3 138.8 52.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1012 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE C 33 O
REMARK 620 2 ASN C 72 OD1 164.9
REMARK 620 3 VAL C 73 O 95.4 96.5
REMARK 620 4 ILE C 131 O 89.7 81.2 89.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1009 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 121 OD1
REMARK 620 2 ILE C 122 O 78.8
REMARK 620 3 GLY C 124 O 162.9 87.4
REMARK 620 4 ASP C 141 OD2 110.7 62.4 70.7
REMARK 620 5 ASP C 141 OD1 110.1 103.7 82.9 43.0
REMARK 620 6 GAL N 2 O6 72.1 64.4 92.8 124.6 167.6
REMARK 620 7 GAL N 2 O4 67.1 114.5 110.6 176.8 139.6 52.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1014 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 123 OE2
REMARK 620 2 GLU C 123 OE1 54.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 168 OD1
REMARK 620 2 VAL C 169 O 72.5
REMARK 620 3 GLY C 171 O 153.8 81.6
REMARK 620 4 ASP C 188 OD2 94.3 68.9 71.7
REMARK 620 5 GAL O 2 O3 97.6 128.6 102.1 161.3
REMARK 620 6 GAL O 2 O4 87.1 70.2 88.5 136.5 58.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1011 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 177 OD1
REMARK 620 2 VAL C 178 O 99.8
REMARK 620 3 ASN C 218 OD1 93.3 159.8
REMARK 620 4 VAL C 219 O 78.5 95.8 101.9
REMARK 620 5 ASP C 265 OD1 94.2 82.0 81.9 171.9
REMARK 620 6 VAL C 266 O 156.9 100.4 70.5 88.6 99.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1010 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 209 OD1
REMARK 620 2 VAL C 210 O 72.5
REMARK 620 3 GLY C 212 O 148.4 83.4
REMARK 620 4 ASP C 229 OD2 110.1 74.4 81.8
REMARK 620 5 GAL P 2 O3 90.8 122.2 84.9 157.3
REMARK 620 6 GAL P 2 O4 63.1 63.3 88.0 137.3 59.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 256 OD1
REMARK 620 2 VAL C 257 O 61.0
REMARK 620 3 GLY C 259 O 132.5 72.4
REMARK 620 4 ASP C 276 OD2 97.8 72.9 75.8
REMARK 620 5 GAL Q 2 O4 66.7 63.5 85.4 136.0
REMARK 620 6 GAL Q 2 O3 100.4 120.5 95.1 161.2 57.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 23 OD1
REMARK 620 2 ILE G 24 O 70.5
REMARK 620 3 GLY G 26 O 142.7 73.6
REMARK 620 4 ASP G 43 OD2 101.8 69.9 74.5
REMARK 620 5 GAL U 2 O3 90.2 121.5 100.3 166.2
REMARK 620 6 GAL U 2 O4 73.6 64.0 82.1 132.5 57.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE G 33 O
REMARK 620 2 ASN G 72 OD1 153.5
REMARK 620 3 VAL G 73 O 99.6 98.3
REMARK 620 4 ILE G 131 O 103.7 87.6 111.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 121 OD1
REMARK 620 2 ILE G 122 O 78.2
REMARK 620 3 GLY G 124 O 162.5 87.0
REMARK 620 4 GAL V 2 O3 88.8 126.0 92.7
REMARK 620 5 GAL V 2 O4 80.3 69.4 86.0 56.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 168 OD1
REMARK 620 2 VAL G 169 O 70.7
REMARK 620 3 GLY G 171 O 151.3 81.0
REMARK 620 4 ASP G 188 OD2 93.2 69.4 71.6
REMARK 620 5 GAL S 2 O3 109.1 133.8 93.9 151.7
REMARK 620 6 GAL S 2 O4 85.6 72.7 90.9 140.1 61.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN G 177 OD1
REMARK 620 2 VAL G 178 O 97.1
REMARK 620 3 ASN G 218 OD1 97.1 165.3
REMARK 620 4 VAL G 219 O 73.1 88.7 99.0
REMARK 620 5 ASP G 265 OD1 100.7 81.8 91.8 168.1
REMARK 620 6 VAL G 266 O 154.0 96.5 71.9 85.1 103.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 209 OD1
REMARK 620 2 VAL G 210 O 70.8
REMARK 620 3 GLY G 212 O 155.5 91.7
REMARK 620 4 ASP G 229 OD2 105.1 77.6 86.9
REMARK 620 5 GAL T 2 O3 93.9 125.2 82.1 154.7
REMARK 620 6 GAL T 2 O4 67.0 65.8 90.5 143.3 59.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 256 OD1
REMARK 620 2 VAL G 257 O 63.7
REMARK 620 3 GLY G 259 O 138.7 75.8
REMARK 620 4 ASP G 276 OD2 94.9 73.0 80.1
REMARK 620 5 GAL R 2 O4 67.1 63.2 88.3 136.1
REMARK 620 6 GAL R 2 O3 92.8 130.2 108.1 156.3 67.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 23 OD1
REMARK 620 2 ILE B 24 O 72.9
REMARK 620 3 GLY B 26 O 145.4 76.1
REMARK 620 4 ASP B 43 OD2 108.5 75.0 77.3
REMARK 620 5 ASP B 43 OD1 110.2 118.7 97.9 45.1
REMARK 620 6 GAL Y 2 O3 89.6 118.9 92.1 160.4 122.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 33 O
REMARK 620 2 ASN B 72 OD1 151.3
REMARK 620 3 VAL B 73 O 106.8 101.6
REMARK 620 4 ILE B 131 O 83.8 96.2 98.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 121 OD1
REMARK 620 2 ILE B 122 O 74.4
REMARK 620 3 GLY B 124 O 150.2 78.2
REMARK 620 4 ASP B 141 OD1 123.3 95.0 70.3
REMARK 620 5 GAL Z 2 O3 101.9 109.4 76.4 133.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 168 OD1
REMARK 620 2 VAL B 169 O 74.6
REMARK 620 3 GLY B 171 O 156.0 81.4
REMARK 620 4 ASP B 188 OD2 100.1 71.5 71.0
REMARK 620 5 GAL X 2 O3 106.3 124.3 87.7 152.0
REMARK 620 6 GAL X 2 O4 88.2 65.1 82.3 131.7 59.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 177 OD1
REMARK 620 2 VAL B 178 O 90.3
REMARK 620 3 ASN B 218 OD1 98.0 141.3
REMARK 620 4 VAL B 219 O 88.2 97.7 120.1
REMARK 620 5 ASP B 265 OD1 83.5 65.8 77.7 161.3
REMARK 620 6 VAL B 266 O 168.2 92.7 72.7 102.6 87.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 209 OD1
REMARK 620 2 VAL B 210 O 62.6
REMARK 620 3 GLY B 212 O 131.0 73.1
REMARK 620 4 ASP B 229 OD2 101.2 65.1 76.5
REMARK 620 5 GAL a 2 O3 87.6 113.7 92.1 168.5
REMARK 620 6 GAL a 2 O4 66.9 50.3 69.2 112.6 63.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 256 OD1
REMARK 620 2 VAL B 257 O 63.3
REMARK 620 3 GLY B 259 O 144.7 81.5
REMARK 620 4 ASP B 276 OD2 93.1 72.9 78.3
REMARK 620 5 GAL W 2 O4 65.3 73.6 103.6 145.8
REMARK 620 6 GAL W 2 O3 91.5 131.3 111.2 154.0 57.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 23 OD1
REMARK 620 2 ILE F 24 O 67.6
REMARK 620 3 GLY F 26 O 139.9 72.8
REMARK 620 4 ASP F 43 OD2 96.9 69.1 73.7
REMARK 620 5 GAL f 2 O3 73.3 89.2 101.0 158.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 510 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN F 32 OD1
REMARK 620 2 ILE F 33 O 87.5
REMARK 620 3 ASN F 72 OD1 103.4 158.1
REMARK 620 4 VAL F 73 O 125.6 98.2 90.9
REMARK 620 5 ILE F 131 O 149.2 93.2 67.7 84.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY F 124 O
REMARK 620 2 ASP F 141 OD1 77.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 168 OD1
REMARK 620 2 VAL F 169 O 71.5
REMARK 620 3 GLY F 171 O 150.8 79.7
REMARK 620 4 ASP F 188 OD2 100.5 73.7 74.9
REMARK 620 5 ASP F 188 OD1 92.5 112.2 102.7 44.4
REMARK 620 6 GAL e 2 O3 112.1 118.8 77.8 147.2 128.0
REMARK 620 7 GAL e 2 O4 89.2 64.5 74.1 131.3 175.6 54.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 509 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN F 177 OD1
REMARK 620 2 VAL F 178 O 105.3
REMARK 620 3 ASN F 218 OD1 98.1 146.1
REMARK 620 4 VAL F 219 O 87.0 99.8 105.7
REMARK 620 5 ASP F 265 OD1 95.9 75.2 78.3 174.7
REMARK 620 6 VAL F 266 O 163.3 91.4 67.2 89.7 88.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 209 OD1
REMARK 620 2 VAL F 210 O 69.5
REMARK 620 3 GLY F 212 O 153.9 89.4
REMARK 620 4 ASP F 229 OD2 103.2 75.0 84.9
REMARK 620 5 GAL d 2 O4 70.3 69.4 88.4 143.8
REMARK 620 6 GAL d 2 O3 89.6 129.3 92.6 155.6 60.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 256 OD1
REMARK 620 2 VAL F 257 O 75.1
REMARK 620 3 GLY F 259 O 160.8 86.6
REMARK 620 4 ASP F 276 OD2 93.2 75.4 76.5
REMARK 620 5 GAL c 2 O3 100.3 136.6 96.8 147.6
REMARK 620 6 GAL c 2 O4 77.7 78.5 104.4 153.7 58.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 23 OD1
REMARK 620 2 ILE E 24 O 75.9
REMARK 620 3 GLY E 26 O 150.4 75.5
REMARK 620 4 ASP E 43 OD2 105.1 72.4 73.2
REMARK 620 5 GAL k 2 O4 80.6 71.7 83.3 140.9
REMARK 620 6 GAL k 2 O3 111.7 130.9 81.9 140.1 62.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 513 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE E 33 O
REMARK 620 2 ASN E 72 OD1 176.8
REMARK 620 3 VAL E 73 O 95.0 84.6
REMARK 620 4 ILE E 131 O 103.0 80.2 90.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 121 OD1
REMARK 620 2 ILE E 122 O 69.4
REMARK 620 3 GLY E 124 O 148.2 79.2
REMARK 620 4 ASP E 141 OD2 100.9 61.7 67.2
REMARK 620 5 GAL l 2 O3 95.5 117.1 94.1 161.3
REMARK 620 6 GAL l 2 O4 73.8 62.3 87.4 121.6 54.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 168 OD1
REMARK 620 2 VAL E 169 O 71.8
REMARK 620 3 GLY E 171 O 149.8 78.1
REMARK 620 4 ASP E 188 OD2 98.8 72.4 70.6
REMARK 620 5 GAL i 2 O3 100.5 121.9 96.1 159.0
REMARK 620 6 GAL i 2 O4 83.6 63.5 83.9 132.7 58.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 177 OD1
REMARK 620 2 VAL E 178 O 95.5
REMARK 620 3 ASN E 218 OD1 102.7 153.0
REMARK 620 4 VAL E 219 O 81.5 91.1 111.1
REMARK 620 5 ASP E 265 OD1 94.5 72.3 86.3 162.6
REMARK 620 6 VAL E 266 O 170.7 91.6 73.0 92.3 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 209 OD1
REMARK 620 2 VAL E 210 O 69.0
REMARK 620 3 GLY E 212 O 151.7 86.7
REMARK 620 4 ASP E 229 OD2 102.4 73.9 83.5
REMARK 620 5 GAL j 2 O3 95.6 130.4 89.4 154.2
REMARK 620 6 GAL j 2 O4 67.8 69.1 90.7 142.8 61.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 515 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 211 OE1
REMARK 620 2 GLU E 211 OE2 59.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 256 OD1
REMARK 620 2 VAL E 257 O 63.7
REMARK 620 3 GLY E 259 O 135.6 73.2
REMARK 620 4 ASP E 276 OD2 102.2 74.1 74.7
REMARK 620 5 GAL h 2 O4 67.3 63.1 84.4 136.2
REMARK 620 6 GAL h 2 O3 96.4 124.7 99.4 158.5 61.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 23 OD1
REMARK 620 2 ILE D 24 O 77.4
REMARK 620 3 GLY D 26 O 156.0 79.5
REMARK 620 4 ASP D 43 OD2 103.4 72.9 75.6
REMARK 620 5 GAL o 2 O3 98.9 129.2 90.8 152.1
REMARK 620 6 GAL o 2 O4 77.9 69.3 88.0 140.9 60.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 511 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE D 33 O
REMARK 620 2 ASN D 72 OD1 171.2
REMARK 620 3 VAL D 73 O 87.9 92.7
REMARK 620 4 ILE D 131 O 88.2 100.5 85.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 121 OD1
REMARK 620 2 ILE D 122 O 73.5
REMARK 620 3 GLY D 124 O 152.5 80.2
REMARK 620 4 ASP D 141 OD2 113.0 60.5 57.9
REMARK 620 5 ASP D 141 OD1 119.6 102.1 73.4 43.2
REMARK 620 6 GAL p 2 O4 71.5 63.9 90.0 118.9 160.4
REMARK 620 7 GAL p 2 O3 89.3 119.7 97.0 154.9 135.0 55.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 168 OD1
REMARK 620 2 VAL D 169 O 73.9
REMARK 620 3 GLY D 171 O 153.7 82.3
REMARK 620 4 ASP D 188 OD2 93.5 70.1 67.5
REMARK 620 5 GAL r 2 O3 103.7 133.2 100.6 154.0
REMARK 620 6 GAL r 2 O4 91.3 70.7 91.2 137.3 62.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 510 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 177 OD1
REMARK 620 2 VAL D 178 O 95.9
REMARK 620 3 ASN D 218 OD1 95.0 146.8
REMARK 620 4 VAL D 219 O 85.5 100.0 112.0
REMARK 620 5 ASP D 265 OD1 88.1 71.8 77.3 169.0
REMARK 620 6 VAL D 266 O 165.7 96.9 70.8 98.4 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 209 OD1
REMARK 620 2 VAL D 210 O 75.4
REMARK 620 3 GLY D 212 O 157.0 96.6
REMARK 620 4 ASP D 229 OD2 108.8 84.4 91.5
REMARK 620 5 GAL q 2 O4 67.9 65.9 89.1 150.2
REMARK 620 6 GAL q 2 O3 74.3 129.1 95.9 144.1 65.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 256 OD1
REMARK 620 2 VAL D 257 O 67.4
REMARK 620 3 GLY D 259 O 153.0 86.0
REMARK 620 4 ASP D 276 OD2 95.6 77.6 82.3
REMARK 620 5 GAL n 2 O4 73.5 70.5 94.0 148.1
REMARK 620 6 GAL n 2 O3 97.3 131.4 97.2 151.0 60.8
REMARK 620 N 1 2 3 4 5
DBREF 3W9T A 1 432 PDB 3W9T 3W9T 1 432
DBREF 3W9T C 1 432 PDB 3W9T 3W9T 1 432
DBREF 3W9T G 1 432 PDB 3W9T 3W9T 1 432
DBREF 3W9T B 1 432 PDB 3W9T 3W9T 1 432
DBREF 3W9T F 1 432 PDB 3W9T 3W9T 1 432
DBREF 3W9T E 1 432 PDB 3W9T 3W9T 1 432
DBREF 3W9T D 1 432 PDB 3W9T 3W9T 1 432
SEQRES 1 A 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 A 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 A 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 A 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 A 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 A 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 A 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 A 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 A 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 A 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 A 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 A 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 A 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 A 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 A 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 A 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 A 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 A 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 A 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 A 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 A 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 A 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 A 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 A 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 A 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 A 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 A 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 A 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 A 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 A 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 A 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 A 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 A 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 A 432 THR ASP ILE
SEQRES 1 C 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 C 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 C 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 C 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 C 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 C 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 C 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 C 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 C 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 C 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 C 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 C 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 C 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 C 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 C 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 C 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 C 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 C 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 C 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 C 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 C 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 C 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 C 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 C 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 C 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 C 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 C 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 C 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 C 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 C 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 C 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 C 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 C 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 C 432 THR ASP ILE
SEQRES 1 G 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 G 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 G 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 G 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 G 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 G 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 G 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 G 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 G 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 G 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 G 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 G 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 G 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 G 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 G 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 G 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 G 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 G 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 G 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 G 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 G 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 G 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 G 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 G 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 G 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 G 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 G 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 G 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 G 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 G 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 G 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 G 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 G 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 G 432 THR ASP ILE
SEQRES 1 B 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 B 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 B 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 B 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 B 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 B 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 B 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 B 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 B 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 B 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 B 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 B 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 B 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 B 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 B 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 B 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 B 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 B 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 B 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 B 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 B 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 B 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 B 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 B 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 B 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 B 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 B 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 B 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 B 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 B 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 B 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 B 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 B 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 B 432 THR ASP ILE
SEQRES 1 F 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 F 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 F 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 F 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 F 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 F 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 F 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 F 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 F 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 F 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 F 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 F 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 F 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 F 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 F 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 F 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 F 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 F 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 F 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 F 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 F 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 F 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 F 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 F 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 F 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 F 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 F 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 F 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 F 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 F 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 F 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 F 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 F 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 F 432 THR ASP ILE
SEQRES 1 E 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 E 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 E 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 E 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 E 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 E 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 E 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 E 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 E 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 E 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 E 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 E 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 E 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 E 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 E 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 E 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 E 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 E 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 E 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 E 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 E 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 E 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 E 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 E 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 E 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 E 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 E 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 E 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 E 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 E 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 E 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 E 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 E 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 E 432 THR ASP ILE
SEQRES 1 D 432 PCA VAL LEU CYS THR ASN PRO LEU ASP ILE GLY GLU LEU
SEQRES 2 D 432 ARG SER PHE LYS SER LYS GLN CYS VAL ASP ILE VAL GLY
SEQRES 3 D 432 ASN GLN GLY SER GLY ASN ILE ALA THR TYR ASP CYS ASP
SEQRES 4 D 432 GLY LEU SER ASP GLN GLN ILE ILE ILE CYS GLY ASP GLY
SEQRES 5 D 432 THR ILE ARG ASN GLU ALA ARG ASN TYR CYS PHE THR PRO
SEQRES 6 D 432 ASP GLY SER GLY ASN ALA ASN VAL MET SER SER PRO CYS
SEQRES 7 D 432 THR LEU TYR PRO GLU ILE PRO SER SER GLN ARG TRP ARG
SEQRES 8 D 432 GLN GLY ARG ARG LYS THR PHE THR ASP ASN GLY GLY ILE
SEQRES 9 D 432 GLU GLN VAL ALA THR GLU ILE ILE ASN LEU ALA SER GLY
SEQRES 10 D 432 LYS CYS LEU ASP ILE GLU GLY SER ASP GLY THR GLY ASP
SEQRES 11 D 432 ILE GLY VAL TYR ASP CYS GLN ASN LEU ASP ASP GLN TYR
SEQRES 12 D 432 PHE TYR VAL ARG SER ARG GLY PRO GLU LEU PHE TYR GLY
SEQRES 13 D 432 ARG LEU ARG ASN GLU LYS SER ASP LEU CYS LEU ASP VAL
SEQRES 14 D 432 GLU GLY SER ASP GLY LYS GLY ASN VAL LEU MET TYR SER
SEQRES 15 D 432 CYS GLU ASP ASN LEU ASP GLN TRP PHE ARG TYR TYR GLU
SEQRES 16 D 432 ASN GLY GLU ILE VAL ASN ALA LYS SER GLY MET CYS LEU
SEQRES 17 D 432 ASP VAL GLU GLY SER ASP GLY SER GLY ASN VAL GLY ILE
SEQRES 18 D 432 TYR ARG CYS ASP ASP LEU ARG ASP GLN MET TRP SER ARG
SEQRES 19 D 432 PRO ASN ALA TYR CYS ASN GLY ASP TYR CYS SER PHE LEU
SEQRES 20 D 432 ASN LYS GLU SER ASN LYS CYS LEU ASP VAL SER GLY ASP
SEQRES 21 D 432 GLN GLY THR GLY ASP VAL GLY THR TRP GLN CYS ASP GLY
SEQRES 22 D 432 LEU PRO ASP GLN ARG PHE LYS TRP VAL PHE ASP ASP TRP
SEQRES 23 D 432 GLU VAL PRO THR ALA THR TRP ASN MET VAL GLY CYS ASP
SEQRES 24 D 432 GLN ASN GLY LYS VAL SER GLN GLN ILE SER ASN THR ILE
SEQRES 25 D 432 SER PHE SER SER THR VAL THR ALA GLY VAL ALA VAL GLU
SEQRES 26 D 432 VAL SER SER THR ILE GLU LYS GLY VAL ILE PHE ALA LYS
SEQRES 27 D 432 ALA THR VAL SER VAL LYS VAL THR ALA SER LEU SER LYS
SEQRES 28 D 432 ALA TRP THR ASN SER GLN SER GLY THR THR ALA ILE THR
SEQRES 29 D 432 TYR THR CYS ASP ASN TYR ASP SER ASP GLU GLU PHE THR
SEQRES 30 D 432 ARG GLY CYS MET TRP GLN LEU ALA ILE GLU THR THR GLU
SEQRES 31 D 432 VAL LYS SER GLY ASP LEU LEU VAL TRP ASN PRO GLN ILE
SEQRES 32 D 432 VAL LYS CYS THR ARG SER ASN THR ALA PRO GLY CYS ALA
SEQRES 33 D 432 PRO PHE THR LYS CYS ALA ASN GLU ASP CYS THR PHE CYS
SEQRES 34 D 432 THR ASP ILE
MODRES 3W9T PCA A 1 GLN PYROGLUTAMIC ACID
MODRES 3W9T PCA C 1 GLN PYROGLUTAMIC ACID
MODRES 3W9T PCA G 1 GLN PYROGLUTAMIC ACID
MODRES 3W9T PCA B 1 GLN PYROGLUTAMIC ACID
MODRES 3W9T PCA F 1 GLN PYROGLUTAMIC ACID
MODRES 3W9T PCA E 1 GLN PYROGLUTAMIC ACID
MODRES 3W9T PCA D 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET PCA C 1 8
HET PCA G 1 8
HET PCA B 1 8
HET PCA F 1 8
HET PCA E 1 8
HET PCA D 1 8
HET FRU H 1 12
HET GAL H 2 11
HET FRU I 1 12
HET GAL I 2 11
HET FRU J 1 12
HET GAL J 2 11
HET FRU K 1 12
HET GAL K 2 11
HET FRU L 1 12
HET GAL L 2 11
HET FRU M 1 12
HET GAL M 2 11
HET FRU N 1 12
HET GAL N 2 11
HET FRU O 1 12
HET GAL O 2 11
HET FRU P 1 12
HET GAL P 2 11
HET FRU Q 1 12
HET GAL Q 2 11
HET FRU R 1 12
HET GAL R 2 11
HET FRU S 1 12
HET GAL S 2 11
HET FRU T 1 12
HET GAL T 2 11
HET FRU U 1 12
HET GAL U 2 11
HET FRU V 1 12
HET GAL V 2 11
HET FRU W 1 12
HET GAL W 2 11
HET FRU X 1 12
HET GAL X 2 11
HET FRU Y 1 12
HET GAL Y 2 11
HET FRU Z 1 12
HET GAL Z 2 11
HET FRU a 1 12
HET GAL a 2 11
HET FRU b 1 12
HET GAL b 2 11
HET FRU c 1 12
HET GAL c 2 11
HET FRU d 1 12
HET GAL d 2 11
HET FRU e 1 12
HET GAL e 2 11
HET FRU f 1 12
HET GAL f 2 11
HET FRU g 1 12
HET GAL g 2 11
HET FRU h 1 12
HET GAL h 2 11
HET FRU i 1 12
HET GAL i 2 11
HET FRU j 1 12
HET GAL j 2 11
HET FRU k 1 12
HET GAL k 2 11
HET FRU l 1 12
HET GAL l 2 11
HET FRU m 1 12
HET GAL m 2 11
HET FRU n 1 12
HET GAL n 2 11
HET FRU o 1 12
HET GAL o 2 11
HET FRU p 1 12
HET GAL p 2 11
HET FRU q 1 12
HET GAL q 2 11
HET FRU r 1 12
HET GAL r 2 11
HET CA A1005 1
HET CA A1006 1
HET CA A1007 1
HET CA A1008 1
HET CA A1009 1
HET MG A1010 1
HET MG A1011 1
HET CA A1013 1
HET CA C1006 1
HET CA C1007 1
HET CA C1008 1
HET CA C1009 1
HET CA C1010 1
HET MG C1011 1
HET MG C1012 1
HET CA C1013 1
HET CA C1014 1
HET CA G 506 1
HET CA G 507 1
HET CA G 508 1
HET CA G 509 1
HET CA G 510 1
HET MG G 511 1
HET MG G 512 1
HET CA G 513 1
HET CA B 505 1
HET CA B 506 1
HET CA B 508 1
HET CA B 509 1
HET CA B 510 1
HET MG B 511 1
HET MG B 512 1
HET CA B 514 1
HET CA F 505 1
HET CA F 506 1
HET CA F 507 1
HET CA F 508 1
HET MG F 509 1
HET MG F 510 1
HET CA F 511 1
HET CA F 513 1
HET CA E 507 1
HET CA E 508 1
HET CA E 509 1
HET CA E 510 1
HET CA E 511 1
HET MG E 512 1
HET MG E 513 1
HET CA E 514 1
HET CA E 515 1
HET CA D 503 1
HET CA D 504 1
HET CA D 505 1
HET CA D 508 1
HET CA D 509 1
HET MG D 510 1
HET MG D 511 1
HET CA D 513 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
FORMUL 1 PCA 7(C5 H7 N O3)
FORMUL 8 FRU 37(C6 H12 O6)
FORMUL 8 GAL 37(C6 H12 O6)
FORMUL 45 CA 44(CA 2+)
FORMUL 50 MG 14(MG 2+)
FORMUL 03 HOH *75(H2 O)
HELIX 1 1 LEU A 41 ASP A 43 5 3
HELIX 2 2 PRO A 85 GLN A 88 5 4
HELIX 3 3 ASN A 186 GLN A 189 5 4
HELIX 4 4 LEU A 227 GLN A 230 5 4
HELIX 5 5 PRO A 235 CYS A 239 5 5
HELIX 6 6 LEU A 274 GLN A 277 5 4
HELIX 7 7 LEU C 41 ASP C 43 5 3
HELIX 8 8 PRO C 85 GLN C 88 5 4
HELIX 9 9 ASN C 186 GLN C 189 5 4
HELIX 10 10 LEU C 227 GLN C 230 5 4
HELIX 11 11 PRO C 235 CYS C 239 5 5
HELIX 12 12 LEU C 274 GLN C 277 5 4
HELIX 13 13 LEU G 41 ASP G 43 5 3
HELIX 14 14 PRO G 85 GLN G 88 5 4
HELIX 15 15 ASN G 186 GLN G 189 5 4
HELIX 16 16 LEU G 227 GLN G 230 5 4
HELIX 17 17 PRO G 235 CYS G 239 5 5
HELIX 18 18 LEU G 274 GLN G 277 5 4
HELIX 19 19 LEU B 41 ASP B 43 5 3
HELIX 20 20 PRO B 85 GLN B 88 5 4
HELIX 21 21 ASN B 186 GLN B 189 5 4
HELIX 22 22 LEU B 227 GLN B 230 5 4
HELIX 23 23 PRO B 235 CYS B 239 5 5
HELIX 24 24 LEU B 274 GLN B 277 5 4
HELIX 25 25 LEU F 41 ASP F 43 5 3
HELIX 26 26 PRO F 85 GLN F 88 5 4
HELIX 27 27 ASN F 186 GLN F 189 5 4
HELIX 28 28 LEU F 227 GLN F 230 5 4
HELIX 29 29 PRO F 235 CYS F 239 5 5
HELIX 30 30 LEU F 274 GLN F 277 5 4
HELIX 31 31 LEU E 41 ASP E 43 5 3
HELIX 32 32 PRO E 85 GLN E 88 5 4
HELIX 33 33 ASN E 186 GLN E 189 5 4
HELIX 34 34 LEU E 227 GLN E 230 5 4
HELIX 35 35 PRO E 235 CYS E 239 5 5
HELIX 36 36 LEU E 274 GLN E 277 5 4
HELIX 37 37 LEU D 41 ASP D 43 5 3
HELIX 38 38 PRO D 85 GLN D 88 5 4
HELIX 39 39 ASN D 186 GLN D 189 5 4
HELIX 40 40 LEU D 227 GLN D 230 5 4
HELIX 41 41 PRO D 235 CYS D 239 5 5
HELIX 42 42 LEU D 274 GLN D 277 5 4
SHEET 1 A 4 ILE A 54 ASN A 56 0
SHEET 2 A 4 GLN A 45 CYS A 49 -1 N ILE A 47 O ARG A 55
SHEET 3 A 4 PRO A 7 SER A 15 -1 N ASP A 9 O ILE A 48
SHEET 4 A 4 PHE A 144 VAL A 146 -1 O TYR A 145 N ARG A 14
SHEET 1 B 4 CYS A 21 ILE A 24 0
SHEET 2 B 4 GLY A 31 TYR A 36 -1 O ALA A 34 N ASP A 23
SHEET 3 B 4 VAL A 73 PRO A 77 -1 O SER A 75 N GLY A 31
SHEET 4 B 4 TYR A 61 PRO A 65 -1 N THR A 64 O MET A 74
SHEET 1 C 2 TRP A 90 THR A 99 0
SHEET 2 C 2 GLU A 105 ASN A 113 -1 O ILE A 112 N ARG A 91
SHEET 1 D 2 ASP A 121 ILE A 122 0
SHEET 2 D 2 ILE A 131 GLY A 132 -1 O GLY A 132 N ASP A 121
SHEET 1 E 5 ILE A 199 ASN A 201 0
SHEET 2 E 5 PHE A 191 TYR A 194 -1 N ARG A 192 O VAL A 200
SHEET 3 E 5 GLU A 152 ASN A 160 -1 N LEU A 153 O TYR A 193
SHEET 4 E 5 PHE A 279 VAL A 282 -1 O LYS A 280 N ARG A 159
SHEET 5 E 5 TYR A 243 CYS A 244 -1 N CYS A 244 O PHE A 279
SHEET 1 F 4 CYS A 166 VAL A 169 0
SHEET 2 F 4 GLY A 176 TYR A 181 -1 O LEU A 179 N ASP A 168
SHEET 3 F 4 VAL A 219 TYR A 222 -1 O ILE A 221 N GLY A 176
SHEET 4 F 4 CYS A 207 VAL A 210 -1 N ASP A 209 O GLY A 220
SHEET 1 G 2 TRP A 232 SER A 233 0
SHEET 2 G 2 LEU A 247 ASN A 248 -1 O LEU A 247 N SER A 233
SHEET 1 H 2 CYS A 254 VAL A 257 0
SHEET 2 H 2 VAL A 266 TRP A 269 -1 O GLY A 267 N ASP A 256
SHEET 1 I22 TRP A 293 ASP A 299 0
SHEET 2 I22 GLY A 379 LEU A 384 -1 O GLN A 383 N ASN A 294
SHEET 3 I22 ILE A 403 THR A 407 -1 O LYS A 405 N TRP A 382
SHEET 4 I22 TRP G 293 ASP G 299 1 O CYS G 298 N VAL A 404
SHEET 5 I22 GLY G 379 LEU G 384 -1 O MET G 381 N VAL G 296
SHEET 6 I22 ILE G 403 THR G 407 -1 O LYS G 405 N TRP G 382
SHEET 7 I22 TRP F 293 ASP F 299 1 O CYS F 298 N VAL G 404
SHEET 8 I22 GLY F 379 LEU F 384 -1 O GLN F 383 N ASN F 294
SHEET 9 I22 ILE F 403 THR F 407 -1 O LYS F 405 N TRP F 382
SHEET 10 I22 TRP E 293 ASP E 299 1 O CYS E 298 N VAL F 404
SHEET 11 I22 GLY E 379 LEU E 384 -1 O GLN E 383 N ASN E 294
SHEET 12 I22 ILE E 403 THR E 407 -1 O LYS E 405 N TRP E 382
SHEET 13 I22 TRP D 293 ASP D 299 1 O CYS D 298 N VAL E 404
SHEET 14 I22 GLY D 379 LEU D 384 -1 O GLN D 383 N ASN D 294
SHEET 15 I22 ILE D 403 THR D 407 -1 O LYS D 405 N TRP D 382
SHEET 16 I22 TRP C 293 ASP C 299 1 N CYS C 298 O VAL D 404
SHEET 17 I22 GLY C 379 LEU C 384 -1 O GLN C 383 N ASN C 294
SHEET 18 I22 ILE C 403 THR C 407 -1 O LYS C 405 N TRP C 382
SHEET 19 I22 TRP B 293 ASP B 299 1 O CYS B 298 N VAL C 404
SHEET 20 I22 GLY B 379 LEU B 384 -1 O GLY B 379 N ASP B 299
SHEET 21 I22 ILE B 403 THR B 407 -1 O LYS B 405 N TRP B 382
SHEET 22 I22 TRP A 293 ASP A 299 1 N CYS A 298 O VAL B 404
SHEET 1 J18 ALA C 337 THR C 366 0
SHEET 2 J18 SER C 328 LYS C 332 -1 N SER C 328 O VAL C 343
SHEET 3 J18 ALA D 337 THR D 366 -1 O LYS D 338 N GLU C 331
SHEET 4 J18 ALA C 337 THR C 366 0
SHEET 5 J18 VAL C 304 GLU C 325 -1 N ILE C 308 O ILE C 363
SHEET 6 J18 ALA D 337 THR D 366 -1 O THR D 354 N SER C 315
SHEET 7 J18 VAL B 304 LYS B 332 0
SHEET 8 J18 ALA B 337 THR B 366 -1 O VAL B 345 N VAL B 326
SHEET 9 J18 VAL A 304 LYS A 332 -1 N SER A 315 O THR B 354
SHEET 10 J18 ALA A 337 THR A 366 -1 O VAL A 345 N VAL A 326
SHEET 11 J18 VAL G 304 LYS G 332 -1 O SER G 315 N THR A 354
SHEET 12 J18 ALA G 337 THR G 366 -1 O VAL G 345 N VAL G 326
SHEET 13 J18 VAL F 304 LYS F 332 -1 O SER F 327 N SER G 342
SHEET 14 J18 ALA F 337 THR F 366 -1 O VAL F 345 N VAL F 326
SHEET 15 J18 VAL E 304 LYS E 332 -1 O SER E 315 N THR F 354
SHEET 16 J18 ALA E 337 THR E 366 -1 O VAL E 345 N VAL E 326
SHEET 17 J18 VAL D 304 LYS D 332 -1 O SER D 327 N SER E 342
SHEET 18 J18 ALA D 337 THR D 366 -1 O VAL D 345 N VAL D 326
SHEET 1 K 2 VAL A 391 SER A 393 0
SHEET 2 K 2 LEU A 397 TRP A 399 -1 O TRP A 399 N VAL A 391
SHEET 1 L 2 THR A 419 CYS A 421 0
SHEET 2 L 2 CYS A 429 ASP A 431 -1 O THR A 430 N LYS A 420
SHEET 1 M 4 ILE C 54 ASN C 56 0
SHEET 2 M 4 GLN C 45 CYS C 49 -1 N ILE C 47 O ARG C 55
SHEET 3 M 4 PRO C 7 SER C 15 -1 N ASP C 9 O ILE C 48
SHEET 4 M 4 PHE C 144 VAL C 146 -1 O TYR C 145 N ARG C 14
SHEET 1 N 4 CYS C 21 ILE C 24 0
SHEET 2 N 4 GLY C 31 TYR C 36 -1 O ALA C 34 N ASP C 23
SHEET 3 N 4 VAL C 73 PRO C 77 -1 O SER C 75 N GLY C 31
SHEET 4 N 4 TYR C 61 PRO C 65 -1 N THR C 64 O MET C 74
SHEET 1 O 2 TRP C 90 THR C 99 0
SHEET 2 O 2 GLU C 105 ASN C 113 -1 O ILE C 112 N ARG C 91
SHEET 1 P 2 CYS C 119 ILE C 122 0
SHEET 2 P 2 ILE C 131 TYR C 134 -1 O TYR C 134 N CYS C 119
SHEET 1 Q 5 ILE C 199 ASN C 201 0
SHEET 2 Q 5 PHE C 191 TYR C 194 -1 N ARG C 192 O VAL C 200
SHEET 3 Q 5 GLU C 152 ASN C 160 -1 N LEU C 153 O TYR C 193
SHEET 4 Q 5 PHE C 279 VAL C 282 -1 O LYS C 280 N ARG C 159
SHEET 5 Q 5 TYR C 243 CYS C 244 -1 N CYS C 244 O PHE C 279
SHEET 1 R 4 CYS C 166 VAL C 169 0
SHEET 2 R 4 GLY C 176 TYR C 181 -1 O TYR C 181 N CYS C 166
SHEET 3 R 4 VAL C 219 TYR C 222 -1 O ILE C 221 N GLY C 176
SHEET 4 R 4 CYS C 207 VAL C 210 -1 N ASP C 209 O GLY C 220
SHEET 1 S 2 TRP C 232 SER C 233 0
SHEET 2 S 2 LEU C 247 ASN C 248 -1 O LEU C 247 N SER C 233
SHEET 1 T 2 CYS C 254 VAL C 257 0
SHEET 2 T 2 VAL C 266 TRP C 269 -1 O GLY C 267 N ASP C 256
SHEET 1 U 2 VAL C 391 SER C 393 0
SHEET 2 U 2 LEU C 397 TRP C 399 -1 O TRP C 399 N VAL C 391
SHEET 1 V 2 THR C 419 CYS C 421 0
SHEET 2 V 2 CYS C 429 ASP C 431 -1 O THR C 430 N LYS C 420
SHEET 1 W 4 ILE G 54 ASN G 56 0
SHEET 2 W 4 GLN G 45 CYS G 49 -1 N ILE G 47 O ARG G 55
SHEET 3 W 4 PRO G 7 SER G 15 -1 N ASP G 9 O ILE G 48
SHEET 4 W 4 PHE G 144 VAL G 146 -1 O TYR G 145 N ARG G 14
SHEET 1 X 4 CYS G 21 ILE G 24 0
SHEET 2 X 4 GLY G 31 TYR G 36 -1 O ALA G 34 N ASP G 23
SHEET 3 X 4 VAL G 73 PRO G 77 -1 O SER G 75 N GLY G 31
SHEET 4 X 4 TYR G 61 PRO G 65 -1 N THR G 64 O MET G 74
SHEET 1 Y 2 TRP G 90 THR G 99 0
SHEET 2 Y 2 GLU G 105 ASN G 113 -1 O GLN G 106 N PHE G 98
SHEET 1 Z 2 CYS G 119 ILE G 122 0
SHEET 2 Z 2 ILE G 131 TYR G 134 -1 O GLY G 132 N ASP G 121
SHEET 1 AA 5 ILE G 199 ASN G 201 0
SHEET 2 AA 5 PHE G 191 TYR G 194 -1 N ARG G 192 O VAL G 200
SHEET 3 AA 5 GLU G 152 ASN G 160 -1 N LEU G 153 O TYR G 193
SHEET 4 AA 5 PHE G 279 VAL G 282 -1 O LYS G 280 N ARG G 159
SHEET 5 AA 5 TYR G 243 CYS G 244 -1 N CYS G 244 O PHE G 279
SHEET 1 AB 4 CYS G 166 VAL G 169 0
SHEET 2 AB 4 GLY G 176 TYR G 181 -1 O LEU G 179 N ASP G 168
SHEET 3 AB 4 VAL G 219 TYR G 222 -1 O ILE G 221 N GLY G 176
SHEET 4 AB 4 CYS G 207 VAL G 210 -1 N ASP G 209 O GLY G 220
SHEET 1 AC 2 TRP G 232 SER G 233 0
SHEET 2 AC 2 LEU G 247 ASN G 248 -1 O LEU G 247 N SER G 233
SHEET 1 AD 2 CYS G 254 VAL G 257 0
SHEET 2 AD 2 VAL G 266 TRP G 269 -1 O GLY G 267 N ASP G 256
SHEET 1 AE 2 VAL G 391 SER G 393 0
SHEET 2 AE 2 LEU G 397 TRP G 399 -1 O TRP G 399 N VAL G 391
SHEET 1 AF 2 THR G 419 CYS G 421 0
SHEET 2 AF 2 CYS G 429 ASP G 431 -1 O THR G 430 N LYS G 420
SHEET 1 AG 4 ILE B 54 ASN B 56 0
SHEET 2 AG 4 GLN B 45 CYS B 49 -1 N ILE B 47 O ARG B 55
SHEET 3 AG 4 PRO B 7 SER B 15 -1 N ASP B 9 O ILE B 48
SHEET 4 AG 4 PHE B 144 VAL B 146 -1 O TYR B 145 N ARG B 14
SHEET 1 AH 4 CYS B 21 ILE B 24 0
SHEET 2 AH 4 GLY B 31 TYR B 36 -1 O ALA B 34 N ASP B 23
SHEET 3 AH 4 VAL B 73 PRO B 77 -1 O SER B 75 N GLY B 31
SHEET 4 AH 4 TYR B 61 PRO B 65 -1 N THR B 64 O MET B 74
SHEET 1 AI 2 TRP B 90 THR B 99 0
SHEET 2 AI 2 GLU B 105 ASN B 113 -1 O ILE B 112 N ARG B 91
SHEET 1 AJ 2 CYS B 119 ILE B 122 0
SHEET 2 AJ 2 ILE B 131 TYR B 134 -1 O GLY B 132 N ASP B 121
SHEET 1 AK 5 ILE B 199 ASN B 201 0
SHEET 2 AK 5 PHE B 191 TYR B 194 -1 N ARG B 192 O VAL B 200
SHEET 3 AK 5 GLU B 152 ASN B 160 -1 N LEU B 153 O TYR B 193
SHEET 4 AK 5 PHE B 279 VAL B 282 -1 O LYS B 280 N ARG B 159
SHEET 5 AK 5 TYR B 243 CYS B 244 -1 N CYS B 244 O PHE B 279
SHEET 1 AL 4 CYS B 166 VAL B 169 0
SHEET 2 AL 4 GLY B 176 TYR B 181 -1 O LEU B 179 N ASP B 168
SHEET 3 AL 4 VAL B 219 TYR B 222 -1 O ILE B 221 N GLY B 176
SHEET 4 AL 4 CYS B 207 VAL B 210 -1 N ASP B 209 O GLY B 220
SHEET 1 AM 2 TRP B 232 SER B 233 0
SHEET 2 AM 2 LEU B 247 ASN B 248 -1 O LEU B 247 N SER B 233
SHEET 1 AN 2 CYS B 254 VAL B 257 0
SHEET 2 AN 2 VAL B 266 TRP B 269 -1 O GLY B 267 N ASP B 256
SHEET 1 AO 2 VAL B 391 SER B 393 0
SHEET 2 AO 2 LEU B 397 TRP B 399 -1 O TRP B 399 N VAL B 391
SHEET 1 AP 2 THR B 419 CYS B 421 0
SHEET 2 AP 2 CYS B 429 ASP B 431 -1 O THR B 430 N LYS B 420
SHEET 1 AQ 4 ILE F 54 ASN F 56 0
SHEET 2 AQ 4 GLN F 45 CYS F 49 -1 N ILE F 47 O ARG F 55
SHEET 3 AQ 4 PRO F 7 SER F 15 -1 N ASP F 9 O ILE F 48
SHEET 4 AQ 4 PHE F 144 VAL F 146 -1 O TYR F 145 N ARG F 14
SHEET 1 AR 4 CYS F 21 ILE F 24 0
SHEET 2 AR 4 GLY F 31 TYR F 36 -1 O ALA F 34 N ASP F 23
SHEET 3 AR 4 VAL F 73 PRO F 77 -1 O SER F 75 N GLY F 31
SHEET 4 AR 4 TYR F 61 PRO F 65 -1 N THR F 64 O MET F 74
SHEET 1 AS 2 TRP F 90 THR F 99 0
SHEET 2 AS 2 GLU F 105 ASN F 113 -1 O ILE F 112 N ARG F 91
SHEET 1 AT 2 CYS F 119 ILE F 122 0
SHEET 2 AT 2 ILE F 131 TYR F 134 -1 O GLY F 132 N ASP F 121
SHEET 1 AU 5 ILE F 199 ASN F 201 0
SHEET 2 AU 5 PHE F 191 TYR F 194 -1 N ARG F 192 O VAL F 200
SHEET 3 AU 5 GLU F 152 ASN F 160 -1 N LEU F 153 O TYR F 193
SHEET 4 AU 5 PHE F 279 VAL F 282 -1 O LYS F 280 N ARG F 159
SHEET 5 AU 5 TYR F 243 CYS F 244 -1 N CYS F 244 O PHE F 279
SHEET 1 AV 4 CYS F 166 VAL F 169 0
SHEET 2 AV 4 GLY F 176 TYR F 181 -1 O LEU F 179 N ASP F 168
SHEET 3 AV 4 VAL F 219 TYR F 222 -1 O ILE F 221 N GLY F 176
SHEET 4 AV 4 CYS F 207 VAL F 210 -1 N ASP F 209 O GLY F 220
SHEET 1 AW 2 TRP F 232 SER F 233 0
SHEET 2 AW 2 LEU F 247 ASN F 248 -1 O LEU F 247 N SER F 233
SHEET 1 AX 2 CYS F 254 VAL F 257 0
SHEET 2 AX 2 VAL F 266 TRP F 269 -1 O GLY F 267 N ASP F 256
SHEET 1 AY 2 VAL F 391 SER F 393 0
SHEET 2 AY 2 LEU F 397 TRP F 399 -1 O TRP F 399 N VAL F 391
SHEET 1 AZ 2 THR F 419 CYS F 421 0
SHEET 2 AZ 2 CYS F 429 ASP F 431 -1 O THR F 430 N LYS F 420
SHEET 1 BA 6 ILE E 54 ASN E 56 0
SHEET 2 BA 6 GLN E 45 CYS E 49 -1 N ILE E 47 O ARG E 55
SHEET 3 BA 6 PRO E 7 SER E 15 -1 N ASP E 9 O ILE E 48
SHEET 4 BA 6 TYR E 143 VAL E 146 -1 O TYR E 145 N ARG E 14
SHEET 5 BA 6 GLU E 105 ASN E 113 -1 N THR E 109 O PHE E 144
SHEET 6 BA 6 TRP E 90 THR E 99 -1 N ARG E 91 O ILE E 112
SHEET 1 BB 4 CYS E 21 ILE E 24 0
SHEET 2 BB 4 GLY E 31 TYR E 36 -1 O ALA E 34 N ASP E 23
SHEET 3 BB 4 VAL E 73 PRO E 77 -1 O SER E 75 N GLY E 31
SHEET 4 BB 4 TYR E 61 PRO E 65 -1 N THR E 64 O MET E 74
SHEET 1 BC 2 CYS E 119 ILE E 122 0
SHEET 2 BC 2 ILE E 131 TYR E 134 -1 O TYR E 134 N CYS E 119
SHEET 1 BD 5 ILE E 199 ASN E 201 0
SHEET 2 BD 5 PHE E 191 TYR E 194 -1 N ARG E 192 O VAL E 200
SHEET 3 BD 5 GLU E 152 ASN E 160 -1 N LEU E 153 O TYR E 193
SHEET 4 BD 5 PHE E 279 VAL E 282 -1 O LYS E 280 N ARG E 159
SHEET 5 BD 5 TYR E 243 CYS E 244 -1 N CYS E 244 O PHE E 279
SHEET 1 BE 4 CYS E 166 VAL E 169 0
SHEET 2 BE 4 GLY E 176 TYR E 181 -1 O TYR E 181 N CYS E 166
SHEET 3 BE 4 VAL E 219 TYR E 222 -1 O ILE E 221 N GLY E 176
SHEET 4 BE 4 CYS E 207 VAL E 210 -1 N ASP E 209 O GLY E 220
SHEET 1 BF 2 TRP E 232 SER E 233 0
SHEET 2 BF 2 LEU E 247 ASN E 248 -1 O LEU E 247 N SER E 233
SHEET 1 BG 2 CYS E 254 VAL E 257 0
SHEET 2 BG 2 VAL E 266 TRP E 269 -1 O GLY E 267 N ASP E 256
SHEET 1 BH 2 VAL E 391 SER E 393 0
SHEET 2 BH 2 LEU E 397 TRP E 399 -1 O TRP E 399 N VAL E 391
SHEET 1 BI 2 THR E 419 CYS E 421 0
SHEET 2 BI 2 CYS E 429 ASP E 431 -1 O THR E 430 N LYS E 420
SHEET 1 BJ 4 ILE D 54 ASN D 56 0
SHEET 2 BJ 4 GLN D 45 CYS D 49 -1 N ILE D 47 O ARG D 55
SHEET 3 BJ 4 PRO D 7 SER D 15 -1 N ASP D 9 O ILE D 48
SHEET 4 BJ 4 PHE D 144 ARG D 147 -1 O TYR D 145 N ARG D 14
SHEET 1 BK 4 CYS D 21 ILE D 24 0
SHEET 2 BK 4 GLY D 31 TYR D 36 -1 O ALA D 34 N ASP D 23
SHEET 3 BK 4 VAL D 73 PRO D 77 -1 O SER D 75 N GLY D 31
SHEET 4 BK 4 TYR D 61 PRO D 65 -1 N THR D 64 O MET D 74
SHEET 1 BL 2 TRP D 90 THR D 99 0
SHEET 2 BL 2 GLU D 105 ASN D 113 -1 O ILE D 112 N ARG D 91
SHEET 1 BM 2 CYS D 119 ILE D 122 0
SHEET 2 BM 2 ILE D 131 TYR D 134 -1 O GLY D 132 N ASP D 121
SHEET 1 BN 5 ILE D 199 ASN D 201 0
SHEET 2 BN 5 PHE D 191 TYR D 194 -1 N ARG D 192 O VAL D 200
SHEET 3 BN 5 GLU D 152 ASN D 160 -1 N LEU D 153 O TYR D 193
SHEET 4 BN 5 PHE D 279 VAL D 282 -1 O LYS D 280 N ARG D 159
SHEET 5 BN 5 TYR D 243 CYS D 244 -1 N CYS D 244 O PHE D 279
SHEET 1 BO 4 CYS D 166 VAL D 169 0
SHEET 2 BO 4 GLY D 176 TYR D 181 -1 O LEU D 179 N ASP D 168
SHEET 3 BO 4 VAL D 219 TYR D 222 -1 O ILE D 221 N GLY D 176
SHEET 4 BO 4 CYS D 207 VAL D 210 -1 N ASP D 209 O GLY D 220
SHEET 1 BP 2 TRP D 232 SER D 233 0
SHEET 2 BP 2 LEU D 247 ASN D 248 -1 O LEU D 247 N SER D 233
SHEET 1 BQ 2 CYS D 254 VAL D 257 0
SHEET 2 BQ 2 VAL D 266 TRP D 269 -1 O GLY D 267 N ASP D 256
SHEET 1 BR 2 VAL D 391 SER D 393 0
SHEET 2 BR 2 LEU D 397 TRP D 399 -1 O TRP D 399 N VAL D 391
SHEET 1 BS 2 THR D 419 CYS D 421 0
SHEET 2 BS 2 CYS D 429 ASP D 431 -1 O THR D 430 N LYS D 420
SSBOND 1 CYS A 4 CYS A 49 1555 1555 2.05
SSBOND 2 CYS A 21 CYS A 38 1555 1555 2.04
SSBOND 3 CYS A 62 CYS A 78 1555 1555 2.04
SSBOND 4 CYS A 119 CYS A 136 1555 1555 2.10
SSBOND 5 CYS A 166 CYS A 183 1555 1555 2.08
SSBOND 6 CYS A 207 CYS A 224 1555 1555 2.04
SSBOND 7 CYS A 239 CYS A 244 1555 1555 2.06
SSBOND 8 CYS A 254 CYS A 271 1555 1555 2.05
SSBOND 9 CYS A 298 CYS A 380 1555 1555 2.05
SSBOND 10 CYS A 367 CYS A 406 1555 1555 2.04
SSBOND 11 CYS A 415 CYS A 429 1555 1555 2.07
SSBOND 12 CYS A 421 CYS A 426 1555 1555 2.03
SSBOND 13 CYS C 4 CYS C 49 1555 1555 2.05
SSBOND 14 CYS C 21 CYS C 38 1555 1555 2.04
SSBOND 15 CYS C 62 CYS C 78 1555 1555 2.06
SSBOND 16 CYS C 119 CYS C 136 1555 1555 2.04
SSBOND 17 CYS C 166 CYS C 183 1555 1555 2.08
SSBOND 18 CYS C 207 CYS C 224 1555 1555 2.06
SSBOND 19 CYS C 239 CYS C 244 1555 1555 2.06
SSBOND 20 CYS C 254 CYS C 271 1555 1555 2.06
SSBOND 21 CYS C 298 CYS C 380 1555 1555 2.06
SSBOND 22 CYS C 367 CYS C 406 1555 1555 2.06
SSBOND 23 CYS C 415 CYS C 429 1555 1555 2.06
SSBOND 24 CYS C 421 CYS C 426 1555 1555 2.05
SSBOND 25 CYS G 4 CYS G 49 1555 1555 2.07
SSBOND 26 CYS G 21 CYS G 38 1555 1555 2.03
SSBOND 27 CYS G 62 CYS G 78 1555 1555 2.04
SSBOND 28 CYS G 119 CYS G 136 1555 1555 2.03
SSBOND 29 CYS G 166 CYS G 183 1555 1555 2.08
SSBOND 30 CYS G 207 CYS G 224 1555 1555 2.05
SSBOND 31 CYS G 239 CYS G 244 1555 1555 2.07
SSBOND 32 CYS G 254 CYS G 271 1555 1555 2.05
SSBOND 33 CYS G 298 CYS G 380 1555 1555 2.03
SSBOND 34 CYS G 367 CYS G 406 1555 1555 2.05
SSBOND 35 CYS G 415 CYS G 429 1555 1555 2.08
SSBOND 36 CYS G 421 CYS G 426 1555 1555 2.05
SSBOND 37 CYS B 4 CYS B 49 1555 1555 2.04
SSBOND 38 CYS B 21 CYS B 38 1555 1555 2.04
SSBOND 39 CYS B 62 CYS B 78 1555 1555 2.05
SSBOND 40 CYS B 119 CYS B 136 1555 1555 2.02
SSBOND 41 CYS B 166 CYS B 183 1555 1555 2.07
SSBOND 42 CYS B 207 CYS B 224 1555 1555 2.04
SSBOND 43 CYS B 239 CYS B 244 1555 1555 2.06
SSBOND 44 CYS B 254 CYS B 271 1555 1555 2.06
SSBOND 45 CYS B 298 CYS B 380 1555 1555 2.05
SSBOND 46 CYS B 367 CYS B 406 1555 1555 2.05
SSBOND 47 CYS B 415 CYS B 429 1555 1555 2.08
SSBOND 48 CYS B 421 CYS B 426 1555 1555 2.04
SSBOND 49 CYS F 4 CYS F 49 1555 1555 2.05
SSBOND 50 CYS F 21 CYS F 38 1555 1555 2.03
SSBOND 51 CYS F 62 CYS F 78 1555 1555 2.04
SSBOND 52 CYS F 119 CYS F 136 1555 1555 2.08
SSBOND 53 CYS F 166 CYS F 183 1555 1555 2.07
SSBOND 54 CYS F 207 CYS F 224 1555 1555 2.03
SSBOND 55 CYS F 239 CYS F 244 1555 1555 2.05
SSBOND 56 CYS F 254 CYS F 271 1555 1555 2.05
SSBOND 57 CYS F 298 CYS F 380 1555 1555 2.03
SSBOND 58 CYS F 367 CYS F 406 1555 1555 2.01
SSBOND 59 CYS F 415 CYS F 429 1555 1555 2.08
SSBOND 60 CYS F 421 CYS F 426 1555 1555 2.03
SSBOND 61 CYS E 4 CYS E 49 1555 1555 2.04
SSBOND 62 CYS E 21 CYS E 38 1555 1555 2.05
SSBOND 63 CYS E 62 CYS E 78 1555 1555 2.04
SSBOND 64 CYS E 119 CYS E 136 1555 1555 2.05
SSBOND 65 CYS E 166 CYS E 183 1555 1555 2.07
SSBOND 66 CYS E 207 CYS E 224 1555 1555 2.04
SSBOND 67 CYS E 239 CYS E 244 1555 1555 2.05
SSBOND 68 CYS E 254 CYS E 271 1555 1555 2.06
SSBOND 69 CYS E 298 CYS E 380 1555 1555 2.04
SSBOND 70 CYS E 367 CYS E 406 1555 1555 2.03
SSBOND 71 CYS E 415 CYS E 429 1555 1555 2.08
SSBOND 72 CYS E 421 CYS E 426 1555 1555 2.03
SSBOND 73 CYS D 4 CYS D 49 1555 1555 2.05
SSBOND 74 CYS D 21 CYS D 38 1555 1555 2.04
SSBOND 75 CYS D 62 CYS D 78 1555 1555 2.05
SSBOND 76 CYS D 119 CYS D 136 1555 1555 2.05
SSBOND 77 CYS D 166 CYS D 183 1555 1555 2.07
SSBOND 78 CYS D 207 CYS D 224 1555 1555 2.05
SSBOND 79 CYS D 239 CYS D 244 1555 1555 2.06
SSBOND 80 CYS D 254 CYS D 271 1555 1555 2.04
SSBOND 81 CYS D 298 CYS D 380 1555 1555 2.04
SSBOND 82 CYS D 367 CYS D 406 1555 1555 2.05
SSBOND 83 CYS D 415 CYS D 429 1555 1555 2.07
SSBOND 84 CYS D 421 CYS D 426 1555 1555 2.04
LINK C PCA A 1 N VAL A 2 1555 1555 1.34
LINK C PCA C 1 N VAL C 2 1555 1555 1.34
LINK C PCA G 1 N VAL G 2 1555 1555 1.32
LINK C PCA B 1 N VAL B 2 1555 1555 1.34
LINK C PCA F 1 N VAL F 2 1555 1555 1.32
LINK C PCA E 1 N VAL E 2 1555 1555 1.34
LINK C PCA D 1 N VAL D 2 1555 1555 1.34
LINK O4 FRU H 1 C1 GAL H 2 1555 1555 1.43
LINK O4 FRU I 1 C1 GAL I 2 1555 1555 1.45
LINK O4 FRU J 1 C1 GAL J 2 1555 1555 1.43
LINK O4 FRU K 1 C1 GAL K 2 1555 1555 1.43
LINK O4 FRU L 1 C1 GAL L 2 1555 1555 1.43
LINK O4 FRU M 1 C1 GAL M 2 1555 1555 1.42
LINK O4 FRU N 1 C1 GAL N 2 1555 1555 1.42
LINK O4 FRU O 1 C1 GAL O 2 1555 1555 1.43
LINK O4 FRU P 1 C1 GAL P 2 1555 1555 1.44
LINK O4 FRU Q 1 C1 GAL Q 2 1555 1555 1.42
LINK O4 FRU R 1 C1 GAL R 2 1555 1555 1.42
LINK O4 FRU S 1 C1 GAL S 2 1555 1555 1.43
LINK O4 FRU T 1 C1 GAL T 2 1555 1555 1.43
LINK O4 FRU U 1 C1 GAL U 2 1555 1555 1.42
LINK O4 FRU V 1 C1 GAL V 2 1555 1555 1.44
LINK O4 FRU W 1 C1 GAL W 2 1555 1555 1.41
LINK O4 FRU X 1 C1 GAL X 2 1555 1555 1.43
LINK O4 FRU Y 1 C1 GAL Y 2 1555 1555 1.43
LINK O4 FRU Z 1 C1 GAL Z 2 1555 1555 1.43
LINK O4 FRU a 1 C1 GAL a 2 1555 1555 1.43
LINK O4 FRU b 1 C1 GAL b 2 1555 1555 1.44
LINK O4 FRU c 1 C1 GAL c 2 1555 1555 1.43
LINK O4 FRU d 1 C1 GAL d 2 1555 1555 1.43
LINK O4 FRU e 1 C1 GAL e 2 1555 1555 1.45
LINK O4 FRU f 1 C1 GAL f 2 1555 1555 1.44
LINK O4 FRU g 1 C1 GAL g 2 1555 1555 1.39
LINK O4 FRU h 1 C1 GAL h 2 1555 1555 1.42
LINK O4 FRU i 1 C1 GAL i 2 1555 1555 1.45
LINK O4 FRU j 1 C1 GAL j 2 1555 1555 1.43
LINK O4 FRU k 1 C1 GAL k 2 1555 1555 1.42
LINK O4 FRU l 1 C1 GAL l 2 1555 1555 1.44
LINK O4 FRU m 1 C1 GAL m 2 1555 1555 1.42
LINK O4 FRU n 1 C1 GAL n 2 1555 1555 1.43
LINK O4 FRU o 1 C1 GAL o 2 1555 1555 1.42
LINK O4 FRU p 1 C1 GAL p 2 1555 1555 1.44
LINK O4 FRU q 1 C1 GAL q 2 1555 1555 1.44
LINK O4 FRU r 1 C1 GAL r 2 1555 1555 1.43
LINK OD1 ASP A 23 CA CA A1005 1555 1555 2.28
LINK O ILE A 24 CA CA A1005 1555 1555 2.56
LINK O GLY A 26 CA CA A1005 1555 1555 2.44
LINK O ILE A 33 MG MG A1011 1555 1555 2.55
LINK OD2 ASP A 43 CA CA A1005 1555 1555 2.52
LINK OD1 ASN A 72 MG MG A1011 1555 1555 2.01
LINK O VAL A 73 MG MG A1011 1555 1555 2.89
LINK OD1 ASP A 121 CA CA A1006 1555 1555 2.54
LINK O ILE A 122 CA CA A1006 1555 1555 2.18
LINK O GLY A 124 CA CA A1006 1555 1555 1.94
LINK O ILE A 131 MG MG A1011 1555 1555 2.69
LINK OD2 ASP A 141 CA CA A1006 1555 1555 2.70
LINK OD1 ASP A 168 CA CA A1008 1555 1555 2.47
LINK O VAL A 169 CA CA A1008 1555 1555 2.56
LINK O GLY A 171 CA CA A1008 1555 1555 2.47
LINK OD1 ASN A 177 MG MG A1010 1555 1555 2.34
LINK O VAL A 178 MG MG A1010 1555 1555 2.59
LINK OD2 ASP A 188 CA CA A1008 1555 1555 2.55
LINK OD1 ASP A 209 CA CA A1009 1555 1555 2.38
LINK O VAL A 210 CA CA A1009 1555 1555 2.91
LINK O GLY A 212 CA CA A1009 1555 1555 2.77
LINK OD1 ASN A 218 MG MG A1010 1555 1555 2.67
LINK O VAL A 219 MG MG A1010 1555 1555 2.35
LINK OD2 ASP A 229 CA CA A1009 1555 1555 2.41
LINK OD1 ASP A 229 CA CA A1009 1555 1555 3.02
LINK OD1 ASP A 256 CA CA A1007 1555 1555 2.40
LINK O VAL A 257 CA CA A1007 1555 1555 2.76
LINK O GLY A 259 CA CA A1007 1555 1555 2.74
LINK OD1 ASP A 265 MG MG A1010 1555 1555 2.67
LINK O VAL A 266 MG MG A1010 1555 1555 2.63
LINK OD2 ASP A 276 CA CA A1007 1555 1555 2.49
LINK OD1 ASP A 373 CA CA A1013 1555 1555 2.81
LINK CA CA A1005 O3 GAL H 2 1555 1555 2.23
LINK CA CA A1005 O4 GAL H 2 1555 1555 2.99
LINK CA CA A1006 O3 GAL I 2 1555 1555 2.81
LINK CA CA A1007 O3 GAL L 2 1555 1555 2.71
LINK CA CA A1007 O4 GAL L 2 1555 1555 2.96
LINK CA CA A1008 O3 GAL J 2 1555 1555 2.23
LINK CA CA A1008 O4 GAL J 2 1555 1555 2.87
LINK CA CA A1009 O3 GAL K 2 1555 1555 2.44
LINK CA CA A1009 O4 GAL K 2 1555 1555 3.02
LINK OD1 ASP C 23 CA CA C1008 1555 1555 2.36
LINK O ILE C 24 CA CA C1008 1555 1555 2.77
LINK O GLY C 26 CA CA C1008 1555 1555 2.49
LINK O ILE C 33 MG MG C1012 1555 1555 2.43
LINK OD2 ASP C 43 CA CA C1008 1555 1555 2.50
LINK OD1 ASP C 43 CA CA C1008 1555 1555 3.20
LINK OD1 ASN C 72 MG MG C1012 1555 1555 2.13
LINK O VAL C 73 MG MG C1012 1555 1555 2.70
LINK OD1 ASP C 121 CA CA C1009 1555 1555 2.46
LINK O ILE C 122 CA CA C1009 1555 1555 2.53
LINK OE2 GLU C 123 CA CA C1014 1555 1555 2.32
LINK OE1 GLU C 123 CA CA C1014 1555 1555 2.45
LINK O GLY C 124 CA CA C1009 1555 1555 2.07
LINK O ILE C 131 MG MG C1012 1555 1555 2.53
LINK OD2 ASP C 141 CA CA C1009 1555 1555 2.87
LINK OD1 ASP C 141 CA CA C1009 1555 1555 3.12
LINK OD1 ASP C 168 CA CA C1007 1555 1555 2.42
LINK O VAL C 169 CA CA C1007 1555 1555 2.61
LINK O GLY C 171 CA CA C1007 1555 1555 2.55
LINK OD1 ASN C 177 MG MG C1011 1555 1555 2.49
LINK O VAL C 178 MG MG C1011 1555 1555 2.23
LINK OD2 ASP C 188 CA CA C1007 1555 1555 2.74
LINK OD1 ASP C 209 CA CA C1010 1555 1555 2.32
LINK O VAL C 210 CA CA C1010 1555 1555 2.57
LINK O GLY C 212 CA CA C1010 1555 1555 2.62
LINK OD1 ASN C 218 MG MG C1011 1555 1555 2.91
LINK O VAL C 219 MG MG C1011 1555 1555 2.66
LINK OD2 ASP C 229 CA CA C1010 1555 1555 2.49
LINK OD1 ASP C 256 CA CA C1006 1555 1555 2.45
LINK O VAL C 257 CA CA C1006 1555 1555 2.73
LINK O GLY C 259 CA CA C1006 1555 1555 2.64
LINK OD1 ASP C 265 MG MG C1011 1555 1555 2.33
LINK O VAL C 266 MG MG C1011 1555 1555 2.54
LINK OD2 ASP C 276 CA CA C1006 1555 1555 2.32
LINK OD1 ASP C 373 CA CA C1013 1555 1555 2.55
LINK CA CA C1006 O4 GAL Q 2 1555 1555 2.60
LINK CA CA C1006 O3 GAL Q 2 1555 1555 2.86
LINK CA CA C1007 O3 GAL O 2 1555 1555 2.38
LINK CA CA C1007 O4 GAL O 2 1555 1555 2.89
LINK CA CA C1008 O6 GAL M 2 1555 1555 2.57
LINK CA CA C1008 O4 GAL M 2 1555 1555 3.19
LINK CA CA C1009 O6 GAL N 2 1555 1555 2.37
LINK CA CA C1009 O4 GAL N 2 1555 1555 2.88
LINK CA CA C1010 O3 GAL P 2 1555 1555 2.68
LINK CA CA C1010 O4 GAL P 2 1555 1555 3.02
LINK OD1 ASP G 23 CA CA G 508 1555 1555 2.39
LINK O ILE G 24 CA CA G 508 1555 1555 2.71
LINK O GLY G 26 CA CA G 508 1555 1555 2.43
LINK O ILE G 33 MG MG G 512 1555 1555 2.42
LINK OD2 ASP G 43 CA CA G 508 1555 1555 2.46
LINK OD1 ASN G 72 MG MG G 512 1555 1555 2.24
LINK O VAL G 73 MG MG G 512 1555 1555 2.57
LINK OD1 ASP G 121 CA CA G 506 1555 1555 2.44
LINK O ILE G 122 CA CA G 506 1555 1555 2.55
LINK O GLY G 124 CA CA G 506 1555 1555 2.05
LINK O ILE G 131 MG MG G 512 1555 1555 2.08
LINK OD1 ASP G 168 CA CA G 509 1555 1555 2.52
LINK O VAL G 169 CA CA G 509 1555 1555 2.59
LINK O GLY G 171 CA CA G 509 1555 1555 2.47
LINK OD1 ASN G 177 MG MG G 511 1555 1555 2.48
LINK O VAL G 178 MG MG G 511 1555 1555 2.35
LINK OD2 ASP G 188 CA CA G 509 1555 1555 2.67
LINK OD1 ASP G 209 CA CA G 510 1555 1555 2.50
LINK O VAL G 210 CA CA G 510 1555 1555 2.47
LINK O GLY G 212 CA CA G 510 1555 1555 2.38
LINK OD1 ASN G 218 MG MG G 511 1555 1555 2.67
LINK O VAL G 219 MG MG G 511 1555 1555 2.89
LINK OD2 ASP G 229 CA CA G 510 1555 1555 2.47
LINK OD1 ASP G 256 CA CA G 507 1555 1555 2.54
LINK O VAL G 257 CA CA G 507 1555 1555 2.61
LINK O GLY G 259 CA CA G 507 1555 1555 2.50
LINK OD1 ASP G 265 MG MG G 511 1555 1555 2.13
LINK O VAL G 266 MG MG G 511 1555 1555 2.57
LINK OD2 ASP G 276 CA CA G 507 1555 1555 2.39
LINK OD1 ASP G 373 CA CA G 513 1555 1555 2.59
LINK CA CA G 506 O3 GAL V 2 1555 1555 2.78
LINK CA CA G 506 O4 GAL V 2 1555 1555 2.95
LINK CA CA G 507 O4 GAL R 2 1555 1555 2.51
LINK CA CA G 507 O3 GAL R 2 1555 1555 2.52
LINK CA CA G 508 O3 GAL U 2 1555 1555 2.55
LINK CA CA G 508 O4 GAL U 2 1555 1555 2.93
LINK CA CA G 509 O3 GAL S 2 1555 1555 2.54
LINK CA CA G 509 O4 GAL S 2 1555 1555 2.67
LINK CA CA G 510 O3 GAL T 2 1555 1555 2.42
LINK CA CA G 510 O4 GAL T 2 1555 1555 2.88
LINK OD1 ASP B 23 CA CA B 508 1555 1555 2.32
LINK O ILE B 24 CA CA B 508 1555 1555 2.58
LINK O GLY B 26 CA CA B 508 1555 1555 2.45
LINK O ILE B 33 MG MG B 511 1555 1555 2.42
LINK OD2 ASP B 43 CA CA B 508 1555 1555 2.26
LINK OD1 ASP B 43 CA CA B 508 1555 1555 3.10
LINK OD1 ASN B 72 MG MG B 511 1555 1555 2.26
LINK O VAL B 73 MG MG B 511 1555 1555 2.32
LINK OD1 ASP B 121 CA CA B 509 1555 1555 2.32
LINK O ILE B 122 CA CA B 509 1555 1555 2.74
LINK O GLY B 124 CA CA B 509 1555 1555 2.23
LINK O ILE B 131 MG MG B 511 1555 1555 2.26
LINK OD1 ASP B 141 CA CA B 509 1555 1555 3.03
LINK OD1 ASP B 168 CA CA B 505 1555 1555 2.33
LINK O VAL B 169 CA CA B 505 1555 1555 2.55
LINK O GLY B 171 CA CA B 505 1555 1555 2.67
LINK OD1 ASN B 177 MG MG B 512 1555 1555 2.50
LINK O VAL B 178 MG MG B 512 1555 1555 2.62
LINK OD2 ASP B 188 CA CA B 505 1555 1555 2.61
LINK OD1 ASP B 209 CA CA B 510 1555 1555 2.46
LINK O VAL B 210 CA CA B 510 1555 1555 3.08
LINK O GLY B 212 CA CA B 510 1555 1555 2.75
LINK OD1 ASN B 218 MG MG B 512 1555 1555 2.70
LINK O VAL B 219 MG MG B 512 1555 1555 2.22
LINK OD2 ASP B 229 CA CA B 510 1555 1555 2.67
LINK OD1 ASP B 256 CA CA B 506 1555 1555 2.63
LINK O VAL B 257 CA CA B 506 1555 1555 2.51
LINK O GLY B 259 CA CA B 506 1555 1555 2.34
LINK OD1 ASP B 265 MG MG B 512 1555 1555 2.84
LINK O VAL B 266 MG MG B 512 1555 1555 2.52
LINK OD2 ASP B 276 CA CA B 506 1555 1555 2.52
LINK OD1 ASP B 373 CA CA B 514 1555 1555 2.67
LINK CA CA B 505 O3 GAL X 2 1555 1555 2.51
LINK CA CA B 505 O4 GAL X 2 1555 1555 2.88
LINK CA CA B 506 O4 GAL W 2 1555 1555 2.61
LINK CA CA B 506 O3 GAL W 2 1555 1555 2.93
LINK CA CA B 508 O3 GAL Y 2 1555 1555 2.94
LINK CA CA B 509 O3 GAL Z 2 1555 1555 2.19
LINK CA CA B 510 O3 GAL a 2 1555 1555 2.23
LINK CA CA B 510 O4 GAL a 2 1555 1555 3.06
LINK OD1 ASP F 23 CA CA F 506 1555 1555 2.47
LINK O ILE F 24 CA CA F 506 1555 1555 2.80
LINK O GLY F 26 CA CA F 506 1555 1555 2.35
LINK OD1 ASN F 32 MG MG F 510 1555 1555 2.89
LINK O ILE F 33 MG MG F 510 1555 1555 2.28
LINK OD2 ASP F 43 CA CA F 506 1555 1555 2.51
LINK OD1 ASN F 72 MG MG F 510 1555 1555 2.39
LINK O VAL F 73 MG MG F 510 1555 1555 2.73
LINK O GLY F 124 CA CA F 511 1555 1555 3.11
LINK O ILE F 131 MG MG F 510 1555 1555 2.99
LINK OD1 ASP F 141 CA CA F 511 1555 1555 2.99
LINK OD1 ASP F 168 CA CA F 508 1555 1555 2.50
LINK O VAL F 169 CA CA F 508 1555 1555 2.57
LINK O GLY F 171 CA CA F 508 1555 1555 2.44
LINK OD1 ASN F 177 MG MG F 509 1555 1555 2.24
LINK O VAL F 178 MG MG F 509 1555 1555 2.41
LINK OD2 ASP F 188 CA CA F 508 1555 1555 2.35
LINK OD1 ASP F 188 CA CA F 508 1555 1555 3.15
LINK OD1 ASP F 209 CA CA F 507 1555 1555 2.48
LINK O VAL F 210 CA CA F 507 1555 1555 2.53
LINK O GLY F 212 CA CA F 507 1555 1555 2.35
LINK OD1 ASN F 218 MG MG F 509 1555 1555 2.87
LINK O VAL F 219 MG MG F 509 1555 1555 2.46
LINK OD2 ASP F 229 CA CA F 507 1555 1555 2.49
LINK OD1 ASP F 256 CA CA F 505 1555 1555 2.34
LINK O VAL F 257 CA CA F 505 1555 1555 2.18
LINK O GLY F 259 CA CA F 505 1555 1555 2.47
LINK OD1 ASP F 265 MG MG F 509 1555 1555 2.58
LINK O VAL F 266 MG MG F 509 1555 1555 2.75
LINK OD2 ASP F 276 CA CA F 505 1555 1555 2.60
LINK OD1 ASP F 373 CA CA F 513 1555 1555 2.68
LINK CA CA F 505 O3 GAL c 2 1555 1555 2.66
LINK CA CA F 505 O4 GAL c 2 1555 1555 2.75
LINK CA CA F 506 O3 GAL f 2 1555 1555 2.60
LINK CA CA F 507 O4 GAL d 2 1555 1555 2.53
LINK CA CA F 507 O3 GAL d 2 1555 1555 2.76
LINK CA CA F 508 O3 GAL e 2 1555 1555 2.82
LINK CA CA F 508 O4 GAL e 2 1555 1555 2.99
LINK OD1 ASP E 23 CA CA E 510 1555 1555 2.27
LINK O ILE E 24 CA CA E 510 1555 1555 2.59
LINK O GLY E 26 CA CA E 510 1555 1555 2.48
LINK O ILE E 33 MG MG E 513 1555 1555 2.17
LINK OD2 ASP E 43 CA CA E 510 1555 1555 2.52
LINK OD1 ASN E 72 MG MG E 513 1555 1555 2.34
LINK O VAL E 73 MG MG E 513 1555 1555 2.93
LINK OD1 ASP E 121 CA CA E 511 1555 1555 2.54
LINK O ILE E 122 CA CA E 511 1555 1555 2.88
LINK O GLY E 124 CA CA E 511 1555 1555 2.08
LINK O ILE E 131 MG MG E 513 1555 1555 2.40
LINK OD2 ASP E 141 CA CA E 511 1555 1555 3.09
LINK OD1 ASP E 168 CA CA E 507 1555 1555 2.44
LINK O VAL E 169 CA CA E 507 1555 1555 2.62
LINK O GLY E 171 CA CA E 507 1555 1555 2.55
LINK OD1 ASN E 177 MG MG E 512 1555 1555 2.38
LINK O VAL E 178 MG MG E 512 1555 1555 2.54
LINK OD2 ASP E 188 CA CA E 507 1555 1555 2.50
LINK OD1 ASP E 209 CA CA E 509 1555 1555 2.54
LINK O VAL E 210 CA CA E 509 1555 1555 2.62
LINK OE1 GLU E 211 CA CA E 515 1555 1555 2.16
LINK OE2 GLU E 211 CA CA E 515 1555 1555 2.24
LINK O GLY E 212 CA CA E 509 1555 1555 2.39
LINK OD1 ASN E 218 MG MG E 512 1555 1555 2.63
LINK O VAL E 219 MG MG E 512 1555 1555 2.57
LINK OD2 ASP E 229 CA CA E 509 1555 1555 2.52
LINK OD1 ASP E 256 CA CA E 508 1555 1555 2.42
LINK O VAL E 257 CA CA E 508 1555 1555 2.67
LINK O GLY E 259 CA CA E 508 1555 1555 2.64
LINK OD1 ASP E 265 MG MG E 512 1555 1555 2.49
LINK O VAL E 266 MG MG E 512 1555 1555 2.58
LINK OD2 ASP E 276 CA CA E 508 1555 1555 2.29
LINK OD1 ASP E 373 CA CA E 514 1555 1555 2.64
LINK CA CA E 507 O3 GAL i 2 1555 1555 2.57
LINK CA CA E 507 O4 GAL i 2 1555 1555 2.85
LINK CA CA E 508 O4 GAL h 2 1555 1555 2.69
LINK CA CA E 508 O3 GAL h 2 1555 1555 2.83
LINK CA CA E 509 O3 GAL j 2 1555 1555 2.55
LINK CA CA E 509 O4 GAL j 2 1555 1555 2.56
LINK CA CA E 510 O4 GAL k 2 1555 1555 2.67
LINK CA CA E 510 O3 GAL k 2 1555 1555 2.92
LINK CA CA E 511 O3 GAL l 2 1555 1555 2.97
LINK CA CA E 511 O4 GAL l 2 1555 1555 3.03
LINK OD1 ASP D 23 CA CA D 508 1555 1555 2.30
LINK O ILE D 24 CA CA D 508 1555 1555 2.45
LINK O GLY D 26 CA CA D 508 1555 1555 2.40
LINK O ILE D 33 MG MG D 511 1555 1555 2.56
LINK OD2 ASP D 43 CA CA D 508 1555 1555 2.48
LINK OD1 ASN D 72 MG MG D 511 1555 1555 1.97
LINK O VAL D 73 MG MG D 511 1555 1555 2.92
LINK OD1 ASP D 121 CA CA D 509 1555 1555 2.35
LINK O ILE D 122 CA CA D 509 1555 1555 2.73
LINK O GLY D 124 CA CA D 509 1555 1555 2.20
LINK O ILE D 131 MG MG D 511 1555 1555 2.41
LINK OD2 ASP D 141 CA CA D 509 1555 1555 2.96
LINK OD1 ASP D 141 CA CA D 509 1555 1555 3.06
LINK OD1 ASP D 168 CA CA D 505 1555 1555 2.47
LINK O VAL D 169 CA CA D 505 1555 1555 2.49
LINK O GLY D 171 CA CA D 505 1555 1555 2.46
LINK OD1 ASN D 177 MG MG D 510 1555 1555 2.44
LINK O VAL D 178 MG MG D 510 1555 1555 2.42
LINK OD2 ASP D 188 CA CA D 505 1555 1555 2.79
LINK OD1 ASP D 209 CA CA D 504 1555 1555 2.51
LINK O VAL D 210 CA CA D 504 1555 1555 2.30
LINK O GLY D 212 CA CA D 504 1555 1555 2.36
LINK OD1 ASN D 218 MG MG D 510 1555 1555 2.85
LINK O VAL D 219 MG MG D 510 1555 1555 2.35
LINK OD2 ASP D 229 CA CA D 504 1555 1555 2.35
LINK OD1 ASP D 256 CA CA D 503 1555 1555 2.50
LINK O VAL D 257 CA CA D 503 1555 1555 2.38
LINK O GLY D 259 CA CA D 503 1555 1555 2.34
LINK OD1 ASP D 265 MG MG D 510 1555 1555 2.64
LINK O VAL D 266 MG MG D 510 1555 1555 2.52
LINK OD2 ASP D 276 CA CA D 503 1555 1555 2.44
LINK OD1 ASP D 373 CA CA D 513 1555 1555 2.49
LINK CA CA D 503 O4 GAL n 2 1555 1555 2.53
LINK CA CA D 503 O3 GAL n 2 1555 1555 2.69
LINK CA CA D 504 O4 GAL q 2 1555 1555 2.64
LINK CA CA D 504 O3 GAL q 2 1555 1555 2.74
LINK CA CA D 505 O3 GAL r 2 1555 1555 2.43
LINK CA CA D 505 O4 GAL r 2 1555 1555 2.95
LINK CA CA D 508 O3 GAL o 2 1555 1555 2.36
LINK CA CA D 508 O4 GAL o 2 1555 1555 2.80
LINK CA CA D 509 O4 GAL p 2 1555 1555 2.71
LINK CA CA D 509 O3 GAL p 2 1555 1555 3.18
CISPEP 1 TYR A 81 PRO A 82 0 5.37
CISPEP 2 GLY A 127 THR A 128 0 18.63
CISPEP 3 TYR C 81 PRO C 82 0 3.81
CISPEP 4 TYR G 81 PRO G 82 0 4.88
CISPEP 5 TYR B 81 PRO B 82 0 5.15
CISPEP 6 ARG B 378 GLY B 379 0 -1.98
CISPEP 7 TYR F 81 PRO F 82 0 4.96
CISPEP 8 TYR E 81 PRO E 82 0 4.04
CISPEP 9 TYR D 81 PRO D 82 0 2.90
CRYST1 219.800 228.650 133.020 90.00 127.13 90.00 C 1 2 1 28
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 0.004550 0.000000 0.003445 0.00000
SCALE2 0.000000 0.004373 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009429 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.715623 -0.681754 0.151970 71.19553 1
MTRIX2 2 0.682308 0.635745 -0.360949 -54.07935 1
MTRIX3 2 0.149465 0.361994 0.920120 -40.51479 1
MTRIX1 3 0.678702 0.722479 0.131865 -8.93051 1
MTRIX2 3 -0.720887 0.621072 0.307557 101.91695 1
MTRIX3 3 0.140306 -0.303799 0.942348 3.64025 1
MTRIX1 4 0.006637 0.874369 0.485217 55.22257 1
MTRIX2 4 -0.889714 -0.216333 0.402006 172.51936 1
MTRIX3 4 0.456470 -0.434372 0.776502 -25.34215 1
MTRIX1 5 -0.562523 0.386421 0.730922 148.05255 1
MTRIX2 5 -0.408928 -0.898388 0.160243 160.72713 1
MTRIX3 5 0.718572 -0.208754 0.663382 -66.96054 1
MTRIX1 6 -0.543318 -0.395233 0.740673 192.59212 1
MTRIX2 6 0.382098 -0.901991 -0.201028 74.26899 1
MTRIX3 6 0.747534 0.173787 0.641086 -94.74038 1
MTRIX1 7 -0.010275 -0.875096 0.483841 165.11728 1
MTRIX2 7 0.874593 -0.242431 -0.419897 -19.32623 1
MTRIX3 7 0.484748 0.418849 0.767844 -79.91350 1
HETATM 1 N PCA A 1 112.182 119.670 -6.433 1.00 83.84 N
ANISOU 1 N PCA A 1 9282 10407 12168 1746 -1171 -1849 N
HETATM 2 CA PCA A 1 110.788 120.015 -6.210 1.00 89.98 C
ANISOU 2 CA PCA A 1 10139 11223 12826 1748 -1134 -1781 C
HETATM 3 CB PCA A 1 110.601 119.741 -4.721 1.00 93.65 C
ANISOU 3 CB PCA A 1 10690 11719 13175 1860 -1246 -1862 C
HETATM 4 CG PCA A 1 111.507 118.519 -4.537 1.00 92.17 C
ANISOU 4 CG PCA A 1 10521 11549 12952 1900 -1292 -1901 C
HETATM 5 CD PCA A 1 112.219 118.475 -5.867 1.00 86.69 C
ANISOU 5 CD PCA A 1 9730 10820 12390 1806 -1213 -1857 C
HETATM 6 OE PCA A 1 112.628 117.442 -6.359 1.00 85.63 O
ANISOU 6 OE PCA A 1 9609 10708 12220 1789 -1182 -1822 O
HETATM 7 C PCA A 1 110.240 121.290 -6.783 1.00 87.63 C
ANISOU 7 C PCA A 1 9787 10888 12620 1687 -1071 -1739 C
HETATM 8 O PCA A 1 110.202 122.329 -6.114 1.00 93.65 O
ANISOU 8 O PCA A 1 10521 11613 13449 1721 -1130 -1811 O
(ATOM LINES ARE NOT SHOWN.)
END
