HEADER HYDROLASE 29-JAN-13 3W5G
TITLE CRYSTAL STRUCTURE OF TOMATO BETA-GALACTOSIDASE 4 IN COMPLEX WITH
TITLE 2 GALACTOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.2.1.23;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM LYCOPERSICUM;
SOURCE 3 ORGANISM_COMMON: TOMATO;
SOURCE 4 ORGANISM_TAXID: 4081;
SOURCE 5 GENE: TBG4;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SMD1168H;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZ ALPHA A
KEYWDS TIM BARREL, BETA-SANDWICH, HYDROLASE, GLYCOSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.EDA,T.TADA
REVDAT 3 08-NOV-23 3W5G 1 HETSYN
REVDAT 2 29-JUL-20 3W5G 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE ATOM
REVDAT 1 29-JAN-14 3W5G 0
JRNL AUTH M.EDA,T.TADA
JRNL TITL CRYSTAL STRUCTURE OF TOMATO BETA-GALACTOSIDASE 4 IN COMPLEX
JRNL TITL 2 WITH GALACTOSE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 31068
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1653
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2119
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11062
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 166
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.482
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11569 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15740 ; 0.975 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1408 ; 4.915 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 508 ;38.131 ;24.055
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1806 ;15.502 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;17.495 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1657 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8889 ; 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 : NULL
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: NULL
REMARK 4
REMARK 4 3W5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000095909.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 LIQUID NITROGEN COOLING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32837
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3W5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 20% (W/V) PEG 10000, 0.1M
REMARK 280 D-GALACTOSE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 46.96500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.18950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.19100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.18950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.96500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.19100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 18
REMARK 465 ALA A 19
REMARK 465 GLU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 727
REMARK 465 ALA A 728
REMARK 465 ALA A 729
REMARK 465 SER A 730
REMARK 465 PHE A 731
REMARK 465 LEU A 732
REMARK 465 GLU A 733
REMARK 465 GLN A 734
REMARK 465 LYS A 735
REMARK 465 GLU B 18
REMARK 465 ALA B 19
REMARK 465 GLU B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 727
REMARK 465 ALA B 728
REMARK 465 ALA B 729
REMARK 465 SER B 730
REMARK 465 PHE B 731
REMARK 465 LEU B 732
REMARK 465 GLU B 733
REMARK 465 GLN B 734
REMARK 465 LYS B 735
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 ARG A 30 -61.55 -91.99
REMARK 500 PHE A 89 30.50 -141.16
REMARK 500 CYS A 118 -93.66 59.58
REMARK 500 ALA A 119 17.63 56.69
REMARK 500 ASN A 122 125.13 -37.59
REMARK 500 ASN A 141 75.57 -69.81
REMARK 500 GLU A 179 172.38 64.47
REMARK 500 CYS A 234 40.51 -150.52
REMARK 500 ASN A 281 56.93 -111.40
REMARK 500 ASN A 282 -4.36 74.52
REMARK 500 ASN A 389 -7.56 70.49
REMARK 500 CYS A 405 -7.98 70.50
REMARK 500 ASN A 452 42.75 -87.95
REMARK 500 VAL A 543 78.76 -102.08
REMARK 500 VAL A 602 73.33 -68.18
REMARK 500 MET A 610 -160.94 -163.66
REMARK 500 LEU A 616 71.24 52.64
REMARK 500 ASN A 681 44.01 71.54
REMARK 500 ARG B 30 -60.98 -93.88
REMARK 500 GLN B 54 31.28 -91.34
REMARK 500 CYS B 118 -91.93 61.05
REMARK 500 ALA B 119 19.08 56.04
REMARK 500 ASN B 122 119.56 -33.01
REMARK 500 GLU B 179 178.44 61.81
REMARK 500 CYS B 234 6.71 -152.86
REMARK 500 ASN B 281 57.89 -106.28
REMARK 500 GLN B 578 -175.54 -67.03
REMARK 500 MET B 610 116.77 -39.49
REMARK 500 LEU B 616 71.51 51.46
REMARK 500 TRP B 655 55.57 -151.82
REMARK 500 CYS B 678 70.59 -107.96
REMARK 500 ASN B 681 39.17 70.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W5F RELATED DB: PDB
DBREF 3W5G A 24 724 UNP O81100 O81100_SOLLC 24 724
DBREF 3W5G B 24 724 UNP O81100 O81100_SOLLC 24 724
SEQADV 3W5G GLU A 18 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA A 19 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU A 20 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA A 21 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU A 22 UNP O81100 EXPRESSION TAG
SEQADV 3W5G PHE A 23 UNP O81100 EXPRESSION TAG
SEQADV 3W5G SER A 725 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA A 726 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA A 727 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA A 728 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA A 729 UNP O81100 EXPRESSION TAG
SEQADV 3W5G SER A 730 UNP O81100 EXPRESSION TAG
SEQADV 3W5G PHE A 731 UNP O81100 EXPRESSION TAG
SEQADV 3W5G LEU A 732 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU A 733 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLN A 734 UNP O81100 EXPRESSION TAG
SEQADV 3W5G LYS A 735 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU B 18 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA B 19 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU B 20 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA B 21 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU B 22 UNP O81100 EXPRESSION TAG
SEQADV 3W5G PHE B 23 UNP O81100 EXPRESSION TAG
SEQADV 3W5G SER B 725 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA B 726 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA B 727 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA B 728 UNP O81100 EXPRESSION TAG
SEQADV 3W5G ALA B 729 UNP O81100 EXPRESSION TAG
SEQADV 3W5G SER B 730 UNP O81100 EXPRESSION TAG
SEQADV 3W5G PHE B 731 UNP O81100 EXPRESSION TAG
SEQADV 3W5G LEU B 732 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLU B 733 UNP O81100 EXPRESSION TAG
SEQADV 3W5G GLN B 734 UNP O81100 EXPRESSION TAG
SEQADV 3W5G LYS B 735 UNP O81100 EXPRESSION TAG
SEQRES 1 A 718 GLU ALA GLU ALA GLU PHE SER VAL SER TYR ASP ASP ARG
SEQRES 2 A 718 ALA ILE ILE ILE ASN GLY LYS ARG LYS ILE LEU ILE SER
SEQRES 3 A 718 GLY SER ILE HIS TYR PRO ARG SER THR PRO GLN MET TRP
SEQRES 4 A 718 PRO ASP LEU ILE GLN LYS ALA LYS ASP GLY GLY LEU ASP
SEQRES 5 A 718 VAL ILE GLU THR TYR VAL PHE TRP ASN GLY HIS GLU PRO
SEQRES 6 A 718 SER PRO GLY LYS TYR ASN PHE GLU GLY ARG TYR ASP LEU
SEQRES 7 A 718 VAL ARG PHE ILE LYS MET VAL GLN ARG ALA GLY LEU TYR
SEQRES 8 A 718 VAL ASN LEU ARG ILE GLY PRO TYR VAL CYS ALA GLU TRP
SEQRES 9 A 718 ASN PHE GLY GLY PHE PRO VAL TRP LEU LYS TYR VAL PRO
SEQRES 10 A 718 GLY MET GLU PHE ARG THR ASN ASN GLN PRO PHE LYS VAL
SEQRES 11 A 718 ALA MET GLN GLY PHE VAL GLN LYS ILE VAL ASN MET MET
SEQRES 12 A 718 LYS SER GLU ASN LEU PHE GLU SER GLN GLY GLY PRO ILE
SEQRES 13 A 718 ILE MET ALA GLN ILE GLU ASN GLU TYR GLY PRO VAL GLU
SEQRES 14 A 718 TRP GLU ILE GLY ALA PRO GLY LYS ALA TYR THR LYS TRP
SEQRES 15 A 718 ALA ALA GLN MET ALA VAL GLY LEU LYS THR GLY VAL PRO
SEQRES 16 A 718 TRP ILE MET CYS LYS GLN GLU ASP ALA PRO ASP PRO VAL
SEQRES 17 A 718 ILE ASP THR CYS ASN GLY PHE TYR CYS GLU GLY PHE ARG
SEQRES 18 A 718 PRO ASN LYS PRO TYR LYS PRO LYS MET TRP THR GLU VAL
SEQRES 19 A 718 TRP THR GLY TRP TYR THR LYS PHE GLY GLY PRO ILE PRO
SEQRES 20 A 718 GLN ARG PRO ALA GLU ASP ILE ALA PHE SER VAL ALA ARG
SEQRES 21 A 718 PHE VAL GLN ASN ASN GLY SER PHE PHE ASN TYR TYR MET
SEQRES 22 A 718 TYR HIS GLY GLY THR ASN PHE GLY ARG THR SER SER GLY
SEQRES 23 A 718 LEU PHE ILE ALA THR SER TYR ASP TYR ASP ALA PRO LEU
SEQRES 24 A 718 ASP GLU TYR GLY LEU LEU ASN GLU PRO LYS TYR GLY HIS
SEQRES 25 A 718 LEU ARG ASP LEU HIS LYS ALA ILE LYS LEU SER GLU PRO
SEQRES 26 A 718 ALA LEU VAL SER SER TYR ALA ALA VAL THR SER LEU GLY
SEQRES 27 A 718 SER ASN GLN GLU ALA HIS VAL TYR ARG SER LYS SER GLY
SEQRES 28 A 718 ALA CYS ALA ALA PHE LEU SER ASN TYR ASP SER ARG TYR
SEQRES 29 A 718 SER VAL LYS VAL THR PHE GLN ASN ARG PRO TYR ASN LEU
SEQRES 30 A 718 PRO PRO TRP SER ILE SER ILE LEU PRO ASP CYS LYS THR
SEQRES 31 A 718 ALA VAL TYR ASN THR ALA GLN VAL ASN SER GLN SER SER
SEQRES 32 A 718 SER ILE LYS MET THR PRO ALA GLY GLY GLY LEU SER TRP
SEQRES 33 A 718 GLN SER TYR ASN GLU GLU THR PRO THR ALA ASP ASP SER
SEQRES 34 A 718 ASP THR LEU THR ALA ASN GLY LEU TRP GLU GLN LYS ASN
SEQRES 35 A 718 VAL THR ARG ASP SER SER ASP TYR LEU TRP TYR MET THR
SEQRES 36 A 718 ASN VAL ASN ILE ALA SER ASN GLU GLY PHE LEU LYS ASN
SEQRES 37 A 718 GLY LYS ASP PRO TYR LEU THR VAL MET SER ALA GLY HIS
SEQRES 38 A 718 VAL LEU HIS VAL PHE VAL ASN GLY LYS LEU SER GLY THR
SEQRES 39 A 718 VAL TYR GLY THR LEU ASP ASN PRO LYS LEU THR TYR SER
SEQRES 40 A 718 GLY ASN VAL LYS LEU ARG ALA GLY ILE ASN LYS ILE SER
SEQRES 41 A 718 LEU LEU SER VAL SER VAL GLY LEU PRO ASN VAL GLY VAL
SEQRES 42 A 718 HIS TYR ASP THR TRP ASN ALA GLY VAL LEU GLY PRO VAL
SEQRES 43 A 718 THR LEU SER GLY LEU ASN GLU GLY SER ARG ASN LEU ALA
SEQRES 44 A 718 LYS GLN LYS TRP SER TYR LYS VAL GLY LEU LYS GLY GLU
SEQRES 45 A 718 SER LEU SER LEU HIS SER LEU SER GLY SER SER SER VAL
SEQRES 46 A 718 GLU TRP VAL ARG GLY SER LEU MET ALA GLN LYS GLN PRO
SEQRES 47 A 718 LEU THR TRP TYR LYS ALA THR PHE ASN ALA PRO GLY GLY
SEQRES 48 A 718 ASN ASP PRO LEU ALA LEU ASP MET ALA SER MET GLY LYS
SEQRES 49 A 718 GLY GLN ILE TRP ILE ASN GLY GLU GLY VAL GLY ARG HIS
SEQRES 50 A 718 TRP PRO GLY TYR ILE ALA GLN GLY ASP CYS SER LYS CYS
SEQRES 51 A 718 SER TYR ALA GLY THR PHE ASN GLU LYS LYS CYS GLN THR
SEQRES 52 A 718 ASN CYS GLY GLN PRO SER GLN ARG TRP TYR HIS VAL PRO
SEQRES 53 A 718 ARG SER TRP LEU LYS PRO SER GLY ASN LEU LEU VAL VAL
SEQRES 54 A 718 PHE GLU GLU TRP GLY GLY ASN PRO THR GLY ILE SER LEU
SEQRES 55 A 718 VAL ARG ARG SER ARG SER ALA ALA ALA ALA SER PHE LEU
SEQRES 56 A 718 GLU GLN LYS
SEQRES 1 B 718 GLU ALA GLU ALA GLU PHE SER VAL SER TYR ASP ASP ARG
SEQRES 2 B 718 ALA ILE ILE ILE ASN GLY LYS ARG LYS ILE LEU ILE SER
SEQRES 3 B 718 GLY SER ILE HIS TYR PRO ARG SER THR PRO GLN MET TRP
SEQRES 4 B 718 PRO ASP LEU ILE GLN LYS ALA LYS ASP GLY GLY LEU ASP
SEQRES 5 B 718 VAL ILE GLU THR TYR VAL PHE TRP ASN GLY HIS GLU PRO
SEQRES 6 B 718 SER PRO GLY LYS TYR ASN PHE GLU GLY ARG TYR ASP LEU
SEQRES 7 B 718 VAL ARG PHE ILE LYS MET VAL GLN ARG ALA GLY LEU TYR
SEQRES 8 B 718 VAL ASN LEU ARG ILE GLY PRO TYR VAL CYS ALA GLU TRP
SEQRES 9 B 718 ASN PHE GLY GLY PHE PRO VAL TRP LEU LYS TYR VAL PRO
SEQRES 10 B 718 GLY MET GLU PHE ARG THR ASN ASN GLN PRO PHE LYS VAL
SEQRES 11 B 718 ALA MET GLN GLY PHE VAL GLN LYS ILE VAL ASN MET MET
SEQRES 12 B 718 LYS SER GLU ASN LEU PHE GLU SER GLN GLY GLY PRO ILE
SEQRES 13 B 718 ILE MET ALA GLN ILE GLU ASN GLU TYR GLY PRO VAL GLU
SEQRES 14 B 718 TRP GLU ILE GLY ALA PRO GLY LYS ALA TYR THR LYS TRP
SEQRES 15 B 718 ALA ALA GLN MET ALA VAL GLY LEU LYS THR GLY VAL PRO
SEQRES 16 B 718 TRP ILE MET CYS LYS GLN GLU ASP ALA PRO ASP PRO VAL
SEQRES 17 B 718 ILE ASP THR CYS ASN GLY PHE TYR CYS GLU GLY PHE ARG
SEQRES 18 B 718 PRO ASN LYS PRO TYR LYS PRO LYS MET TRP THR GLU VAL
SEQRES 19 B 718 TRP THR GLY TRP TYR THR LYS PHE GLY GLY PRO ILE PRO
SEQRES 20 B 718 GLN ARG PRO ALA GLU ASP ILE ALA PHE SER VAL ALA ARG
SEQRES 21 B 718 PHE VAL GLN ASN ASN GLY SER PHE PHE ASN TYR TYR MET
SEQRES 22 B 718 TYR HIS GLY GLY THR ASN PHE GLY ARG THR SER SER GLY
SEQRES 23 B 718 LEU PHE ILE ALA THR SER TYR ASP TYR ASP ALA PRO LEU
SEQRES 24 B 718 ASP GLU TYR GLY LEU LEU ASN GLU PRO LYS TYR GLY HIS
SEQRES 25 B 718 LEU ARG ASP LEU HIS LYS ALA ILE LYS LEU SER GLU PRO
SEQRES 26 B 718 ALA LEU VAL SER SER TYR ALA ALA VAL THR SER LEU GLY
SEQRES 27 B 718 SER ASN GLN GLU ALA HIS VAL TYR ARG SER LYS SER GLY
SEQRES 28 B 718 ALA CYS ALA ALA PHE LEU SER ASN TYR ASP SER ARG TYR
SEQRES 29 B 718 SER VAL LYS VAL THR PHE GLN ASN ARG PRO TYR ASN LEU
SEQRES 30 B 718 PRO PRO TRP SER ILE SER ILE LEU PRO ASP CYS LYS THR
SEQRES 31 B 718 ALA VAL TYR ASN THR ALA GLN VAL ASN SER GLN SER SER
SEQRES 32 B 718 SER ILE LYS MET THR PRO ALA GLY GLY GLY LEU SER TRP
SEQRES 33 B 718 GLN SER TYR ASN GLU GLU THR PRO THR ALA ASP ASP SER
SEQRES 34 B 718 ASP THR LEU THR ALA ASN GLY LEU TRP GLU GLN LYS ASN
SEQRES 35 B 718 VAL THR ARG ASP SER SER ASP TYR LEU TRP TYR MET THR
SEQRES 36 B 718 ASN VAL ASN ILE ALA SER ASN GLU GLY PHE LEU LYS ASN
SEQRES 37 B 718 GLY LYS ASP PRO TYR LEU THR VAL MET SER ALA GLY HIS
SEQRES 38 B 718 VAL LEU HIS VAL PHE VAL ASN GLY LYS LEU SER GLY THR
SEQRES 39 B 718 VAL TYR GLY THR LEU ASP ASN PRO LYS LEU THR TYR SER
SEQRES 40 B 718 GLY ASN VAL LYS LEU ARG ALA GLY ILE ASN LYS ILE SER
SEQRES 41 B 718 LEU LEU SER VAL SER VAL GLY LEU PRO ASN VAL GLY VAL
SEQRES 42 B 718 HIS TYR ASP THR TRP ASN ALA GLY VAL LEU GLY PRO VAL
SEQRES 43 B 718 THR LEU SER GLY LEU ASN GLU GLY SER ARG ASN LEU ALA
SEQRES 44 B 718 LYS GLN LYS TRP SER TYR LYS VAL GLY LEU LYS GLY GLU
SEQRES 45 B 718 SER LEU SER LEU HIS SER LEU SER GLY SER SER SER VAL
SEQRES 46 B 718 GLU TRP VAL ARG GLY SER LEU MET ALA GLN LYS GLN PRO
SEQRES 47 B 718 LEU THR TRP TYR LYS ALA THR PHE ASN ALA PRO GLY GLY
SEQRES 48 B 718 ASN ASP PRO LEU ALA LEU ASP MET ALA SER MET GLY LYS
SEQRES 49 B 718 GLY GLN ILE TRP ILE ASN GLY GLU GLY VAL GLY ARG HIS
SEQRES 50 B 718 TRP PRO GLY TYR ILE ALA GLN GLY ASP CYS SER LYS CYS
SEQRES 51 B 718 SER TYR ALA GLY THR PHE ASN GLU LYS LYS CYS GLN THR
SEQRES 52 B 718 ASN CYS GLY GLN PRO SER GLN ARG TRP TYR HIS VAL PRO
SEQRES 53 B 718 ARG SER TRP LEU LYS PRO SER GLY ASN LEU LEU VAL VAL
SEQRES 54 B 718 PHE GLU GLU TRP GLY GLY ASN PRO THR GLY ILE SER LEU
SEQRES 55 B 718 VAL ARG ARG SER ARG SER ALA ALA ALA ALA SER PHE LEU
SEQRES 56 B 718 GLU GLN LYS
MODRES 3W5G ASN A 459 ASN GLYCOSYLATION SITE
MODRES 3W5G ASN B 282 ASN GLYCOSYLATION SITE
MODRES 3W5G ASN B 459 ASN GLYCOSYLATION SITE
MODRES 3W5G ASN A 282 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 801 14
HET NAG A 802 14
HET GAL A 803 12
HET GAL A 804 12
HET GAL A 805 12
HET GAL A 806 12
HET GAL B 801 12
HET NAG B 804 14
HET GAL B 805 12
HET GAL B 806 12
HET GAL B 807 12
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 6 GAL 8(C6 H12 O6)
FORMUL 15 HOH *198(H2 O)
HELIX 1 1 TYR A 48 SER A 51 5 4
HELIX 2 2 MET A 55 GLY A 66 1 12
HELIX 3 3 PHE A 76 GLU A 81 1 6
HELIX 4 4 GLU A 90 TYR A 93 5 4
HELIX 5 5 ASP A 94 ALA A 105 1 12
HELIX 6 6 TRP A 121 PHE A 126 5 6
HELIX 7 7 PRO A 127 VAL A 133 5 7
HELIX 8 8 ASN A 142 GLU A 163 1 22
HELIX 9 9 PHE A 166 GLY A 170 5 5
HELIX 10 10 TYR A 182 GLY A 190 1 9
HELIX 11 11 GLY A 190 GLY A 206 1 17
HELIX 12 12 PRO A 267 ASN A 281 1 15
HELIX 13 13 PRO A 325 VAL A 345 1 21
HELIX 14 14 GLU A 456 ARG A 462 1 7
HELIX 15 15 GLU A 480 ASN A 485 1 6
HELIX 16 16 HIS A 551 TRP A 555 5 5
HELIX 17 17 LEU A 586 LEU A 591 1 6
HELIX 18 18 PRO A 693 LEU A 697 5 5
HELIX 19 19 ASN A 713 ILE A 717 5 5
HELIX 20 20 TYR B 48 SER B 51 5 4
HELIX 21 21 MET B 55 GLY B 66 1 12
HELIX 22 22 PHE B 76 GLU B 81 1 6
HELIX 23 23 GLU B 90 TYR B 93 5 4
HELIX 24 24 ASP B 94 ALA B 105 1 12
HELIX 25 25 TRP B 121 PHE B 126 5 6
HELIX 26 26 PRO B 127 VAL B 133 5 7
HELIX 27 27 ASN B 142 GLU B 163 1 22
HELIX 28 28 PHE B 166 GLY B 170 5 5
HELIX 29 29 TYR B 182 GLY B 190 1 9
HELIX 30 30 GLY B 190 LEU B 207 1 18
HELIX 31 31 PRO B 267 ASN B 281 1 15
HELIX 32 32 PRO B 325 VAL B 345 1 21
HELIX 33 33 GLU B 456 ARG B 462 1 7
HELIX 34 34 HIS B 551 TRP B 555 5 5
HELIX 35 35 LEU B 586 LEU B 591 1 6
HELIX 36 36 SER B 595 SER B 601 1 7
HELIX 37 37 ARG B 606 MET B 610 5 5
HELIX 38 38 PRO B 693 LEU B 697 5 5
HELIX 39 39 ASN B 713 ILE B 717 5 5
SHEET 1 A 3 VAL A 25 TYR A 27 0
SHEET 2 A 3 ILE A 32 ILE A 34 -1 O ILE A 33 N SER A 26
SHEET 3 A 3 LYS A 37 LYS A 39 -1 O LYS A 37 N ILE A 34
SHEET 1 B 9 LEU A 41 ILE A 46 0
SHEET 2 B 9 VAL A 70 TYR A 74 1 O GLU A 72 N ILE A 46
SHEET 3 B 9 TYR A 108 GLY A 114 1 O ARG A 112 N THR A 73
SHEET 4 B 9 ILE A 173 ILE A 178 1 O ILE A 174 N VAL A 109
SHEET 5 B 9 TRP A 213 CYS A 216 1 O ILE A 214 N ALA A 176
SHEET 6 B 9 ILE A 226 GLY A 231 1 O ILE A 226 N MET A 215
SHEET 7 B 9 MET A 247 TRP A 252 1 O GLU A 250 N GLY A 231
SHEET 8 B 9 PHE A 285 HIS A 292 1 O ASN A 287 N VAL A 251
SHEET 9 B 9 LEU A 41 ILE A 46 1 N SER A 45 O TYR A 288
SHEET 1 C 2 ILE A 263 PRO A 264 0
SHEET 2 C 2 GLN A 679 THR A 680 -1 O THR A 680 N ILE A 263
SHEET 1 D 5 ALA A 350 SER A 353 0
SHEET 2 D 5 GLN A 358 ARG A 364 -1 O VAL A 362 N ALA A 350
SHEET 3 D 5 CYS A 370 ASN A 376 -1 O ALA A 371 N TYR A 363
SHEET 4 D 5 SER A 398 LEU A 402 -1 O LEU A 402 N ALA A 372
SHEET 5 D 5 TYR A 410 ASN A 411 -1 O TYR A 410 N ILE A 401
SHEET 1 E 2 VAL A 383 PHE A 387 0
SHEET 2 E 2 ARG A 390 LEU A 394 -1 O LEU A 394 N VAL A 383
SHEET 1 F 4 SER A 421 PRO A 426 0
SHEET 2 F 4 SER A 718 SER A 725 -1 O ARG A 721 N THR A 425
SHEET 3 F 4 LEU A 632 ASP A 635 -1 N ASP A 635 O SER A 718
SHEET 4 F 4 TRP A 689 VAL A 692 -1 O VAL A 692 N LEU A 632
SHEET 1 G 5 GLN A 434 ASN A 437 0
SHEET 2 G 5 THR A 617 PHE A 623 -1 O TRP A 618 N TYR A 436
SHEET 3 G 5 ASN A 702 GLU A 708 -1 O GLU A 708 N THR A 617
SHEET 4 G 5 GLY A 642 ILE A 646 -1 N TRP A 645 O VAL A 705
SHEET 5 G 5 GLU A 649 HIS A 654 -1 O GLU A 649 N ILE A 646
SHEET 1 H 6 THR A 450 ALA A 451 0
SHEET 2 H 6 TRP A 580 VAL A 584 -1 O TRP A 580 N ALA A 451
SHEET 3 H 6 TYR A 467 ILE A 476 -1 N MET A 471 O SER A 581
SHEET 4 H 6 GLY A 532 VAL A 541 -1 O ASN A 534 N VAL A 474
SHEET 5 H 6 VAL A 499 VAL A 504 -1 N PHE A 503 O SER A 537
SHEET 6 H 6 LYS A 507 TYR A 513 -1 O SER A 509 N VAL A 502
SHEET 1 I 4 LEU A 521 ASN A 526 0
SHEET 2 I 4 TYR A 490 SER A 495 -1 N VAL A 493 O TYR A 523
SHEET 3 I 4 VAL A 559 SER A 566 -1 O SER A 566 N TYR A 490
SHEET 4 I 4 SER A 572 ASN A 574 -1 O ARG A 573 N LEU A 565
SHEET 1 J 3 VAL B 25 TYR B 27 0
SHEET 2 J 3 ILE B 32 ILE B 34 -1 O ILE B 33 N SER B 26
SHEET 3 J 3 LYS B 37 LYS B 39 -1 O LYS B 37 N ILE B 34
SHEET 1 K 9 LEU B 41 ILE B 46 0
SHEET 2 K 9 VAL B 70 TYR B 74 1 O GLU B 72 N GLY B 44
SHEET 3 K 9 TYR B 108 GLY B 114 1 O ARG B 112 N THR B 73
SHEET 4 K 9 ILE B 173 ILE B 178 1 O ILE B 174 N VAL B 109
SHEET 5 K 9 TRP B 213 CYS B 216 1 O ILE B 214 N ALA B 176
SHEET 6 K 9 ILE B 226 GLY B 231 1 O ILE B 226 N MET B 215
SHEET 7 K 9 MET B 247 TRP B 252 1 O GLU B 250 N GLY B 231
SHEET 8 K 9 PHE B 285 HIS B 292 1 O PHE B 285 N TRP B 248
SHEET 9 K 9 LEU B 41 ILE B 46 1 N SER B 45 O TYR B 288
SHEET 1 L 2 ILE B 263 GLN B 265 0
SHEET 2 L 2 CYS B 678 THR B 680 -1 O THR B 680 N ILE B 263
SHEET 1 M 5 ALA B 350 SER B 353 0
SHEET 2 M 5 GLN B 358 ARG B 364 -1 O VAL B 362 N ALA B 350
SHEET 3 M 5 CYS B 370 ASN B 376 -1 O ALA B 371 N TYR B 363
SHEET 4 M 5 SER B 398 LEU B 402 -1 O LEU B 402 N ALA B 372
SHEET 5 M 5 TYR B 410 ASN B 411 -1 O TYR B 410 N ILE B 401
SHEET 1 N 2 VAL B 383 PHE B 387 0
SHEET 2 N 2 ARG B 390 LEU B 394 -1 O TYR B 392 N VAL B 385
SHEET 1 O 4 SER B 421 PRO B 426 0
SHEET 2 O 4 SER B 718 SER B 725 -1 O ARG B 721 N THR B 425
SHEET 3 O 4 LEU B 632 ASP B 635 -1 N ASP B 635 O SER B 718
SHEET 4 O 4 TRP B 689 VAL B 692 -1 O VAL B 692 N LEU B 632
SHEET 1 P 5 GLN B 434 ASN B 437 0
SHEET 2 P 5 THR B 617 PHE B 623 -1 O TRP B 618 N TYR B 436
SHEET 3 P 5 ASN B 702 GLU B 708 -1 O GLU B 708 N THR B 617
SHEET 4 P 5 GLY B 642 ILE B 646 -1 N TRP B 645 O VAL B 705
SHEET 5 P 5 GLU B 649 HIS B 654 -1 O HIS B 654 N GLY B 642
SHEET 1 Q 6 THR B 450 ALA B 451 0
SHEET 2 Q 6 TRP B 580 VAL B 584 -1 O TRP B 580 N ALA B 451
SHEET 3 Q 6 TYR B 467 ILE B 476 -1 N MET B 471 O SER B 581
SHEET 4 Q 6 GLY B 532 VAL B 541 -1 O ASN B 534 N VAL B 474
SHEET 5 Q 6 VAL B 499 VAL B 504 -1 N PHE B 503 O SER B 537
SHEET 6 Q 6 LYS B 507 TYR B 513 -1 O SER B 509 N VAL B 502
SHEET 1 R 4 LEU B 521 ASN B 526 0
SHEET 2 R 4 TYR B 490 SER B 495 -1 N VAL B 493 O TYR B 523
SHEET 3 R 4 VAL B 559 SER B 566 -1 O SER B 566 N TYR B 490
SHEET 4 R 4 SER B 572 ASN B 574 -1 O ARG B 573 N LEU B 565
SSBOND 1 CYS A 229 CYS A 234 1555 1555 2.09
SSBOND 2 CYS A 370 CYS A 405 1555 1555 2.04
SSBOND 3 CYS A 664 CYS A 682 1555 1555 2.02
SSBOND 4 CYS A 667 CYS A 678 1555 1555 2.04
SSBOND 5 CYS B 229 CYS B 234 1555 1555 2.07
SSBOND 6 CYS B 370 CYS B 405 1555 1555 2.05
SSBOND 7 CYS B 664 CYS B 682 1555 1555 2.02
SSBOND 8 CYS B 667 CYS B 678 1555 1555 2.03
LINK ND2 ASN A 282 C1 NAG A 801 1555 1555 1.53
LINK ND2 ASN A 459 C1 NAG A 802 1555 1555 1.41
LINK ND2 ASN B 282 C1 NAG C 1 1555 1555 1.41
LINK ND2 ASN B 459 C1 NAG B 804 1555 1555 1.50
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
CISPEP 1 GLY A 114 PRO A 115 0 1.50
CISPEP 2 ASP A 223 PRO A 224 0 1.74
CISPEP 3 TYR A 289 MET A 290 0 0.20
CISPEP 4 GLU A 324 PRO A 325 0 6.26
CISPEP 5 GLY A 497 HIS A 498 0 -2.14
CISPEP 6 GLY A 561 PRO A 562 0 -2.85
CISPEP 7 GLY B 114 PRO B 115 0 4.17
CISPEP 8 ASP B 223 PRO B 224 0 2.26
CISPEP 9 TYR B 289 MET B 290 0 1.19
CISPEP 10 GLU B 324 PRO B 325 0 9.31
CISPEP 11 GLY B 497 HIS B 498 0 -3.03
CISPEP 12 GLY B 561 PRO B 562 0 -0.81
CRYST1 93.930 106.382 162.379 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010646 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006158 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
