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HEADER HYDROLASE 19-JUL-10 3O0D
TITLE CRYSTAL STRUCTURE OF LIP2 LIPASE FROM YARROWIA LIPOLYTICA AT 1.7 A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G;
COMPND 4 SYNONYM: YALI0A20350P;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YARROWIA LIPOLYTICA;
SOURCE 3 ORGANISM_COMMON: CANDIDA LIPOLYTICA;
SOURCE 4 ORGANISM_TAXID: 4952;
SOURCE 5 GENE: LIP2, YALI0A20350G;
SOURCE 6 EXPRESSION_SYSTEM: YARROWIA LIPOLYTICA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4952
KEYWDS ALPHA/BETA-HYDROLASE, LIPASE, LIPIDS BINDING, GLYCOSYLATION,
KEYWDS 2 EXTRACELLULAR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.BORDES,S.TRANIER,L.MOUREY,A.MARTY
REVDAT 1 24-NOV-10 3O0D 0
JRNL AUTH F.BORDES,S.BARBE,P.ESCALIER,L.MOUREY,I.ANDRE,A.MARTY,
JRNL AUTH 2 S.TRANIER
JRNL TITL EXPLORING THE CONFORMATIONAL STATES AND REARRANGEMENTS OF
JRNL TITL 2 YARROWIA LIPOLYTICA LIPASE.
JRNL REF BIOPHYS.J. V. 99 2225 2010
JRNL REFN ISSN 0006-3495
JRNL PMID 20923657
JRNL DOI 10.1016/J.BPJ.2010.07.040
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 216938
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11428
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 805
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16269
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 339
REMARK 3 SOLVENT ATOMS : 1653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : -0.13000
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): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.962
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17431 ; 0.027 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23882 ; 2.109 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2191 ; 6.668 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 816 ;35.623 ;24.951
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2597 ;14.740 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;17.206 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2666 ; 0.169 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13547 ; 0.013 ; 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): 10637 ; 1.411 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17301 ; 2.244 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6794 ; 3.221 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6552 ; 4.824 ; 4.500
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O0D COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060505.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9395
REMARK 200 MONOCHROMATOR : CHANNEL CUT ESRF 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 : 228540
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07300
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34300
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 0.1M MES, 0.02M CACL2, 0.2M
REMARK 280 NACL, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K
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 57.67700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.62750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.07050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.62750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.67700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.07050
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, 3, 4, 5, 6, 7
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 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET D 101
REMARK 465 GLN D 102
REMARK 465 ALA D 103
REMARK 465 PRO D 104
REMARK 465 ILE F 100
REMARK 465 MET F 101
REMARK 465 GLN F 102
REMARK 465 LEU G 280
REMARK 465 GLN G 281
REMARK 465 GLN G 282
REMARK 465 VAL G 283
REMARK 465 ILE G 301
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 92 CD OE1 OE2
REMARK 470 SER A 116 OG
REMARK 470 ASN A 127 OD1 ND2
REMARK 470 LYS B 218 CE NZ
REMARK 470 LYS C 36 CD CE NZ
REMARK 470 GLU C 92 CG CD OE1 OE2
REMARK 470 TYR D 2 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 36 CE NZ
REMARK 470 GLU D 57 OE2
REMARK 470 ARG D 99 NH1 NH2
REMARK 470 ILE D 100 CD1
REMARK 470 ASP D 121 CG OD1 OD2
REMARK 470 LYS D 203 CD CE NZ
REMARK 470 LYS D 218 CD CE NZ
REMARK 470 PHE D 237 CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP D 238 CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP D 238 CH2
REMARK 470 ASP D 239 CG OD1 OD2
REMARK 470 LYS D 271 CD CE NZ
REMARK 470 LEU D 279 CD1 CD2
REMARK 470 LEU D 280 CD1 CD2
REMARK 470 LYS E 36 CE NZ
REMARK 470 GLN E 131 CG CD OE1 NE2
REMARK 470 LYS E 203 CE NZ
REMARK 470 PHE E 237 CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP E 239 CG OD1 OD2
REMARK 470 THR F 117 CG2
REMARK 470 GLU F 149 CD OE1 OE2
REMARK 470 LYS F 203 CD CE NZ
REMARK 470 ASN F 210 OD1 ND2
REMARK 470 LYS F 218 CG CD CE NZ
REMARK 470 ASP F 239 CG OD1 OD2
REMARK 470 LEU F 279 CD1 CD2
REMARK 470 LEU F 280 CD1 CD2
REMARK 470 VAL G 1 CG2
REMARK 470 ASN G 42 CG OD1 ND2
REMARK 470 GLN G 46 CG CD OE1 NE2
REMARK 470 VAL G 53 CG2
REMARK 470 GLU G 57 CD OE1 OE2
REMARK 470 LEU G 72 CD1
REMARK 470 LYS G 79 CD CE NZ
REMARK 470 LEU G 105 CG CD1 CD2
REMARK 470 GLU G 149 CG CD OE1 OE2
REMARK 470 ASP G 153 CG OD1 OD2
REMARK 470 LEU G 279 CG CD1 CD2
REMARK 470 ILE G 286 CG1 CD1
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 O HOH C 1042 O HOH C 1586 1.85
REMARK 500 O HOH E 939 O HOH E 2119 1.86
REMARK 500 O HOH D 1934 O HOH E 1223 1.87
REMARK 500 O HOH C 363 O HOH C 1361 1.93
REMARK 500 O HOH F 346 O HOH F 1061 1.95
REMARK 500 O HOH E 1578 O HOH E 1800 1.99
REMARK 500 O HOH D 926 O HOH D 1403 1.99
REMARK 500 O HOH D 2011 O HOH D 2160 2.01
REMARK 500 O HOH E 1388 O HOH E 1749 2.02
REMARK 500 O HOH C 856 O HOH C 1774 2.03
REMARK 500 O HOH A 1867 O HOH A 2002 2.04
REMARK 500 O HOH B 488 O HOH B 1525 2.05
REMARK 500 O HOH C 349 O HOH C 1815 2.11
REMARK 500 NZ LYS B 176 O HOH B 1996 2.12
REMARK 500 O4 MPD E 304 O HOH E 952 2.12
REMARK 500 O HOH E 972 O HOH E 1460 2.13
REMARK 500 O HOH E 379 O HOH E 1377 2.13
REMARK 500 O HOH A 1059 O HOH A 1660 2.13
REMARK 500 O HOH F 1572 O HOH F 2074 2.14
REMARK 500 O SER G 116 O HOH G 1994 2.15
REMARK 500 O HOH F 1706 O HOH F 1793 2.16
REMARK 500 O HOH D 2090 O HOH E 1811 2.18
REMARK 500 OE2 GLU B 6 O HOH B 1982 2.18
REMARK 500 OD1 ASN B 210 O HOH B 2149 2.19
REMARK 500 OE2 GLU A 57 O HOH A 2103 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 CD2 LEU D 64 CG2 THR G 96 4565 2.14
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 TYR E 137 CD1 TYR E 137 CE1 0.106
REMARK 500 TRP E 238 CB TRP E 238 CG -0.142
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 LEU G 45 CA - CB - CG ANGL. DEV. = 16.5 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 PHE A 41 69.94 -163.11
REMARK 500 CYS A 43 33.66 -163.25
REMARK 500 SER A 162 -131.82 65.03
REMARK 500 CYS A 273 -144.35 -117.74
REMARK 500 PHE A 293 -58.40 70.92
REMARK 500 PHE B 41 75.28 -157.20
REMARK 500 CYS B 43 33.95 -160.80
REMARK 500 SER B 162 -127.31 66.08
REMARK 500 CYS B 273 -142.32 -120.67
REMARK 500 ASN B 284 66.74 82.68
REMARK 500 PHE B 293 -63.16 68.35
REMARK 500 PHE C 41 73.26 -163.58
REMARK 500 CYS C 43 34.53 -164.40
REMARK 500 SER C 162 -131.55 70.64
REMARK 500 CYS C 273 -140.60 -122.21
REMARK 500 ASN C 284 63.51 82.99
REMARK 500 PHE C 293 -63.79 75.44
REMARK 500 PHE D 41 74.41 -168.75
REMARK 500 CYS D 43 33.03 -162.28
REMARK 500 HIS D 126 121.98 -39.20
REMARK 500 SER D 162 -130.84 70.14
REMARK 500 CYS D 273 -139.23 -112.72
REMARK 500 ASN D 284 58.67 91.60
REMARK 500 PHE D 293 -60.64 69.04
REMARK 500 PHE E 41 74.57 -162.26
REMARK 500 CYS E 43 28.57 -164.45
REMARK 500 SER E 162 -130.00 66.00
REMARK 500 PHE E 237 68.72 -105.76
REMARK 500 ASP E 239 93.80 -17.09
REMARK 500 CYS E 273 -145.96 -117.29
REMARK 500 PHE E 293 -59.58 74.15
REMARK 500 PHE F 41 69.23 -165.79
REMARK 500 CYS F 43 31.18 -159.33
REMARK 500 SER F 162 -129.20 71.72
REMARK 500 CYS F 273 -137.11 -121.72
REMARK 500 VAL F 283 167.95 -49.94
REMARK 500 PHE F 293 -62.87 70.26
REMARK 500 PHE G 41 82.66 -161.26
REMARK 500 LEU G 45 55.06 -95.44
REMARK 500 GLN G 46 -44.69 -143.77
REMARK 500 GLN G 102 36.56 -89.01
REMARK 500 SER G 162 -134.30 61.52
REMARK 500 CYS G 273 -134.58 -117.75
REMARK 500 PHE G 293 -53.28 77.43
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 D2086 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH F2073 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH F2074 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A2089 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH E2132 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH C2075 DISTANCE = 6.56 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD F 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 304
DBREF 3O0D A 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
DBREF 3O0D B 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
DBREF 3O0D C 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
DBREF 3O0D D 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
DBREF 3O0D E 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
DBREF 3O0D F 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
DBREF 3O0D G 1 301 UNP Q9P8F7 Q9P8F7_YARLI 34 334
SEQRES 1 A 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 A 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 A 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 A 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 A 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 A 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 A 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 A 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 A 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 A 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 A 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 A 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 A 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 A 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 A 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 A 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 A 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 A 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 A 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 A 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 A 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 A 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 A 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 A 301 GLY ILE
SEQRES 1 B 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 B 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 B 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 B 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 B 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 B 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 B 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 B 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 B 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 B 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 B 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 B 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 B 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 B 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 B 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 B 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 B 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 B 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 B 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 B 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 B 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 B 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 B 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 B 301 GLY ILE
SEQRES 1 C 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 C 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 C 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 C 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 C 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 C 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 C 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 C 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 C 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 C 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 C 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 C 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 C 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 C 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 C 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 C 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 C 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 C 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 C 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 C 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 C 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 C 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 C 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 C 301 GLY ILE
SEQRES 1 D 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 D 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 D 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 D 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 D 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 D 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 D 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 D 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 D 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 D 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 D 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 D 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 D 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 D 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 D 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 D 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 D 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 D 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 D 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 D 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 D 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 D 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 D 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 D 301 GLY ILE
SEQRES 1 E 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 E 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 E 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 E 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 E 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 E 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 E 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 E 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 E 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 E 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 E 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 E 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 E 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 E 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 E 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 E 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 E 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 E 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 E 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 E 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 E 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 E 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 E 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 E 301 GLY ILE
SEQRES 1 F 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 F 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 F 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 F 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 F 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 F 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 F 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 F 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 F 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 F 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 F 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 F 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 F 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 F 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 F 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 F 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 F 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 F 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 F 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 F 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 F 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 F 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 F 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 F 301 GLY ILE
SEQRES 1 G 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 G 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 G 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 G 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 G 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 G 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 G 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 G 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 G 301 LEU THR ASN PHE ASP LEU ALA ALA ASN ILE SER SER THR
SEQRES 10 G 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 G 301 GLN SER TYR ASN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 G 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 G 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 G 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 G 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 G 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 G 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 G 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 G 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 G 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 G 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 G 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 G 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 G 301 GLY ILE
MODRES 3O0D ASN E 134 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN E 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN B 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN C 134 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN D 134 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN G 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN F 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN G 134 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN C 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN D 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN A 134 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN A 113 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN F 134 ASN GLYCOSYLATION SITE
MODRES 3O0D ASN B 134 ASN GLYCOSYLATION SITE
HET NAG A 302 14
HET NAG A 303 14
HET MPD A 304 8
HET MPD A 305 8
HET MPD A 306 8
HET MRD A 307 8
HET K A 308 1
HET NAG B 302 28
HET NAG B 303 14
HET MPD B 304 8
HET MPD B 305 8
HET MRD B 306 8
HET K B 307 1
HET NAG C 302 14
HET NAG C 303 14
HET MPD C 304 8
HET MPD C 305 8
HET MPD C 306 8
HET K C 307 1
HET NAG D 302 14
HET NAG D 303 14
HET MPD D 304 8
HET MRD D 305 8
HET MPD D 306 8
HET K D 307 1
HET NAG E 302 14
HET NAG E 303 14
HET MPD E 304 8
HET MPD E 305 8
HET K E 306 1
HET NAG F 302 14
HET NAG F 303 14
HET MRD F 304 8
HET MPD F 305 8
HET K F 306 1
HET NAG G 302 14
HET NAG G 303 14
HET K G 304 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM K POTASSIUM ION
FORMUL 8 NAG 14(C8 H15 N O6)
FORMUL 10 MPD 13(C6 H14 O2)
FORMUL 13 MRD 4(C6 H14 O2)
FORMUL 14 K 7(K 1+)
FORMUL 46 HOH *1653(H2 O)
HELIX 1 1 ASP A 11 GLY A 28 1 18
HELIX 2 2 TYR A 29 VAL A 31 5 3
HELIX 3 3 GLN A 46 PHE A 50 5 5
HELIX 4 4 SER A 90 MET A 101 1 12
HELIX 5 5 ASP A 109 ALA A 111 5 3
HELIX 6 6 ASN A 127 TYR A 151 1 25
HELIX 7 7 SER A 162 ASN A 178 1 17
HELIX 8 8 ASN A 194 GLY A 207 1 14
HELIX 9 9 ILE A 231 VAL A 235 5 5
HELIX 10 10 PRO A 258 SER A 260 5 3
HELIX 11 11 CYS A 273 ASN A 277 5 5
HELIX 12 12 ASN A 284 GLN A 291 1 8
HELIX 13 13 ASP B 11 GLY B 28 1 18
HELIX 14 14 TYR B 29 VAL B 31 5 3
HELIX 15 15 GLN B 46 PHE B 50 5 5
HELIX 16 16 SER B 90 MET B 101 1 12
HELIX 17 17 ASP B 109 ALA B 111 5 3
HELIX 18 18 ASN B 127 TYR B 151 1 25
HELIX 19 19 SER B 162 ASN B 178 1 17
HELIX 20 20 ASN B 194 GLY B 207 1 14
HELIX 21 21 ILE B 231 VAL B 235 5 5
HELIX 22 22 PRO B 258 SER B 260 5 3
HELIX 23 23 CYS B 273 ASN B 277 5 5
HELIX 24 24 ASN B 284 GLN B 291 1 8
HELIX 25 25 ASP C 11 GLY C 28 1 18
HELIX 26 26 TYR C 29 VAL C 31 5 3
HELIX 27 27 GLN C 46 PHE C 50 5 5
HELIX 28 28 SER C 90 MET C 101 1 12
HELIX 29 29 ASP C 109 ALA C 111 5 3
HELIX 30 30 ASN C 127 TYR C 151 1 25
HELIX 31 31 SER C 162 ASN C 178 1 17
HELIX 32 32 ASN C 194 GLY C 207 1 14
HELIX 33 33 ILE C 231 VAL C 235 5 5
HELIX 34 34 PRO C 258 SER C 260 5 3
HELIX 35 35 CYS C 273 ASN C 277 5 5
HELIX 36 36 ASN C 284 GLN C 291 1 8
HELIX 37 37 ASP D 11 GLY D 28 1 18
HELIX 38 38 TYR D 29 VAL D 31 5 3
HELIX 39 39 GLN D 46 PHE D 50 5 5
HELIX 40 40 SER D 90 ILE D 100 1 11
HELIX 41 41 ASP D 109 ALA D 111 5 3
HELIX 42 42 HIS D 126 TYR D 151 1 26
HELIX 43 43 SER D 162 ASN D 178 1 17
HELIX 44 44 ALA D 195 GLY D 207 1 13
HELIX 45 45 ILE D 231 VAL D 235 5 5
HELIX 46 46 PRO D 258 SER D 260 5 3
HELIX 47 47 CYS D 273 ASN D 277 5 5
HELIX 48 48 ASN D 284 GLN D 291 1 8
HELIX 49 49 ASP E 11 GLY E 28 1 18
HELIX 50 50 TYR E 29 VAL E 31 5 3
HELIX 51 51 GLN E 46 PHE E 50 5 5
HELIX 52 52 SER E 90 MET E 101 1 12
HELIX 53 53 ASP E 109 ALA E 111 5 3
HELIX 54 54 ASN E 127 TYR E 151 1 25
HELIX 55 55 SER E 162 ASN E 178 1 17
HELIX 56 56 ALA E 195 GLY E 207 1 13
HELIX 57 57 ILE E 231 VAL E 235 5 5
HELIX 58 58 PRO E 258 SER E 260 5 3
HELIX 59 59 CYS E 273 ASN E 277 5 5
HELIX 60 60 ASN E 284 GLN E 291 1 8
HELIX 61 61 ASP F 11 GLY F 28 1 18
HELIX 62 62 TYR F 29 VAL F 31 5 3
HELIX 63 63 GLN F 46 PHE F 50 5 5
HELIX 64 64 SER F 90 ARG F 99 1 10
HELIX 65 65 ASP F 109 ALA F 111 5 3
HELIX 66 66 ASN F 127 TYR F 151 1 25
HELIX 67 67 SER F 162 ASN F 178 1 17
HELIX 68 68 ASN F 194 GLY F 207 1 14
HELIX 69 69 ILE F 231 VAL F 235 5 5
HELIX 70 70 PRO F 258 SER F 260 5 3
HELIX 71 71 CYS F 273 ASN F 277 5 5
HELIX 72 72 THR F 278 VAL F 283 1 6
HELIX 73 73 ASN F 284 GLN F 291 1 8
HELIX 74 74 ASP G 11 GLY G 28 1 18
HELIX 75 75 TYR G 29 VAL G 31 5 3
HELIX 76 76 GLN G 46 PHE G 50 5 5
HELIX 77 77 SER G 90 ILE G 95 1 6
HELIX 78 78 ASP G 97 MET G 101 5 5
HELIX 79 79 ASP G 109 ALA G 111 5 3
HELIX 80 80 ASN G 127 TYR G 151 1 25
HELIX 81 81 SER G 162 ASN G 178 1 17
HELIX 82 82 ASN G 194 GLY G 207 1 14
HELIX 83 83 ILE G 231 VAL G 235 5 5
HELIX 84 84 PRO G 258 SER G 260 5 3
HELIX 85 85 CYS G 273 ASN G 277 5 5
HELIX 86 86 ASN G 284 GLN G 291 1 8
SHEET 1 A 2 THR A 3 SER A 4 0
SHEET 2 A 2 SER A 269 ASN A 270 1 O SER A 269 N SER A 4
SHEET 1 B 9 THR A 7 SER A 8 0
SHEET 2 B 9 VAL A 262 CYS A 265 -1 O MET A 264 N SER A 8
SHEET 3 B 9 GLU A 247 ILE A 250 -1 N GLU A 247 O CYS A 265
SHEET 4 B 9 LEU A 222 HIS A 227 1 N THR A 226 O VAL A 248
SHEET 5 B 9 LEU A 183 LEU A 187 1 N THR A 186 O ILE A 225
SHEET 6 B 9 GLN A 155 HIS A 161 1 N VAL A 158 O LEU A 183
SHEET 7 B 9 GLN A 80 GLY A 87 1 N ILE A 81 O ALA A 157
SHEET 8 B 9 VAL A 68 ASP A 75 -1 N ASP A 75 O GLN A 80
SHEET 9 B 9 VAL A 53 HIS A 60 -1 N ILE A 56 O LEU A 72
SHEET 1 C 2 LEU A 105 ASN A 107 0
SHEET 2 C 2 LEU A 124 HIS A 126 -1 O VAL A 125 N THR A 106
SHEET 1 D 2 THR B 3 SER B 4 0
SHEET 2 D 2 SER B 269 ASN B 270 1 O SER B 269 N SER B 4
SHEET 1 E 9 THR B 7 HIS B 9 0
SHEET 2 E 9 VAL B 262 CYS B 265 -1 O MET B 264 N SER B 8
SHEET 3 E 9 GLU B 247 ILE B 250 -1 N GLU B 247 O CYS B 265
SHEET 4 E 9 LEU B 222 HIS B 227 1 N THR B 226 O VAL B 248
SHEET 5 E 9 LEU B 183 LEU B 187 1 N THR B 186 O ILE B 225
SHEET 6 E 9 GLN B 155 HIS B 161 1 N VAL B 158 O LEU B 183
SHEET 7 E 9 GLN B 80 GLY B 87 1 N ILE B 81 O ALA B 157
SHEET 8 E 9 VAL B 68 ASP B 75 -1 N ASP B 75 O GLN B 80
SHEET 9 E 9 VAL B 53 HIS B 60 -1 N ILE B 56 O LEU B 72
SHEET 1 F 2 LEU B 105 ASN B 107 0
SHEET 2 F 2 LEU B 124 HIS B 126 -1 O VAL B 125 N THR B 106
SHEET 1 G 2 THR C 3 SER C 4 0
SHEET 2 G 2 SER C 269 ASN C 270 1 O SER C 269 N SER C 4
SHEET 1 H 9 THR C 7 HIS C 9 0
SHEET 2 H 9 VAL C 262 CYS C 265 -1 O MET C 264 N SER C 8
SHEET 3 H 9 GLU C 247 ILE C 250 -1 N GLU C 247 O CYS C 265
SHEET 4 H 9 LEU C 222 HIS C 227 1 N THR C 226 O ILE C 250
SHEET 5 H 9 LEU C 183 LEU C 187 1 N THR C 186 O ILE C 225
SHEET 6 H 9 GLN C 155 HIS C 161 1 N VAL C 158 O LEU C 183
SHEET 7 H 9 GLN C 80 GLY C 87 1 N ILE C 81 O ALA C 157
SHEET 8 H 9 VAL C 68 ASP C 75 -1 N ASP C 75 O GLN C 80
SHEET 9 H 9 VAL C 53 HIS C 60 -1 N ILE C 56 O LEU C 72
SHEET 1 I 2 LEU C 105 ASN C 107 0
SHEET 2 I 2 LEU C 124 HIS C 126 -1 O VAL C 125 N THR C 106
SHEET 1 J 2 THR D 3 SER D 4 0
SHEET 2 J 2 SER D 269 ASN D 270 1 O SER D 269 N SER D 4
SHEET 1 K 9 THR D 7 HIS D 9 0
SHEET 2 K 9 VAL D 262 CYS D 265 -1 O MET D 264 N SER D 8
SHEET 3 K 9 GLU D 247 ILE D 250 -1 N PHE D 249 O VAL D 263
SHEET 4 K 9 LEU D 222 HIS D 227 1 N THR D 226 O VAL D 248
SHEET 5 K 9 LEU D 183 LEU D 187 1 N THR D 186 O ILE D 225
SHEET 6 K 9 GLN D 155 HIS D 161 1 N VAL D 158 O LEU D 183
SHEET 7 K 9 GLN D 80 GLY D 87 1 N ILE D 81 O ALA D 157
SHEET 8 K 9 VAL D 68 ASP D 75 -1 N ALA D 73 O TYR D 82
SHEET 9 K 9 VAL D 53 HIS D 60 -1 N ILE D 56 O LEU D 72
SHEET 1 L 2 THR D 106 ASN D 107 0
SHEET 2 L 2 LEU D 124 VAL D 125 -1 O VAL D 125 N THR D 106
SHEET 1 M 2 GLY D 193 ASN D 194 0
SHEET 2 M 2 TYR D 241 GLN D 242 -1 O GLN D 242 N GLY D 193
SHEET 1 N 2 THR E 3 SER E 4 0
SHEET 2 N 2 SER E 269 ASN E 270 1 O SER E 269 N SER E 4
SHEET 1 O 9 THR E 7 HIS E 9 0
SHEET 2 O 9 VAL E 262 CYS E 265 -1 O MET E 264 N SER E 8
SHEET 3 O 9 GLU E 247 ILE E 250 -1 N PHE E 249 O VAL E 263
SHEET 4 O 9 LEU E 222 HIS E 227 1 N ARG E 224 O VAL E 248
SHEET 5 O 9 LEU E 183 LEU E 187 1 N THR E 186 O ILE E 225
SHEET 6 O 9 GLN E 155 HIS E 161 1 N VAL E 158 O LEU E 183
SHEET 7 O 9 GLN E 80 GLY E 87 1 N ILE E 81 O ALA E 157
SHEET 8 O 9 VAL E 68 ASP E 75 -1 N ASP E 75 O GLN E 80
SHEET 9 O 9 VAL E 53 HIS E 60 -1 N ILE E 56 O LEU E 72
SHEET 1 P 2 LEU E 105 ASN E 107 0
SHEET 2 P 2 LEU E 124 HIS E 126 -1 O VAL E 125 N THR E 106
SHEET 1 Q 2 GLY E 193 ASN E 194 0
SHEET 2 Q 2 TYR E 241 GLN E 242 -1 O GLN E 242 N GLY E 193
SHEET 1 R 2 THR F 3 SER F 4 0
SHEET 2 R 2 SER F 269 ASN F 270 1 O SER F 269 N SER F 4
SHEET 1 S 9 THR F 7 HIS F 9 0
SHEET 2 S 9 VAL F 262 CYS F 265 -1 O MET F 264 N SER F 8
SHEET 3 S 9 GLU F 247 ILE F 250 -1 N PHE F 249 O VAL F 263
SHEET 4 S 9 LEU F 222 HIS F 227 1 N THR F 226 O VAL F 248
SHEET 5 S 9 LEU F 183 LEU F 187 1 N THR F 186 O ILE F 225
SHEET 6 S 9 GLN F 155 HIS F 161 1 N VAL F 158 O LEU F 183
SHEET 7 S 9 GLN F 80 GLY F 87 1 N ILE F 81 O ALA F 157
SHEET 8 S 9 VAL F 68 ASP F 75 -1 N ASP F 75 O GLN F 80
SHEET 9 S 9 VAL F 53 HIS F 60 -1 N ILE F 56 O LEU F 72
SHEET 1 T 2 LEU F 105 ASN F 107 0
SHEET 2 T 2 LEU F 124 HIS F 126 -1 O VAL F 125 N THR F 106
SHEET 1 U 2 THR G 3 SER G 4 0
SHEET 2 U 2 SER G 269 ASN G 270 1 O SER G 269 N SER G 4
SHEET 1 V 9 THR G 7 HIS G 9 0
SHEET 2 V 9 VAL G 262 CYS G 265 -1 O MET G 264 N SER G 8
SHEET 3 V 9 GLU G 247 ILE G 250 -1 N PHE G 249 O VAL G 263
SHEET 4 V 9 LEU G 222 HIS G 227 1 N THR G 226 O VAL G 248
SHEET 5 V 9 LEU G 183 LEU G 187 1 N THR G 186 O ILE G 225
SHEET 6 V 9 GLN G 155 HIS G 161 1 N VAL G 158 O LEU G 183
SHEET 7 V 9 GLN G 80 GLY G 87 1 N ILE G 81 O ALA G 157
SHEET 8 V 9 VAL G 68 ASP G 75 -1 N ALA G 73 O TYR G 82
SHEET 9 V 9 VAL G 53 PHE G 59 -1 N PHE G 59 O GLY G 70
SHEET 1 W 2 LEU G 105 ASN G 107 0
SHEET 2 W 2 LEU G 124 HIS G 126 -1 O VAL G 125 N THR G 106
SSBOND 1 CYS A 30 CYS A 299 1555 1555 2.11
SSBOND 2 CYS A 43 CYS A 47 1555 1555 2.09
SSBOND 3 CYS A 120 CYS A 123 1555 1555 2.10
SSBOND 4 CYS A 265 CYS A 273 1555 1555 2.09
SSBOND 5 CYS B 30 CYS B 299 1555 1555 2.06
SSBOND 6 CYS B 43 CYS B 47 1555 1555 2.10
SSBOND 7 CYS B 120 CYS B 123 1555 1555 2.05
SSBOND 8 CYS B 265 CYS B 273 1555 1555 2.06
SSBOND 9 CYS C 30 CYS C 299 1555 1555 2.09
SSBOND 10 CYS C 43 CYS C 47 1555 1555 2.23
SSBOND 11 CYS C 120 CYS C 123 1555 1555 2.10
SSBOND 12 CYS C 265 CYS C 273 1555 1555 2.09
SSBOND 13 CYS D 30 CYS D 299 1555 1555 2.02
SSBOND 14 CYS D 43 CYS D 47 1555 1555 2.09
SSBOND 15 CYS D 120 CYS D 123 1555 1555 2.10
SSBOND 16 CYS D 265 CYS D 273 1555 1555 2.05
SSBOND 17 CYS E 30 CYS E 299 1555 1555 2.03
SSBOND 18 CYS E 43 CYS E 47 1555 1555 2.13
SSBOND 19 CYS E 120 CYS E 123 1555 1555 2.09
SSBOND 20 CYS E 265 CYS E 273 1555 1555 2.23
SSBOND 21 CYS F 30 CYS F 299 1555 1555 2.15
SSBOND 22 CYS F 43 CYS F 47 1555 1555 2.10
SSBOND 23 CYS F 120 CYS F 123 1555 1555 2.08
SSBOND 24 CYS F 265 CYS F 273 1555 1555 2.04
SSBOND 25 CYS G 30 CYS G 299 1555 1555 2.07
SSBOND 26 CYS G 43 CYS G 47 1555 1555 2.15
SSBOND 27 CYS G 120 CYS G 123 1555 1555 2.08
SSBOND 28 CYS G 265 CYS G 273 1555 1555 2.05
LINK ND2 ASN E 134 C1 NAG E 303 1555 1555 1.42
LINK ND2 ASN E 113 C1 NAG E 302 1555 1555 1.43
LINK ND2 ASN B 113 C1 BNAG B 302 1555 1555 1.43
LINK ND2 ASN C 134 C1 NAG C 303 1555 1555 1.44
LINK ND2 ASN D 134 C1 NAG D 303 1555 1555 1.44
LINK ND2 ASN G 113 C1 NAG G 302 1555 1555 1.44
LINK ND2 ASN F 113 C1 NAG F 302 1555 1555 1.44
LINK ND2 ASN G 134 C1 NAG G 303 1555 1555 1.44
LINK ND2 ASN C 113 C1 NAG C 302 1555 1555 1.44
LINK ND2 ASN D 113 C1 NAG D 302 1555 1555 1.45
LINK ND2 ASN A 134 C1 NAG A 303 1555 1555 1.45
LINK ND2 ASN B 113 C1 ANAG B 302 1555 1555 1.45
LINK ND2 ASN A 113 C1 NAG A 302 1555 1555 1.45
LINK ND2 ASN F 134 C1 NAG F 303 1555 1555 1.46
LINK ND2 ASN B 134 C1 NAG B 303 1555 1555 1.46
LINK K K G 304 O HOH G1277 1555 1555 2.84
LINK K K C 307 O HOH C 333 1555 1555 2.94
LINK K K F 306 O HOH F 470 1555 1555 2.95
LINK K K E 306 O HOH E 541 1555 1555 2.96
LINK K K D 307 O HOH D 444 1555 1555 2.97
LINK K K B 307 O HOH B 371 1555 1555 2.99
LINK K K A 308 O HOH A 896 1555 1555 3.11
CISPEP 1 LYS A 39 PRO A 40 0 2.96
CISPEP 2 VAL A 235 PRO A 236 0 -7.84
CISPEP 3 LYS B 39 PRO B 40 0 5.06
CISPEP 4 VAL B 235 PRO B 236 0 -3.96
CISPEP 5 LYS C 39 PRO C 40 0 0.53
CISPEP 6 VAL C 235 PRO C 236 0 -5.15
CISPEP 7 LYS D 39 PRO D 40 0 -1.71
CISPEP 8 VAL D 235 PRO D 236 0 -3.05
CISPEP 9 LYS E 39 PRO E 40 0 -5.22
CISPEP 10 VAL E 235 PRO E 236 0 -0.53
CISPEP 11 LYS F 39 PRO F 40 0 3.68
CISPEP 12 VAL F 235 PRO F 236 0 -2.56
CISPEP 13 LYS G 39 PRO G 40 0 4.61
CISPEP 14 VAL G 235 PRO G 236 0 -7.97
SITE 1 AC1 8 ASN A 113 TYR A 137 GLY A 141 ASP A 145
SITE 2 AC1 8 ASN A 174 LEU A 175 ASN A 178 HIS A 180
SITE 1 AC2 8 LEU A 110 ALA A 112 ILE A 130 ASN A 134
SITE 2 AC2 8 ASN A 138 HOH A 829 HOH A1201 HOH A1579
SITE 1 AC3 6 GLN A 282 HOH A 343 HOH A 359 THR C 117
SITE 2 AC3 6 ALA C 118 HOH C 644
SITE 1 AC4 1 HOH B 762
SITE 1 AC5 2 PHE A 17 VAL A 216
SITE 1 AC6 6 ASP A 251 HOH A 491 HOH A 560 HOH A 929
SITE 2 AC6 6 ASN B 42 ALA B 48
SITE 1 AC7 3 GLN A 189 HIS A 243 CYS A 244
SITE 1 AC8 8 ASN B 113 TYR B 137 GLY B 141 ASP B 145
SITE 2 AC8 8 ASN B 174 LEU B 175 ASN B 178 HIS B 180
SITE 1 AC9 8 LEU B 110 ASN B 134 ASN B 138 HOH B 757
SITE 2 AC9 8 HOH B 942 HOH B1342 HOH B1503 HOH B1775
SITE 1 BC1 2 HIS B 9 HOH B 492
SITE 1 BC2 8 GLN A 12 HOH A 793 HOH A1008 GLN B 12
SITE 2 BC2 8 HOH B 325 HOH B 869 GLN C 12 HOH C 359
SITE 1 BC3 7 ARG B 228 ASP B 251 HOH B 753 HOH B1327
SITE 2 BC3 7 ASN C 42 ALA C 48 PRO C 51
SITE 1 BC4 4 GLN B 189 HIS B 243 CYS B 244 HOH B 371
SITE 1 BC5 13 ARG A 99 TRP A 238 HOH A1936 ASN C 113
SITE 2 BC5 13 TYR C 137 GLY C 141 ASP C 145 ASN C 174
SITE 3 BC5 13 LEU C 175 ASN C 178 HIS C 180 HOH C 944
SITE 4 BC5 13 HOH C1730
SITE 1 BC6 9 LEU C 110 ALA C 112 ASN C 134 ASN C 138
SITE 2 BC6 9 HOH C 546 HOH C 860 HOH C 970 HOH C1491
SITE 3 BC6 9 HOH C1623
SITE 1 BC7 7 ASN A 42 ALA A 48 PRO A 51 ARG C 228
SITE 2 BC7 7 ASP C 251 HOH C 469 HOH C1136
SITE 1 BC8 3 HOH A 812 HIS C 9 HOH C1774
SITE 1 BC9 4 HOH C 329 PHE D 38 GLU E 54 ILE E 56
SITE 1 CC1 4 GLN C 189 HIS C 243 CYS C 244 HOH C 333
SITE 1 CC2 11 GLN B 102 TRP B 238 ASP B 239 ASN D 113
SITE 2 CC2 11 TYR D 137 GLY D 141 ASP D 145 ASN D 174
SITE 3 CC2 11 LEU D 175 ASN D 178 HIS D 180
SITE 1 CC3 4 LEU D 110 ILE D 130 ASN D 134 ASN D 138
SITE 1 CC4 8 GLN D 12 HOH D 326 GLN E 12 HOH E 367
SITE 2 CC4 8 HOH E 503 HOH E1439 GLN F 12 HOH F 322
SITE 1 CC5 7 ILE C 286 GLY C 297 HOH C1379 LEU D 91
SITE 2 CC5 7 GLU D 92 HOH D 930 HOH D 959
SITE 1 CC6 2 HIS D 9 HOH E 561
SITE 1 CC7 4 GLN D 189 HIS D 243 CYS D 244 HOH D 444
SITE 1 CC8 12 GLN C 102 TRP C 238 ASP C 239 ASN E 113
SITE 2 CC8 12 TYR E 137 GLY E 141 ASP E 145 ASN E 174
SITE 3 CC8 12 LEU E 175 ASN E 178 HIS E 180 HOH E 994
SITE 1 CC9 7 MET C 101 HOH C1443 LEU E 110 ALA E 112
SITE 2 CC9 7 ILE E 130 ASN E 134 ASN E 138
SITE 1 DC1 7 GLY B 297 HOH B1190 HOH B1367 HOH B1375
SITE 2 DC1 7 HOH E 395 HOH E 847 HOH E 952
SITE 1 DC2 1 HOH F 695
SITE 1 DC3 4 GLN E 189 HIS E 243 CYS E 244 HOH E 541
SITE 1 DC4 8 ASN F 113 TYR F 137 GLY F 141 ASP F 145
SITE 2 DC4 8 ASN F 174 LEU F 175 ASN F 178 HIS F 180
SITE 1 DC5 6 GLN B 208 ASP B 212 HOH B 356 LEU F 110
SITE 2 DC5 6 ASN F 134 ASN F 138
SITE 1 DC6 2 HOH D 633 HIS F 9
SITE 1 DC7 6 HOH A1117 ILE F 286 GLY F 297 HOH F 339
SITE 2 DC7 6 HOH F1169 HOH F1305
SITE 1 DC8 4 GLN F 189 HIS F 243 CYS F 244 HOH F 470
SITE 1 DC9 8 ASN G 113 TYR G 137 GLY G 141 ASP G 145
SITE 2 DC9 8 ASN G 174 LEU G 175 ASN G 178 HIS G 180
SITE 1 EC1 4 GLN E 102 LEU G 110 ILE G 130 ASN G 134
SITE 1 EC2 4 GLN G 189 HIS G 243 CYS G 244 HOH G1277
CRYST1 115.354 132.141 137.255 90.00 90.00 90.00 P 21 21 21 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 0.008669 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007286 0.00000
TER 2413 ILE A 301
TER 4818 ILE B 301
TER 7191 ILE C 301
TER 9526 ILE D 301
TER 11947 ILE E 301
TER 14302 ILE F 301
TER 16592 GLY G 300
MASTER 665 0 38 86 95 0 64 618261 7 430 168
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