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HEADER HYDROLASE 16-MAY-17 5VTA
TITLE CO-CRYSTAL STRUCTURE OF DPPIV WITH A CHEMIBODY INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 37-767;
COMPND 5 SYNONYM: BILE CANALICULUS DOMAIN-SPECIFIC MEMBRANE GLYCOPROTEIN,
COMPND 6 DIPEPTIDYL PEPTIDASE IV,DPP IV,GP110 GLYCOPROTEIN,T-CELL ACTIVATION
COMPND 7 ANTIGEN CD26;
COMPND 8 EC: 3.4.14.5;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: FAB LIGHT CHAIN;
COMPND 12 CHAIN: L, E, G, J;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: FAB HEAVY CHAIN;
COMPND 16 CHAIN: H, F, I, K;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: DPP4, CD26;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 18 ORGANISM_COMMON: MOUSE;
SOURCE 19 ORGANISM_TAXID: 10090;
SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS HYDROLASE, CHEMIBODY
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WANG,S.JOHNSTONE,A.CHENG
REVDAT 1 09-MAY-18 5VTA 0
JRNL AUTH A.CHENG,E.DOHERTY,S.JOHNSTONE,E.DIMAURO,J.DAO,A.LUTHRA,J.YE,
JRNL AUTH 2 J.TANG,T.NIXEY,X.MIN,P.TAGARI,L.MIRANDA,Z.WANG
JRNL TITL STRUCTURED-GUIDED DESIGN OF ANTIBODY-SMALL MOLECULE HYBRIDS
JRNL TITL 2 AS BIVALENT DPP-IV INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 130806
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6869
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7861
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.3770
REMARK 3 BIN FREE R VALUE SET COUNT : 422
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 33201
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 549
REMARK 3 SOLVENT ATOMS : 118
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.38000
REMARK 3 B22 (A**2) : -0.62000
REMARK 3 B33 (A**2) : -3.11000
REMARK 3 B12 (A**2) : -0.58000
REMARK 3 B13 (A**2) : -1.09000
REMARK 3 B23 (A**2) : 0.43000
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): 0.453
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.440
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.751
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.886
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.824
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 34712 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 31496 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 47153 ; 1.573 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 72714 ; 1.007 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4143 ; 6.428 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1569 ;34.848 ;24.207
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5536 ;20.106 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 135 ;18.200 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5091 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 38950 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 8235 ; 0.002 ; 0.020
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5VTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000227966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.5.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138383
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.13300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.79400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 1000, SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L, H
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 SER A 37
REMARK 465 ARG A 38
REMARK 465 ARG A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 HIS A 773
REMARK 465 HIS A 774
REMARK 465 HIS A 775
REMARK 465 SER B 37
REMARK 465 ARG B 38
REMARK 465 ASP B 329
REMARK 465 LYS B 330
REMARK 465 THR B 331
REMARK 465 THR B 332
REMARK 465 LEU B 333
REMARK 465 ARG B 389
REMARK 465 LYS B 390
REMARK 465 PRO B 391
REMARK 465 GLU B 392
REMARK 465 GLN B 393
REMARK 465 ARG B 767
REMARK 465 HIS B 768
REMARK 465 HIS B 769
REMARK 465 HIS B 770
REMARK 465 HIS B 771
REMARK 465 HIS B 772
REMARK 465 HIS B 773
REMARK 465 HIS B 774
REMARK 465 HIS B 775
REMARK 465 SER C 37
REMARK 465 ARG C 38
REMARK 465 ARG C 767
REMARK 465 HIS C 768
REMARK 465 HIS C 769
REMARK 465 HIS C 770
REMARK 465 HIS C 771
REMARK 465 HIS C 772
REMARK 465 HIS C 773
REMARK 465 HIS C 774
REMARK 465 HIS C 775
REMARK 465 SER D 37
REMARK 465 ARG D 38
REMARK 465 LEU D 766
REMARK 465 ARG D 767
REMARK 465 HIS D 768
REMARK 465 HIS D 769
REMARK 465 HIS D 770
REMARK 465 HIS D 771
REMARK 465 HIS D 772
REMARK 465 HIS D 773
REMARK 465 HIS D 774
REMARK 465 HIS D 775
REMARK 465 ASN L 209
REMARK 465 ARG L 210
REMARK 465 GLY L 211
REMARK 465 GLU L 212
REMARK 465 CYS L 213
REMARK 465 ASP E 150
REMARK 465 ASN E 151
REMARK 465 ALA E 152
REMARK 465 PHE E 208
REMARK 465 ASN E 209
REMARK 465 ARG E 210
REMARK 465 GLY E 211
REMARK 465 GLU E 212
REMARK 465 CYS E 213
REMARK 465 GLY G 16
REMARK 465 GLU G 17
REMARK 465 ILE G 74
REMARK 465 SER G 75
REMARK 465 ILE G 105
REMARK 465 ASP G 106
REMARK 465 ARG G 107
REMARK 465 THR G 108
REMARK 465 VAL G 109
REMARK 465 ALA G 110
REMARK 465 ALA G 111
REMARK 465 PRO G 112
REMARK 465 SER G 113
REMARK 465 VAL G 114
REMARK 465 PHE G 115
REMARK 465 ILE G 116
REMARK 465 PHE G 117
REMARK 465 PRO G 118
REMARK 465 PRO G 119
REMARK 465 SER G 120
REMARK 465 ASP G 121
REMARK 465 GLU G 122
REMARK 465 GLN G 123
REMARK 465 LEU G 124
REMARK 465 LYS G 125
REMARK 465 SER G 126
REMARK 465 GLY G 127
REMARK 465 THR G 128
REMARK 465 ALA G 129
REMARK 465 SER G 130
REMARK 465 VAL G 131
REMARK 465 VAL G 132
REMARK 465 CYS G 133
REMARK 465 LEU G 134
REMARK 465 LEU G 135
REMARK 465 ASN G 136
REMARK 465 ASN G 137
REMARK 465 PHE G 138
REMARK 465 TYR G 139
REMARK 465 PRO G 140
REMARK 465 ARG G 141
REMARK 465 GLU G 142
REMARK 465 ALA G 143
REMARK 465 LYS G 144
REMARK 465 VAL G 145
REMARK 465 GLN G 146
REMARK 465 TRP G 147
REMARK 465 LYS G 148
REMARK 465 VAL G 149
REMARK 465 ASP G 150
REMARK 465 ASN G 151
REMARK 465 ALA G 152
REMARK 465 LEU G 153
REMARK 465 GLN G 154
REMARK 465 SER G 155
REMARK 465 GLY G 156
REMARK 465 ASN G 157
REMARK 465 SER G 158
REMARK 465 GLN G 159
REMARK 465 GLU G 160
REMARK 465 SER G 161
REMARK 465 VAL G 162
REMARK 465 THR G 163
REMARK 465 GLU G 164
REMARK 465 GLN G 165
REMARK 465 ASP G 166
REMARK 465 SER G 167
REMARK 465 LYS G 168
REMARK 465 ASP G 169
REMARK 465 SER G 170
REMARK 465 THR G 171
REMARK 465 TYR G 172
REMARK 465 SER G 173
REMARK 465 LEU G 174
REMARK 465 SER G 175
REMARK 465 SER G 176
REMARK 465 THR G 177
REMARK 465 LEU G 178
REMARK 465 THR G 179
REMARK 465 LEU G 180
REMARK 465 SER G 181
REMARK 465 LYS G 182
REMARK 465 ALA G 183
REMARK 465 ASP G 184
REMARK 465 TYR G 185
REMARK 465 GLU G 186
REMARK 465 LYS G 187
REMARK 465 HIS G 188
REMARK 465 LYS G 189
REMARK 465 VAL G 190
REMARK 465 TYR G 191
REMARK 465 ALA G 192
REMARK 465 CYS G 193
REMARK 465 GLU G 194
REMARK 465 VAL G 195
REMARK 465 THR G 196
REMARK 465 HIS G 197
REMARK 465 GLN G 198
REMARK 465 GLY G 199
REMARK 465 LEU G 200
REMARK 465 SER G 201
REMARK 465 SER G 202
REMARK 465 PRO G 203
REMARK 465 VAL G 204
REMARK 465 THR G 205
REMARK 465 LYS G 206
REMARK 465 SER G 207
REMARK 465 PHE G 208
REMARK 465 ASN G 209
REMARK 465 ARG G 210
REMARK 465 GLY G 211
REMARK 465 GLU G 212
REMARK 465 CYS G 213
REMARK 465 GLU I 1
REMARK 465 ALA I 117
REMARK 465 SER I 118
REMARK 465 THR I 119
REMARK 465 LYS I 120
REMARK 465 GLY I 121
REMARK 465 PRO I 122
REMARK 465 SER I 123
REMARK 465 VAL I 124
REMARK 465 PHE I 125
REMARK 465 PRO I 126
REMARK 465 LEU I 127
REMARK 465 ALA I 128
REMARK 465 PRO I 129
REMARK 465 SER I 130
REMARK 465 SER I 131
REMARK 465 LYS I 132
REMARK 465 SER I 133
REMARK 465 THR I 134
REMARK 465 SER I 135
REMARK 465 GLY I 136
REMARK 465 GLY I 137
REMARK 465 THR I 138
REMARK 465 ALA I 139
REMARK 465 ALA I 140
REMARK 465 LEU I 141
REMARK 465 GLY I 142
REMARK 465 CYS I 143
REMARK 465 LEU I 144
REMARK 465 VAL I 145
REMARK 465 LYS I 146
REMARK 465 ASP I 147
REMARK 465 TYR I 148
REMARK 465 PHE I 149
REMARK 465 PRO I 150
REMARK 465 GLU I 151
REMARK 465 PRO I 152
REMARK 465 VAL I 153
REMARK 465 THR I 154
REMARK 465 VAL I 155
REMARK 465 SER I 156
REMARK 465 TRP I 157
REMARK 465 ASN I 158
REMARK 465 SER I 159
REMARK 465 GLY I 160
REMARK 465 ALA I 161
REMARK 465 LEU I 162
REMARK 465 THR I 163
REMARK 465 SER I 164
REMARK 465 GLY I 165
REMARK 465 VAL I 166
REMARK 465 HIS I 167
REMARK 465 THR I 168
REMARK 465 PHE I 169
REMARK 465 PRO I 170
REMARK 465 ALA I 171
REMARK 465 VAL I 172
REMARK 465 LEU I 173
REMARK 465 GLN I 174
REMARK 465 SER I 175
REMARK 465 SER I 176
REMARK 465 GLY I 177
REMARK 465 LEU I 178
REMARK 465 TYR I 179
REMARK 465 SER I 180
REMARK 465 LEU I 181
REMARK 465 SER I 182
REMARK 465 SER I 183
REMARK 465 VAL I 184
REMARK 465 VAL I 185
REMARK 465 THR I 186
REMARK 465 VAL I 187
REMARK 465 PRO I 188
REMARK 465 SER I 189
REMARK 465 SER I 190
REMARK 465 SER I 191
REMARK 465 LEU I 192
REMARK 465 GLY I 193
REMARK 465 THR I 194
REMARK 465 GLN I 195
REMARK 465 THR I 196
REMARK 465 TYR I 197
REMARK 465 ILE I 198
REMARK 465 CYS I 199
REMARK 465 ASN I 200
REMARK 465 VAL I 201
REMARK 465 ASN I 202
REMARK 465 HIS I 203
REMARK 465 LYS I 204
REMARK 465 PRO I 205
REMARK 465 SER I 206
REMARK 465 ASN I 207
REMARK 465 THR I 208
REMARK 465 LYS I 209
REMARK 465 VAL I 210
REMARK 465 ASP I 211
REMARK 465 LYS I 212
REMARK 465 LYS I 213
REMARK 465 VAL I 214
REMARK 465 GLU I 215
REMARK 465 PRO I 216
REMARK 465 LYS I 217
REMARK 465 LEU J 10A
REMARK 465 SER J 10B
REMARK 465 ALA J 10C
REMARK 465 SER J 10D
REMARK 465 PRO J 10E
REMARK 465 GLY J 10F
REMARK 465 GLU J 10G
REMARK 465 GLU J 79
REMARK 465 ASP J 80
REMARK 465 ALA J 81
REMARK 465 ALA J 82
REMARK 465 THR J 100
REMARK 465 LYS J 101
REMARK 465 LEU J 102
REMARK 465 GLU J 103
REMARK 465 ILE J 104
REMARK 465 ASP J 105
REMARK 465 ARG J 106
REMARK 465 THR J 107
REMARK 465 VAL J 108
REMARK 465 ALA J 109
REMARK 465 ALA J 110
REMARK 465 PRO J 111
REMARK 465 SER J 112
REMARK 465 VAL J 113
REMARK 465 PHE J 114
REMARK 465 ILE J 115
REMARK 465 PHE J 116
REMARK 465 PRO J 117
REMARK 465 PRO J 118
REMARK 465 SER J 119
REMARK 465 ASP J 120
REMARK 465 GLU J 121
REMARK 465 GLN J 122
REMARK 465 LEU J 123
REMARK 465 LYS J 124
REMARK 465 SER J 125
REMARK 465 GLY J 126
REMARK 465 THR J 127
REMARK 465 ALA J 128
REMARK 465 SER J 129
REMARK 465 VAL J 130
REMARK 465 VAL J 131
REMARK 465 CYS J 132
REMARK 465 LEU J 133
REMARK 465 LEU J 134
REMARK 465 ASN J 135
REMARK 465 ASN J 136
REMARK 465 PHE J 137
REMARK 465 TYR J 138
REMARK 465 PRO J 139
REMARK 465 ARG J 140
REMARK 465 GLU J 141
REMARK 465 ALA J 142
REMARK 465 LYS J 143
REMARK 465 VAL J 144
REMARK 465 GLN J 145
REMARK 465 TRP J 146
REMARK 465 LYS J 147
REMARK 465 VAL J 148
REMARK 465 ASP J 149
REMARK 465 ASN J 150
REMARK 465 ALA J 151
REMARK 465 LEU J 152
REMARK 465 GLN J 153
REMARK 465 SER J 154
REMARK 465 GLY J 155
REMARK 465 ASN J 156
REMARK 465 SER J 157
REMARK 465 GLN J 158
REMARK 465 GLU J 159
REMARK 465 SER J 160
REMARK 465 VAL J 161
REMARK 465 THR J 162
REMARK 465 GLU J 163
REMARK 465 GLN J 164
REMARK 465 ASP J 165
REMARK 465 SER J 166
REMARK 465 LYS J 167
REMARK 465 ASP J 168
REMARK 465 SER J 169
REMARK 465 THR J 170
REMARK 465 TYR J 171
REMARK 465 SER J 172
REMARK 465 LEU J 173
REMARK 465 SER J 174
REMARK 465 SER J 175
REMARK 465 THR J 176
REMARK 465 LEU J 177
REMARK 465 THR J 178
REMARK 465 LEU J 179
REMARK 465 SER J 180
REMARK 465 LYS J 181
REMARK 465 ALA J 182
REMARK 465 ASP J 183
REMARK 465 TYR J 184
REMARK 465 GLU J 185
REMARK 465 LYS J 186
REMARK 465 HIS J 187
REMARK 465 LYS J 188
REMARK 465 VAL J 189
REMARK 465 TYR J 190
REMARK 465 ALA J 191
REMARK 465 CYS J 192
REMARK 465 GLU J 193
REMARK 465 VAL J 194
REMARK 465 THR J 195
REMARK 465 HIS J 196
REMARK 465 GLN J 197
REMARK 465 GLY J 198
REMARK 465 LEU J 199
REMARK 465 SER J 200
REMARK 465 SER J 201
REMARK 465 PRO J 202
REMARK 465 VAL J 203
REMARK 465 THR J 204
REMARK 465 LYS J 205
REMARK 465 SER J 206
REMARK 465 PHE J 207
REMARK 465 ASN J 208
REMARK 465 ARG J 209
REMARK 465 GLY J 210
REMARK 465 GLU J 211
REMARK 465 CYS J 212
REMARK 465 GLU K 1
REMARK 465 ASP K 31
REMARK 465 TYR K 32
REMARK 465 VAL K 114
REMARK 465 SER K 115
REMARK 465 SER K 116
REMARK 465 ALA K 117
REMARK 465 SER K 118
REMARK 465 THR K 119
REMARK 465 LYS K 120
REMARK 465 GLY K 121
REMARK 465 PRO K 122
REMARK 465 SER K 123
REMARK 465 VAL K 124
REMARK 465 PHE K 125
REMARK 465 PRO K 126
REMARK 465 LEU K 127
REMARK 465 ALA K 128
REMARK 465 PRO K 129
REMARK 465 SER K 130
REMARK 465 SER K 131
REMARK 465 LYS K 132
REMARK 465 SER K 133
REMARK 465 THR K 134
REMARK 465 SER K 135
REMARK 465 GLY K 136
REMARK 465 GLY K 137
REMARK 465 THR K 138
REMARK 465 ALA K 139
REMARK 465 ALA K 140
REMARK 465 LEU K 141
REMARK 465 GLY K 142
REMARK 465 CYS K 143
REMARK 465 LEU K 144
REMARK 465 VAL K 145
REMARK 465 LYS K 146
REMARK 465 ASP K 147
REMARK 465 TYR K 148
REMARK 465 PHE K 149
REMARK 465 PRO K 150
REMARK 465 GLU K 151
REMARK 465 PRO K 152
REMARK 465 VAL K 153
REMARK 465 THR K 154
REMARK 465 VAL K 155
REMARK 465 SER K 156
REMARK 465 TRP K 157
REMARK 465 ASN K 158
REMARK 465 SER K 159
REMARK 465 GLY K 160
REMARK 465 ALA K 161
REMARK 465 LEU K 162
REMARK 465 THR K 163
REMARK 465 SER K 164
REMARK 465 GLY K 165
REMARK 465 VAL K 166
REMARK 465 HIS K 167
REMARK 465 THR K 168
REMARK 465 PHE K 169
REMARK 465 PRO K 170
REMARK 465 ALA K 171
REMARK 465 VAL K 172
REMARK 465 LEU K 173
REMARK 465 GLN K 174
REMARK 465 SER K 175
REMARK 465 SER K 176
REMARK 465 GLY K 177
REMARK 465 LEU K 178
REMARK 465 TYR K 179
REMARK 465 SER K 180
REMARK 465 LEU K 181
REMARK 465 SER K 182
REMARK 465 SER K 183
REMARK 465 VAL K 184
REMARK 465 VAL K 185
REMARK 465 THR K 186
REMARK 465 VAL K 187
REMARK 465 PRO K 188
REMARK 465 SER K 189
REMARK 465 SER K 190
REMARK 465 SER K 191
REMARK 465 LEU K 192
REMARK 465 GLY K 193
REMARK 465 THR K 194
REMARK 465 GLN K 195
REMARK 465 THR K 196
REMARK 465 TYR K 197
REMARK 465 ILE K 198
REMARK 465 CYS K 199
REMARK 465 ASN K 200
REMARK 465 VAL K 201
REMARK 465 ASN K 202
REMARK 465 HIS K 203
REMARK 465 LYS K 204
REMARK 465 PRO K 205
REMARK 465 SER K 206
REMARK 465 ASN K 207
REMARK 465 THR K 208
REMARK 465 LYS K 209
REMARK 465 VAL K 210
REMARK 465 ASP K 211
REMARK 465 LYS K 212
REMARK 465 LYS K 213
REMARK 465 VAL K 214
REMARK 465 GLU K 215
REMARK 465 PRO K 216
REMARK 465 LYS K 217
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 ALA A 466 OG SER A 486 2.16
REMARK 500 ND2 ASN B 83 O5 NAG B 801 2.19
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 CYS B 473 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 685 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 CYS D 383 CA - CB - SG ANGL. DEV. = 8.2 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 TYR A 41 105.25 -58.57
REMARK 500 HIS A 81 -155.64 -100.37
REMARK 500 GLN A 121 -94.55 -116.72
REMARK 500 TRP A 122 -153.74 -104.23
REMARK 500 GLU A 144 72.74 46.17
REMARK 500 TRP A 152 117.71 -162.39
REMARK 500 HIS A 160 25.32 -142.73
REMARK 500 LYS A 167 51.86 39.22
REMARK 500 VAL A 191 -52.80 -126.72
REMARK 500 SER A 240 -142.57 63.63
REMARK 500 THR A 438 -76.89 -64.04
REMARK 500 GLU A 496 117.36 -162.87
REMARK 500 ARG A 598 55.60 -148.99
REMARK 500 THR A 601 -86.69 -123.27
REMARK 500 SER A 631 -119.29 60.83
REMARK 500 ALA A 708 44.35 -107.84
REMARK 500 ASN A 711 -72.39 -92.81
REMARK 500 ASP A 740 -150.13 -90.96
REMARK 500 SER B 55 -169.26 -101.03
REMARK 500 GLN B 121 -94.06 -111.19
REMARK 500 TRP B 122 -151.71 -101.57
REMARK 500 LYS B 167 51.17 37.95
REMARK 500 VAL B 191 -63.35 -126.88
REMARK 500 ILE B 205 -80.02 -120.23
REMARK 500 SER B 240 -165.17 69.53
REMARK 500 ASP B 414 24.56 -144.07
REMARK 500 GLU B 496 95.46 -160.29
REMARK 500 ALA B 549 18.61 52.39
REMARK 500 CYS B 552 32.36 76.24
REMARK 500 LYS B 597 4.53 56.79
REMARK 500 THR B 601 -78.32 -131.83
REMARK 500 SER B 631 -120.95 55.05
REMARK 500 SER B 645 -37.62 -39.82
REMARK 500 ASN B 711 -76.88 -86.37
REMARK 500 GLN B 715 -39.60 -37.67
REMARK 500 TRP C 60 98.10 -66.17
REMARK 500 HIS C 81 -154.91 -119.18
REMARK 500 ARG C 109 30.39 70.01
REMARK 500 GLN C 121 -90.20 -116.61
REMARK 500 TRP C 122 -156.39 -108.67
REMARK 500 ASN C 149 72.75 -103.53
REMARK 500 VAL C 191 -67.25 -130.69
REMARK 500 ILE C 205 -59.97 -129.44
REMARK 500 ALA C 208 145.77 -170.58
REMARK 500 SER C 240 -160.48 57.73
REMARK 500 GLN C 318 47.12 -85.06
REMARK 500 ALA C 402 58.11 -91.82
REMARK 500 ASP C 414 18.65 -144.26
REMARK 500 ASN C 451 79.21 -161.62
REMARK 500 TYR C 548 -65.13 -107.26
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 9K4 A 813
REMARK 610 9K4 C 812
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9K4 A 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9K4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9K4 C 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9K4 D 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound
REMARK 800 to ASN A 83
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 803 bound
REMARK 800 to ASN A 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 804 bound
REMARK 800 to ASN A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 805 bound
REMARK 800 to ASN A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 801 bound
REMARK 800 to ASN B 83
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 802 bound
REMARK 800 to ASN B 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 803 bound
REMARK 800 to ASN B 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 804 bound
REMARK 800 to ASN B 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 801 bound
REMARK 800 to ASN C 83
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 802 bound
REMARK 800 to ASN C 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 803 bound
REMARK 800 to ASN C 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 804 bound
REMARK 800 to ASN C 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 805 bound
REMARK 800 to ASN C 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 806 bound
REMARK 800 to ASN C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 805 bound
REMARK 800 to ASN D 83
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 801 bound
REMARK 800 to ASN D 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 802 bound
REMARK 800 to ASN D 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 806 bound
REMARK 800 to ASN D 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 803 bound
REMARK 800 to ASN D 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 804 bound
REMARK 800 to ASN D 521
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FFV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP4, DPP-IV, CD26)
REMARK 900 IN COMPLEX WITH 11A19 FAB
REMARK 900 RELATED ID: 4FFW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP4, DPP-IV, CD26)
REMARK 900 IN COMPLEX WITH FAB + SITAGLIPTIN
DBREF 5VTA A 37 767 UNP P14740 DPP4_RAT 37 767
DBREF 5VTA B 37 767 UNP P14740 DPP4_RAT 37 767
DBREF 5VTA C 37 767 UNP P14740 DPP4_RAT 37 767
DBREF 5VTA D 37 767 UNP P14740 DPP4_RAT 37 767
DBREF 5VTA L 1 213 PDB 5VTA 5VTA 1 213
DBREF 5VTA E 1 213 PDB 5VTA 5VTA 1 213
DBREF 5VTA H 1 217 PDB 5VTA 5VTA 1 217
DBREF 5VTA F 1 217 PDB 5VTA 5VTA 1 217
DBREF 5VTA G 1 213 PDB 5VTA 5VTA 1 213
DBREF 5VTA I 1 217 PDB 5VTA 5VTA 1 217
DBREF 5VTA J 1 212 PDB 5VTA 5VTA 1 212
DBREF 5VTA K 1 217 PDB 5VTA 5VTA 1 217
SEQADV 5VTA HIS A 768 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 769 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 770 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 771 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 772 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 773 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 774 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS A 775 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 768 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 769 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 770 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 771 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 772 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 773 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 774 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS B 775 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 768 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 769 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 770 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 771 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 772 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 773 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 774 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS C 775 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 768 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 769 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 770 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 771 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 772 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 773 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 774 UNP P14740 EXPRESSION TAG
SEQADV 5VTA HIS D 775 UNP P14740 EXPRESSION TAG
SEQRES 1 A 739 SER ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN
SEQRES 2 A 739 THR PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER
SEQRES 3 A 739 ASP SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 739 LEU PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU
SEQRES 5 A 739 GLU ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER
SEQRES 6 A 739 ASP TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU
SEQRES 7 A 739 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 739 ALA SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 739 ILE THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 A 739 THR TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 739 LYS ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO
SEQRES 12 A 739 SER HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE
SEQRES 13 A 739 PHE ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 A 739 PHE GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 739 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL
SEQRES 16 A 739 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 739 GLN TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA
SEQRES 18 A 739 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN
SEQRES 19 A 739 THR ASP SER LEU SER SER THR THR THR THR ILE PRO MET
SEQRES 20 A 739 GLN ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS
SEQRES 21 A 739 TYR LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE
SEQRES 22 A 739 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 739 MET ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP
SEQRES 24 A 739 ASN CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA
SEQRES 25 A 739 THR GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 A 739 PHE THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER
SEQRES 27 A 739 ASP LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS
SEQRES 28 A 739 ASP ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS
SEQRES 29 A 739 GLY ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER
SEQRES 30 A 739 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET
SEQRES 31 A 739 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP
SEQRES 32 A 739 HIS THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO
SEQRES 33 A 739 GLU ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU
SEQRES 34 A 739 ALA LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU
SEQRES 35 A 739 PRO LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU
SEQRES 36 A 739 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 A 739 LEU GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 A 739 ILE VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE
SEQRES 39 A 739 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 A 739 LEU ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 A 739 ASP ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 A 739 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 A 739 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 A 739 ASN LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE
SEQRES 45 A 739 GLU ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP
SEQRES 46 A 739 SER LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 A 739 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 A 739 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 A 739 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 A 739 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 A 739 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 A 739 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 A 739 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 A 739 ASP ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 A 739 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 A 739 ILE TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE
SEQRES 57 A 739 SER LEU ARG HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 739 SER ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN
SEQRES 2 B 739 THR PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER
SEQRES 3 B 739 ASP SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 739 LEU PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU
SEQRES 5 B 739 GLU ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER
SEQRES 6 B 739 ASP TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU
SEQRES 7 B 739 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 739 ALA SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 739 ILE THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 B 739 THR TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 739 LYS ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO
SEQRES 12 B 739 SER HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE
SEQRES 13 B 739 PHE ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 B 739 PHE GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 739 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL
SEQRES 16 B 739 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 739 GLN TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA
SEQRES 18 B 739 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN
SEQRES 19 B 739 THR ASP SER LEU SER SER THR THR THR THR ILE PRO MET
SEQRES 20 B 739 GLN ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS
SEQRES 21 B 739 TYR LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE
SEQRES 22 B 739 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 739 MET ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP
SEQRES 24 B 739 ASN CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA
SEQRES 25 B 739 THR GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 B 739 PHE THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER
SEQRES 27 B 739 ASP LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS
SEQRES 28 B 739 ASP ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS
SEQRES 29 B 739 GLY ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER
SEQRES 30 B 739 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET
SEQRES 31 B 739 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP
SEQRES 32 B 739 HIS THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO
SEQRES 33 B 739 GLU ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU
SEQRES 34 B 739 ALA LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU
SEQRES 35 B 739 PRO LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU
SEQRES 36 B 739 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 B 739 LEU GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 B 739 ILE VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE
SEQRES 39 B 739 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 B 739 LEU ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 B 739 ASP ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 B 739 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 B 739 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 B 739 ASN LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE
SEQRES 45 B 739 GLU ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP
SEQRES 46 B 739 SER LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 B 739 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 B 739 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 B 739 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 B 739 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 B 739 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 B 739 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 B 739 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 B 739 ASP ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 B 739 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 B 739 ILE TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE
SEQRES 57 B 739 SER LEU ARG HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 739 SER ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN
SEQRES 2 C 739 THR PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER
SEQRES 3 C 739 ASP SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 739 LEU PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU
SEQRES 5 C 739 GLU ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER
SEQRES 6 C 739 ASP TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU
SEQRES 7 C 739 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 739 ALA SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 739 ILE THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 C 739 THR TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 739 LYS ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO
SEQRES 12 C 739 SER HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE
SEQRES 13 C 739 PHE ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 C 739 PHE GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 739 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL
SEQRES 16 C 739 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 739 GLN TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA
SEQRES 18 C 739 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN
SEQRES 19 C 739 THR ASP SER LEU SER SER THR THR THR THR ILE PRO MET
SEQRES 20 C 739 GLN ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS
SEQRES 21 C 739 TYR LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE
SEQRES 22 C 739 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 C 739 MET ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP
SEQRES 24 C 739 ASN CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA
SEQRES 25 C 739 THR GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 C 739 PHE THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER
SEQRES 27 C 739 ASP LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS
SEQRES 28 C 739 ASP ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS
SEQRES 29 C 739 GLY ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER
SEQRES 30 C 739 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET
SEQRES 31 C 739 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP
SEQRES 32 C 739 HIS THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO
SEQRES 33 C 739 GLU ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU
SEQRES 34 C 739 ALA LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU
SEQRES 35 C 739 PRO LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU
SEQRES 36 C 739 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 C 739 LEU GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 C 739 ILE VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE
SEQRES 39 C 739 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 C 739 LEU ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 C 739 ASP ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 C 739 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 C 739 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 C 739 ASN LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE
SEQRES 45 C 739 GLU ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP
SEQRES 46 C 739 SER LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 C 739 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 C 739 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 C 739 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 C 739 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 C 739 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 C 739 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 C 739 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 C 739 ASP ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 C 739 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 C 739 ILE TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE
SEQRES 57 C 739 SER LEU ARG HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 739 SER ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN
SEQRES 2 D 739 THR PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER
SEQRES 3 D 739 ASP SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 739 LEU PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU
SEQRES 5 D 739 GLU ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER
SEQRES 6 D 739 ASP TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU
SEQRES 7 D 739 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 D 739 ALA SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 D 739 ILE THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 D 739 THR TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 D 739 LYS ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO
SEQRES 12 D 739 SER HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE
SEQRES 13 D 739 PHE ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 D 739 PHE GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 D 739 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL
SEQRES 16 D 739 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 D 739 GLN TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA
SEQRES 18 D 739 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN
SEQRES 19 D 739 THR ASP SER LEU SER SER THR THR THR THR ILE PRO MET
SEQRES 20 D 739 GLN ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS
SEQRES 21 D 739 TYR LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE
SEQRES 22 D 739 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 D 739 MET ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP
SEQRES 24 D 739 ASN CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA
SEQRES 25 D 739 THR GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 D 739 PHE THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER
SEQRES 27 D 739 ASP LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS
SEQRES 28 D 739 ASP ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS
SEQRES 29 D 739 GLY ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER
SEQRES 30 D 739 ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET
SEQRES 31 D 739 PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP
SEQRES 32 D 739 HIS THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO
SEQRES 33 D 739 GLU ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU
SEQRES 34 D 739 ALA LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU
SEQRES 35 D 739 PRO LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU
SEQRES 36 D 739 LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET
SEQRES 37 D 739 LEU GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE
SEQRES 38 D 739 ILE VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE
SEQRES 39 D 739 LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU
SEQRES 40 D 739 LEU ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA
SEQRES 41 D 739 ASP ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA
SEQRES 42 D 739 SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG
SEQRES 43 D 739 GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE
SEQRES 44 D 739 ASN LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE
SEQRES 45 D 739 GLU ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP
SEQRES 46 D 739 SER LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY
SEQRES 47 D 739 TYR VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL
SEQRES 48 D 739 PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP
SEQRES 49 D 739 GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY
SEQRES 50 D 739 LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN
SEQRES 51 D 739 SER THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL
SEQRES 52 D 739 GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL
SEQRES 53 D 739 HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL
SEQRES 54 D 739 ASP ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP
SEQRES 55 D 739 GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS
SEQRES 56 D 739 ILE TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE
SEQRES 57 D 739 SER LEU ARG HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 L 213 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA
SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER
SEQRES 3 L 213 SER SER VAL CYS ASN MET HIS TRP TYR GLN GLN LYS PRO
SEQRES 4 L 213 GLY SER SER PRO LYS PRO TRP LEU HIS GLY THR SER ASN
SEQRES 5 L 213 LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 L 213 SER GLY THR SER PHE SER LEU THR ILE SER ARG VAL GLU
SEQRES 7 L 213 ALA GLU ASP ALA ALA THR TYR PHE CYS GLN GLN TRP SER
SEQRES 8 L 213 ASN HIS PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 L 213 ILE ASP ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE
SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER
SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA
SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY
SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP
SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS
SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL
SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE
SEQRES 17 L 213 ASN ARG GLY GLU CYS
SEQRES 1 E 213 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA
SEQRES 2 E 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER
SEQRES 3 E 213 SER SER VAL CYS ASN MET HIS TRP TYR GLN GLN LYS PRO
SEQRES 4 E 213 GLY SER SER PRO LYS PRO TRP LEU HIS GLY THR SER ASN
SEQRES 5 E 213 LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 E 213 SER GLY THR SER PHE SER LEU THR ILE SER ARG VAL GLU
SEQRES 7 E 213 ALA GLU ASP ALA ALA THR TYR PHE CYS GLN GLN TRP SER
SEQRES 8 E 213 ASN HIS PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 E 213 ILE ASP ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE
SEQRES 10 E 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER
SEQRES 11 E 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA
SEQRES 12 E 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY
SEQRES 13 E 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP
SEQRES 14 E 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS
SEQRES 15 E 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL
SEQRES 16 E 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE
SEQRES 17 E 213 ASN ARG GLY GLU CYS
SEQRES 1 H 217 GLU PHE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 H 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 H 217 TYR SER PHE THR ASP TYR ASN ILE ASN TRP MET LYS GLN
SEQRES 4 H 217 SER ASN GLY LYS SER LEU GLU TRP ILE GLY VAL VAL ILE
SEQRES 5 H 217 PRO LYS TYR GLY THR THR ASN TYR ASN GLN LYS PHE GLN
SEQRES 6 H 217 GLY LYS ALA THR LEU THR VAL ASP GLN SER SER SER THR
SEQRES 7 H 217 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 H 217 ALA VAL TYR TYR CYS THR ARG PHE ARG VAL PHE PHE ASP
SEQRES 9 H 217 VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER ALA
SEQRES 10 H 217 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER
SEQRES 11 H 217 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS
SEQRES 12 H 217 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER
SEQRES 13 H 217 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE
SEQRES 14 H 217 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER
SEQRES 15 H 217 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN
SEQRES 16 H 217 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR
SEQRES 17 H 217 LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 1 F 217 GLU PHE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 F 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 F 217 TYR SER PHE THR ASP TYR ASN ILE ASN TRP MET LYS GLN
SEQRES 4 F 217 SER ASN GLY LYS SER LEU GLU TRP ILE GLY VAL VAL ILE
SEQRES 5 F 217 PRO LYS TYR GLY THR THR ASN TYR ASN GLN LYS PHE GLN
SEQRES 6 F 217 GLY LYS ALA THR LEU THR VAL ASP GLN SER SER SER THR
SEQRES 7 F 217 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 F 217 ALA VAL TYR TYR CYS THR ARG PHE ARG VAL PHE PHE ASP
SEQRES 9 F 217 VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER ALA
SEQRES 10 F 217 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER
SEQRES 11 F 217 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS
SEQRES 12 F 217 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER
SEQRES 13 F 217 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE
SEQRES 14 F 217 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER
SEQRES 15 F 217 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN
SEQRES 16 F 217 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR
SEQRES 17 F 217 LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 1 G 213 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA
SEQRES 2 G 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER
SEQRES 3 G 213 SER SER VAL CYS ASN MET HIS TRP TYR GLN GLN LYS PRO
SEQRES 4 G 213 GLY SER SER PRO LYS PRO TRP LEU HIS GLY THR SER ASN
SEQRES 5 G 213 LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 G 213 SER GLY THR SER PHE SER LEU THR ILE SER ARG VAL GLU
SEQRES 7 G 213 ALA GLU ASP ALA ALA THR TYR PHE CYS GLN GLN TRP SER
SEQRES 8 G 213 ASN HIS PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 G 213 ILE ASP ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE
SEQRES 10 G 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER
SEQRES 11 G 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA
SEQRES 12 G 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY
SEQRES 13 G 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP
SEQRES 14 G 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS
SEQRES 15 G 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL
SEQRES 16 G 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE
SEQRES 17 G 213 ASN ARG GLY GLU CYS
SEQRES 1 I 217 GLU PHE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 I 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 I 217 TYR SER PHE THR ASP TYR ASN ILE ASN TRP MET LYS GLN
SEQRES 4 I 217 SER ASN GLY LYS SER LEU GLU TRP ILE GLY VAL VAL ILE
SEQRES 5 I 217 PRO LYS TYR GLY THR THR ASN TYR ASN GLN LYS PHE GLN
SEQRES 6 I 217 GLY LYS ALA THR LEU THR VAL ASP GLN SER SER SER THR
SEQRES 7 I 217 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 I 217 ALA VAL TYR TYR CYS THR ARG PHE ARG VAL PHE PHE ASP
SEQRES 9 I 217 VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER ALA
SEQRES 10 I 217 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER
SEQRES 11 I 217 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS
SEQRES 12 I 217 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER
SEQRES 13 I 217 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE
SEQRES 14 I 217 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER
SEQRES 15 I 217 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN
SEQRES 16 I 217 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR
SEQRES 17 I 217 LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 1 J 213 GLN ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA
SEQRES 2 J 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER
SEQRES 3 J 213 SER SER VAL CYS ASN MET HIS TRP TYR GLN GLN LYS PRO
SEQRES 4 J 213 GLY SER SER PRO LYS PRO TRP LEU HIS GLY THR SER ASN
SEQRES 5 J 213 LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 J 213 SER GLY THR SER PHE SER LEU THR ILE SER ARG VAL GLU
SEQRES 7 J 213 ALA GLU ASP ALA ALA THR TYR PHE CYS GLN GLN TRP SER
SEQRES 8 J 213 ASN HIS PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 J 213 ILE ASP ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE
SEQRES 10 J 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER
SEQRES 11 J 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA
SEQRES 12 J 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY
SEQRES 13 J 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP
SEQRES 14 J 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS
SEQRES 15 J 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL
SEQRES 16 J 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE
SEQRES 17 J 213 ASN ARG GLY GLU CYS
SEQRES 1 K 217 GLU PHE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 K 217 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 K 217 TYR SER PHE THR ASP TYR ASN ILE ASN TRP MET LYS GLN
SEQRES 4 K 217 SER ASN GLY LYS SER LEU GLU TRP ILE GLY VAL VAL ILE
SEQRES 5 K 217 PRO LYS TYR GLY THR THR ASN TYR ASN GLN LYS PHE GLN
SEQRES 6 K 217 GLY LYS ALA THR LEU THR VAL ASP GLN SER SER SER THR
SEQRES 7 K 217 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 K 217 ALA VAL TYR TYR CYS THR ARG PHE ARG VAL PHE PHE ASP
SEQRES 9 K 217 VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER ALA
SEQRES 10 K 217 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER
SEQRES 11 K 217 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS
SEQRES 12 K 217 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER
SEQRES 13 K 217 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE
SEQRES 14 K 217 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER
SEQRES 15 K 217 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN
SEQRES 16 K 217 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR
SEQRES 17 K 217 LYS VAL ASP LYS LYS VAL GLU PRO LYS
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET PG4 A 806 13
HET PEG A 807 7
HET PEG A 808 7
HET EDO A 809 4
HET EDO A 810 4
HET EDO A 811 4
HET EDO A 812 4
HET 9K4 A 813 43
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET EDO B 805 4
HET 9K4 B 806 49
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HET NAG C 805 14
HET NAG C 806 14
HET EDO C 807 4
HET EDO C 808 4
HET EDO C 809 4
HET EDO C 810 4
HET EDO C 811 4
HET 9K4 C 812 40
HET NAG D 801 14
HET NAG D 802 14
HET NAG D 803 14
HET NAG D 804 14
HET NAG D 805 14
HET NAG D 806 14
HET PEG D 807 7
HET 9K4 D 808 49
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 9K4 2-{4-[(3R)-3-AMINO-4-(2,4,5-TRIFLUOROPHENYL)
HETNAM 2 9K4 BUTANOYL]PIPERAZIN-1-YL}-N-(22-OXO-3,6,9,12,15,18-
HETNAM 3 9K4 HEXAOXA-21-AZATRICOSAN-1-YL)ACETAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 13 NAG 21(C8 H15 N O6)
FORMUL 18 PG4 C8 H18 O5
FORMUL 19 PEG 3(C4 H10 O3)
FORMUL 21 EDO 10(C2 H6 O2)
FORMUL 25 9K4 4(C32 H52 F3 N5 O9)
FORMUL 52 HOH *118(H2 O)
HELIX 1 AA1 THR A 42 ASN A 49 1 8
HELIX 2 AA2 GLU A 89 ILE A 95 1 7
HELIX 3 AA3 ASP A 198 ILE A 205 1 8
HELIX 4 AA4 PRO A 288 THR A 293 1 6
HELIX 5 AA5 GLU A 422 MET A 426 5 5
HELIX 6 AA6 ASN A 498 GLN A 506 1 9
HELIX 7 AA7 ASN A 563 THR A 571 1 9
HELIX 8 AA8 GLY A 588 HIS A 593 1 6
HELIX 9 AA9 ALA A 594 ASN A 596 5 3
HELIX 10 AB1 THR A 601 MET A 617 1 17
HELIX 11 AB2 SER A 631 GLY A 642 1 12
HELIX 12 AB3 ASP A 664 GLY A 673 1 10
HELIX 13 AB4 ASN A 680 SER A 687 1 8
HELIX 14 AB5 VAL A 689 VAL A 699 5 11
HELIX 15 AB6 PHE A 714 ALA A 727 1 14
HELIX 16 AB7 SER A 745 PHE A 764 1 20
HELIX 17 AB8 THR B 42 LYS B 48 1 7
HELIX 18 AB9 GLU B 89 ILE B 95 1 7
HELIX 19 AC1 ASP B 198 ILE B 205 1 8
HELIX 20 AC2 PRO B 288 THR B 293 1 6
HELIX 21 AC3 PRO B 338 THR B 340 5 3
HELIX 22 AC4 GLU B 422 MET B 426 5 5
HELIX 23 AC5 ASN B 498 VAL B 508 1 11
HELIX 24 AC6 ASN B 563 ASN B 573 1 11
HELIX 25 AC7 GLY B 588 HIS B 593 1 6
HELIX 26 AC8 THR B 601 MET B 617 1 17
HELIX 27 AC9 SER B 631 GLY B 642 1 12
HELIX 28 AD1 ARG B 659 TYR B 663 5 5
HELIX 29 AD2 ASP B 664 GLY B 673 1 10
HELIX 30 AD3 ASN B 680 ASN B 686 1 7
HELIX 31 AD4 VAL B 689 VAL B 699 5 11
HELIX 32 AD5 HIS B 713 GLY B 728 1 16
HELIX 33 AD6 SER B 745 PHE B 764 1 20
HELIX 34 AD7 THR C 42 LYS C 48 1 7
HELIX 35 AD8 ASN C 90 ILE C 95 1 6
HELIX 36 AD9 ASP C 198 ILE C 205 1 8
HELIX 37 AE1 PRO C 338 THR C 340 5 3
HELIX 38 AE2 GLU C 422 MET C 426 5 5
HELIX 39 AE3 ASN C 498 LEU C 505 1 8
HELIX 40 AE4 GLN C 506 VAL C 508 5 3
HELIX 41 AE5 ASN C 563 THR C 571 1 9
HELIX 42 AE6 GLY C 588 HIS C 593 1 6
HELIX 43 AE7 THR C 601 GLY C 618 1 18
HELIX 44 AE8 SER C 631 GLY C 642 1 12
HELIX 45 AE9 ARG C 659 TYR C 663 5 5
HELIX 46 AF1 ASP C 664 GLY C 673 1 10
HELIX 47 AF2 ASN C 680 SER C 687 1 8
HELIX 48 AF3 VAL C 689 GLN C 698 5 10
HELIX 49 AF4 PHE C 714 ALA C 727 1 14
HELIX 50 AF5 SER C 745 PHE C 764 1 20
HELIX 51 AF6 THR D 42 LYS D 48 1 7
HELIX 52 AF7 GLU D 89 ILE D 95 1 7
HELIX 53 AF8 ASP D 198 ILE D 205 1 8
HELIX 54 AF9 ASP D 272 LEU D 274 5 3
HELIX 55 AG1 PRO D 288 THR D 293 1 6
HELIX 56 AG2 PRO D 338 THR D 340 5 3
HELIX 57 AG3 GLU D 422 MET D 426 5 5
HELIX 58 AG4 ASN D 498 GLN D 506 1 9
HELIX 59 AG5 ASN D 563 THR D 571 1 9
HELIX 60 AG6 GLY D 588 HIS D 593 1 6
HELIX 61 AG7 THR D 601 LYS D 616 1 16
HELIX 62 AG8 SER D 631 SER D 643 1 13
HELIX 63 AG9 ARG D 659 TYR D 663 5 5
HELIX 64 AH1 ASP D 664 GLY D 673 1 10
HELIX 65 AH2 ASN D 680 SER D 687 1 8
HELIX 66 AH3 VAL D 689 LYS D 697 5 9
HELIX 67 AH4 PHE D 714 ALA D 727 1 14
HELIX 68 AH5 SER D 745 SER D 765 1 21
HELIX 69 AH6 GLU L 78 ALA L 82 5 5
HELIX 70 AH7 SER L 120 SER L 126 1 7
HELIX 71 AH8 LYS L 182 GLU L 186 1 5
HELIX 72 AH9 GLU E 78 ALA E 82 5 5
HELIX 73 AI1 SER E 120 GLY E 127 1 8
HELIX 74 AI2 LYS E 182 HIS E 188 1 7
HELIX 75 AI3 SER H 28 TYR H 32 5 5
HELIX 76 AI4 GLN H 74 SER H 76 5 3
HELIX 77 AI5 THR H 87 SER H 91 5 5
HELIX 78 AI6 SER H 130 LYS H 132 5 3
HELIX 79 AI7 SER H 159 ALA H 161 5 3
HELIX 80 AI8 SER F 28 TYR F 32 5 5
HELIX 81 AI9 THR F 87 SER F 91 5 5
HELIX 82 AJ1 SER F 130 LYS F 132 5 3
HELIX 83 AJ2 SER F 159 ALA F 161 5 3
HELIX 84 AJ3 LYS F 204 ASN F 207 5 4
HELIX 85 AJ4 GLU G 78 ALA G 82 5 5
HELIX 86 AJ5 SER I 28 TYR I 32 5 5
HELIX 87 AJ6 GLN I 62 GLN I 65 5 4
SHEET 1 AA1 4 LEU A 58 TRP A 60 0
SHEET 2 AA1 4 GLU A 65 GLN A 70 -1 O LEU A 67 N ARG A 59
SHEET 3 AA1 4 ASN A 73 ASN A 78 -1 O ASN A 73 N GLN A 70
SHEET 4 AA1 4 SER A 84 LEU A 88 -1 O LEU A 88 N ILE A 74
SHEET 1 AA2 4 ILE A 100 VAL A 105 0
SHEET 2 AA2 4 PHE A 111 LYS A 120 -1 O GLU A 115 N ASP A 102
SHEET 3 AA2 4 TYR A 126 ASP A 134 -1 O TYR A 133 N VAL A 112
SHEET 4 AA2 4 GLN A 139 LEU A 140 -1 O GLN A 139 N ASP A 134
SHEET 1 AA3 4 TRP A 152 TRP A 155 0
SHEET 2 AA3 4 LEU A 162 TRP A 166 -1 O ALA A 163 N THR A 154
SHEET 3 AA3 4 ASP A 169 LYS A 173 -1 O TYR A 171 N TYR A 164
SHEET 4 AA3 4 HIS A 181 ARG A 182 -1 O HIS A 181 N VAL A 172
SHEET 1 AA4 3 ILE A 192 ASN A 194 0
SHEET 2 AA4 3 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 AA4 3 LEU A 212 TRP A 214 -1 N TRP A 213 O ALA A 222
SHEET 1 AA5 4 ILE A 192 ASN A 194 0
SHEET 2 AA5 4 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 AA5 4 THR A 263 ASN A 270 -1 O LYS A 265 N GLN A 225
SHEET 4 AA5 4 MET A 283 ILE A 285 -1 O MET A 283 N ILE A 268
SHEET 1 AA6 2 LEU A 233 PHE A 238 0
SHEET 2 AA6 2 LYS A 248 PRO A 253 -1 O VAL A 250 N TYR A 236
SHEET 1 AA7 4 HIS A 296 SER A 305 0
SHEET 2 AA7 4 ARG A 308 ARG A 315 -1 O LEU A 314 N TYR A 297
SHEET 3 AA7 4 TYR A 320 ASP A 329 -1 O CYS A 326 N ILE A 309
SHEET 4 AA7 4 VAL A 334 ASN A 336 -1 O ASN A 336 N ASP A 327
SHEET 1 AA8 4 HIS A 296 SER A 305 0
SHEET 2 AA8 4 ARG A 308 ARG A 315 -1 O LEU A 314 N TYR A 297
SHEET 3 AA8 4 TYR A 320 ASP A 329 -1 O CYS A 326 N ILE A 309
SHEET 4 AA8 4 GLU A 342 THR A 346 -1 O HIS A 343 N MET A 323
SHEET 1 AA9 4 HIS A 361 PHE A 362 0
SHEET 2 AA9 4 SER A 368 SER A 374 -1 O TYR A 370 N HIS A 361
SHEET 3 AA9 4 LYS A 380 GLN A 386 -1 O PHE A 385 N PHE A 369
SHEET 4 AA9 4 THR A 396 PHE A 397 -1 O THR A 396 N GLN A 384
SHEET 1 AB1 4 VAL A 405 LEU A 411 0
SHEET 2 AB1 4 TYR A 415 SER A 420 -1 O TYR A 417 N GLU A 409
SHEET 3 AB1 4 ASN A 431 GLN A 436 -1 O ILE A 435 N LEU A 416
SHEET 4 AB1 4 LYS A 443 CYS A 445 -1 O LYS A 444 N LYS A 434
SHEET 1 AB2 4 CYS A 455 LEU A 462 0
SHEET 2 AB2 4 TYR A 468 PRO A 476 -1 O ARG A 474 N TYR A 457
SHEET 3 AB2 4 LEU A 480 ARG A 485 -1 O LEU A 480 N CYS A 473
SHEET 4 AB2 4 LYS A 490 GLU A 496 -1 O GLU A 496 N TYR A 481
SHEET 1 AB3 8 SER A 512 LEU A 520 0
SHEET 2 AB3 8 THR A 523 LEU A 531 -1 O PHE A 525 N ILE A 518
SHEET 3 AB3 8 ILE A 575 PHE A 579 -1 O VAL A 576 N ILE A 530
SHEET 4 AB3 8 TYR A 541 VAL A 547 1 N LEU A 544 O ILE A 575
SHEET 5 AB3 8 VAL A 620 TRP A 630 1 O ALA A 626 N LEU A 543
SHEET 6 AB3 8 CYS A 650 VAL A 654 1 O VAL A 654 N GLY A 629
SHEET 7 AB3 8 GLU A 700 GLY A 706 1 O ILE A 704 N ALA A 653
SHEET 8 AB3 8 GLN A 732 TYR A 736 1 O GLN A 732 N LEU A 703
SHEET 1 AB4 4 ARG B 59 TRP B 60 0
SHEET 2 AB4 4 GLU B 65 GLN B 70 -1 O LEU B 67 N ARG B 59
SHEET 3 AB4 4 ASN B 73 ASN B 78 -1 O LEU B 75 N TYR B 68
SHEET 4 AB4 4 SER B 84 LEU B 88 -1 O SER B 85 N LEU B 76
SHEET 1 AB5 4 ASP B 102 VAL B 105 0
SHEET 2 AB5 4 PHE B 111 LYS B 120 -1 O GLU B 115 N ASP B 102
SHEET 3 AB5 4 TYR B 126 ASP B 134 -1 O SER B 131 N LEU B 114
SHEET 4 AB5 4 GLN B 139 ILE B 141 -1 O ILE B 141 N ILE B 132
SHEET 1 AB6 3 LEU B 162 TRP B 166 0
SHEET 2 AB6 3 ASP B 169 LYS B 173 -1 O TYR B 171 N TYR B 164
SHEET 3 AB6 3 HIS B 181 ARG B 182 -1 O HIS B 181 N VAL B 172
SHEET 1 AB7 3 ILE B 192 ASN B 194 0
SHEET 2 AB7 3 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 AB7 3 LEU B 212 TRP B 214 -1 N TRP B 213 O ALA B 222
SHEET 1 AB8 4 ILE B 192 ASN B 194 0
SHEET 2 AB8 4 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 AB8 4 THR B 263 ASN B 270 -1 O LYS B 265 N GLN B 225
SHEET 4 AB8 4 MET B 283 ILE B 285 -1 O MET B 283 N ILE B 268
SHEET 1 AB9 2 LEU B 233 PHE B 238 0
SHEET 2 AB9 2 LYS B 248 PRO B 253 -1 O VAL B 250 N TYR B 236
SHEET 1 AC1 4 HIS B 296 SER B 305 0
SHEET 2 AC1 4 ARG B 308 ARG B 315 -1 O LEU B 314 N TYR B 297
SHEET 3 AC1 4 TYR B 320 ASP B 327 -1 O VAL B 322 N TRP B 313
SHEET 4 AC1 4 GLU B 342 THR B 346 -1 O GLU B 345 N SER B 321
SHEET 1 AC2 4 HIS B 361 PHE B 362 0
SHEET 2 AC2 4 SER B 368 SER B 374 -1 O TYR B 370 N HIS B 361
SHEET 3 AC2 4 LYS B 380 GLN B 386 -1 O CYS B 383 N LYS B 371
SHEET 4 AC2 4 THR B 396 PHE B 397 -1 O THR B 396 N GLN B 384
SHEET 1 AC3 4 VAL B 405 LEU B 411 0
SHEET 2 AC3 4 TYR B 415 SER B 420 -1 O TYR B 417 N ALA B 410
SHEET 3 AC3 4 ASN B 431 GLN B 436 -1 O TYR B 433 N TYR B 418
SHEET 4 AC3 4 LYS B 443 CYS B 445 -1 O LYS B 444 N LYS B 434
SHEET 1 AC4 4 CYS B 455 LEU B 462 0
SHEET 2 AC4 4 TYR B 468 PRO B 476 -1 O GLN B 470 N SER B 461
SHEET 3 AC4 4 LEU B 480 ARG B 485 -1 O LEU B 480 N CYS B 473
SHEET 4 AC4 4 LYS B 490 GLU B 496 -1 O LEU B 492 N LEU B 483
SHEET 1 AC5 8 SER B 512 LEU B 520 0
SHEET 2 AC5 8 THR B 523 LEU B 531 -1 O PHE B 525 N ILE B 518
SHEET 3 AC5 8 ILE B 575 PHE B 579 -1 O SER B 578 N GLN B 528
SHEET 4 AC5 8 TYR B 541 ASP B 546 1 N ASP B 546 O ALA B 577
SHEET 5 AC5 8 VAL B 620 TRP B 630 1 O ALA B 626 N ILE B 545
SHEET 6 AC5 8 CYS B 650 VAL B 654 1 O VAL B 654 N GLY B 629
SHEET 7 AC5 8 GLU B 700 GLY B 706 1 O LEU B 702 N GLY B 651
SHEET 8 AC5 8 GLN B 732 TYR B 736 1 O GLN B 732 N TYR B 701
SHEET 1 AC6 4 LEU C 58 ARG C 59 0
SHEET 2 AC6 4 GLU C 65 GLN C 70 -1 O LEU C 67 N ARG C 59
SHEET 3 AC6 4 ASN C 73 ASN C 78 -1 O PHE C 77 N TYR C 66
SHEET 4 AC6 4 SER C 84 LEU C 88 -1 O LEU C 88 N ILE C 74
SHEET 1 AC7 4 ILE C 100 VAL C 105 0
SHEET 2 AC7 4 PHE C 111 LYS C 120 -1 O GLU C 115 N SER C 101
SHEET 3 AC7 4 TYR C 126 ASP C 134 -1 O SER C 131 N LEU C 114
SHEET 4 AC7 4 GLN C 139 LEU C 140 -1 O GLN C 139 N ASP C 134
SHEET 1 AC8 4 THR C 150 TRP C 155 0
SHEET 2 AC8 4 LEU C 162 TRP C 166 -1 O VAL C 165 N GLN C 151
SHEET 3 AC8 4 ASP C 169 LYS C 173 -1 O TYR C 171 N TYR C 164
SHEET 4 AC8 4 HIS C 181 ARG C 182 -1 O HIS C 181 N VAL C 172
SHEET 1 AC9 3 ILE C 192 ASN C 194 0
SHEET 2 AC9 3 PHE C 220 ASN C 227 -1 O PHE C 226 N PHE C 193
SHEET 3 AC9 3 LEU C 212 TRP C 214 -1 N TRP C 213 O ALA C 222
SHEET 1 AD1 4 ILE C 192 ASN C 194 0
SHEET 2 AD1 4 PHE C 220 ASN C 227 -1 O PHE C 226 N PHE C 193
SHEET 3 AD1 4 THR C 263 ASN C 270 -1 O PHE C 267 N TYR C 223
SHEET 4 AD1 4 MET C 283 ILE C 285 -1 O ILE C 285 N PHE C 266
SHEET 1 AD2 2 LEU C 233 PHE C 238 0
SHEET 2 AD2 2 LYS C 248 PRO C 253 -1 O LYS C 248 N PHE C 238
SHEET 1 AD3 4 HIS C 296 TRP C 303 0
SHEET 2 AD3 4 ARG C 308 ARG C 315 -1 O LEU C 314 N TYR C 297
SHEET 3 AD3 4 TYR C 320 ASP C 329 -1 O VAL C 322 N TRP C 313
SHEET 4 AD3 4 VAL C 334 ASN C 336 -1 O VAL C 334 N ASP C 329
SHEET 1 AD4 4 HIS C 296 TRP C 303 0
SHEET 2 AD4 4 ARG C 308 ARG C 315 -1 O LEU C 314 N TYR C 297
SHEET 3 AD4 4 TYR C 320 ASP C 329 -1 O VAL C 322 N TRP C 313
SHEET 4 AD4 4 GLU C 342 THR C 346 -1 O GLU C 345 N SER C 321
SHEET 1 AD5 4 HIS C 361 PHE C 362 0
SHEET 2 AD5 4 SER C 368 SER C 374 -1 O TYR C 370 N HIS C 361
SHEET 3 AD5 4 LYS C 380 GLN C 386 -1 O CYS C 383 N LYS C 371
SHEET 4 AD5 4 THR C 396 PHE C 397 -1 O THR C 396 N GLN C 384
SHEET 1 AD6 4 VAL C 405 LEU C 411 0
SHEET 2 AD6 4 TYR C 415 SER C 420 -1 O ILE C 419 N ILE C 406
SHEET 3 AD6 4 ASN C 431 GLN C 436 -1 O TYR C 433 N TYR C 418
SHEET 4 AD6 4 LYS C 443 CYS C 445 -1 O LYS C 444 N LYS C 434
SHEET 1 AD7 4 CYS C 455 LEU C 462 0
SHEET 2 AD7 4 TYR C 468 PRO C 476 -1 O GLY C 475 N GLN C 456
SHEET 3 AD7 4 LEU C 480 ARG C 485 -1 O HIS C 484 N TYR C 469
SHEET 4 AD7 4 LYS C 490 GLU C 496 -1 O ARG C 493 N LEU C 483
SHEET 1 AD8 8 SER C 512 LEU C 520 0
SHEET 2 AD8 8 THR C 523 LEU C 531 -1 O MET C 529 N LYS C 514
SHEET 3 AD8 8 ILE C 575 PHE C 579 -1 O VAL C 576 N ILE C 530
SHEET 4 AD8 8 TYR C 541 ASP C 546 1 N ASP C 546 O ALA C 577
SHEET 5 AD8 8 VAL C 620 TRP C 630 1 O ALA C 626 N ILE C 545
SHEET 6 AD8 8 CYS C 650 VAL C 654 1 O VAL C 654 N GLY C 629
SHEET 7 AD8 8 GLU C 700 GLY C 706 1 O GLU C 700 N GLY C 651
SHEET 8 AD8 8 GLN C 732 TYR C 736 1 O GLN C 732 N LEU C 703
SHEET 1 AD9 2 GLU D 65 LYS D 69 0
SHEET 2 AD9 2 ILE D 74 ASN D 78 -1 O PHE D 77 N TYR D 66
SHEET 1 AE1 4 ILE D 100 VAL D 105 0
SHEET 2 AE1 4 PHE D 111 LYS D 120 -1 O GLU D 115 N SER D 101
SHEET 3 AE1 4 TYR D 126 ASP D 134 -1 O TYR D 133 N VAL D 112
SHEET 4 AE1 4 GLN D 139 LEU D 140 -1 O GLN D 139 N ASP D 134
SHEET 1 AE2 4 TRP D 152 TRP D 155 0
SHEET 2 AE2 4 LEU D 162 TRP D 166 -1 O VAL D 165 N TRP D 152
SHEET 3 AE2 4 ASP D 169 LYS D 173 -1 O TYR D 171 N TYR D 164
SHEET 4 AE2 4 HIS D 181 ARG D 182 -1 O HIS D 181 N VAL D 172
SHEET 1 AE3 3 ILE D 192 ASN D 194 0
SHEET 2 AE3 3 PHE D 220 ASN D 227 -1 O PHE D 226 N PHE D 193
SHEET 3 AE3 3 LEU D 212 TRP D 214 -1 N TRP D 213 O ALA D 222
SHEET 1 AE4 4 ILE D 192 ASN D 194 0
SHEET 2 AE4 4 PHE D 220 ASN D 227 -1 O PHE D 226 N PHE D 193
SHEET 3 AE4 4 THR D 263 ASN D 270 -1 O VAL D 269 N LEU D 221
SHEET 4 AE4 4 MET D 283 ILE D 285 -1 O MET D 283 N ILE D 268
SHEET 1 AE5 2 LEU D 233 PHE D 238 0
SHEET 2 AE5 2 LYS D 248 PRO D 253 -1 O LYS D 248 N PHE D 238
SHEET 1 AE6 4 HIS D 296 SER D 305 0
SHEET 2 AE6 4 ARG D 308 ARG D 315 -1 O LEU D 314 N TYR D 297
SHEET 3 AE6 4 TYR D 320 ASP D 329 -1 O ALA D 324 N LEU D 311
SHEET 4 AE6 4 VAL D 334 ASN D 336 -1 O ASN D 336 N ASP D 327
SHEET 1 AE7 4 HIS D 296 SER D 305 0
SHEET 2 AE7 4 ARG D 308 ARG D 315 -1 O LEU D 314 N TYR D 297
SHEET 3 AE7 4 TYR D 320 ASP D 329 -1 O ALA D 324 N LEU D 311
SHEET 4 AE7 4 GLU D 342 THR D 346 -1 O HIS D 343 N MET D 323
SHEET 1 AE8 4 HIS D 361 PHE D 362 0
SHEET 2 AE8 4 PHE D 369 SER D 374 -1 O TYR D 370 N HIS D 361
SHEET 3 AE8 4 LYS D 380 GLN D 384 -1 O CYS D 383 N LYS D 371
SHEET 4 AE8 4 THR D 396 PHE D 397 -1 O THR D 396 N GLN D 384
SHEET 1 AE9 4 VAL D 405 LEU D 411 0
SHEET 2 AE9 4 TYR D 415 SER D 420 -1 O TYR D 417 N ALA D 410
SHEET 3 AE9 4 ASN D 431 GLN D 436 -1 O TYR D 433 N TYR D 418
SHEET 4 AE9 4 LYS D 444 CYS D 445 -1 O LYS D 444 N LYS D 434
SHEET 1 AF1 4 CYS D 455 LEU D 462 0
SHEET 2 AF1 4 TYR D 468 PRO D 476 -1 O ARG D 474 N TYR D 457
SHEET 3 AF1 4 LEU D 480 ARG D 485 -1 O THR D 482 N LEU D 471
SHEET 4 AF1 4 GLU D 491 GLU D 496 -1 O GLU D 496 N TYR D 481
SHEET 1 AF2 8 SER D 512 LEU D 520 0
SHEET 2 AF2 8 THR D 523 LEU D 531 -1 O TYR D 527 N ASP D 516
SHEET 3 AF2 8 ILE D 575 PHE D 579 -1 O VAL D 576 N ILE D 530
SHEET 4 AF2 8 TYR D 541 ASP D 546 1 N LEU D 544 O ILE D 575
SHEET 5 AF2 8 VAL D 620 TRP D 630 1 O ALA D 626 N LEU D 543
SHEET 6 AF2 8 CYS D 650 VAL D 654 1 O VAL D 654 N GLY D 629
SHEET 7 AF2 8 GLU D 700 GLY D 706 1 O LEU D 702 N GLY D 651
SHEET 8 AF2 8 GLN D 732 TYR D 736 1 O GLN D 732 N TYR D 701
SHEET 1 AF3 4 LEU L 4 SER L 7 0
SHEET 2 AF3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N SER L 5
SHEET 3 AF3 4 SER L 69 ILE L 74 -1 O PHE L 70 N CYS L 23
SHEET 4 AF3 4 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73
SHEET 1 AF4 6 ILE L 10 SER L 12 0
SHEET 2 AF4 6 THR L 101 GLU L 104 1 O LYS L 102 N LEU L 11
SHEET 3 AF4 6 THR L 84 GLN L 89 -1 N TYR L 85 O THR L 101
SHEET 4 AF4 6 HIS L 33 GLN L 37 -1 N HIS L 33 O GLN L 88
SHEET 5 AF4 6 LYS L 44 HIS L 48 -1 O LYS L 44 N GLN L 36
SHEET 6 AF4 6 ASN L 52 LEU L 53 -1 O ASN L 52 N HIS L 48
SHEET 1 AF5 4 ILE L 10 SER L 12 0
SHEET 2 AF5 4 THR L 101 GLU L 104 1 O LYS L 102 N LEU L 11
SHEET 3 AF5 4 THR L 84 GLN L 89 -1 N TYR L 85 O THR L 101
SHEET 4 AF5 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 89
SHEET 1 AF6 4 SER L 113 PHE L 117 0
SHEET 2 AF6 4 THR L 128 PHE L 138 -1 O LEU L 134 N PHE L 115
SHEET 3 AF6 4 TYR L 172 SER L 181 -1 O LEU L 174 N LEU L 135
SHEET 4 AF6 4 SER L 158 VAL L 162 -1 N SER L 161 O SER L 175
SHEET 1 AF7 3 LYS L 144 VAL L 149 0
SHEET 2 AF7 3 TYR L 191 THR L 196 -1 O ALA L 192 N LYS L 148
SHEET 3 AF7 3 VAL L 204 SER L 207 -1 O SER L 207 N TYR L 191
SHEET 1 AF8 4 LEU E 4 SER E 7 0
SHEET 2 AF8 4 VAL E 19 ALA E 25 -1 O ARG E 24 N SER E 5
SHEET 3 AF8 4 SER E 69 ILE E 74 -1 O LEU E 72 N MET E 21
SHEET 4 AF8 4 PHE E 61 SER E 66 -1 N SER E 62 O THR E 73
SHEET 1 AF9 6 ILE E 10 ALA E 13 0
SHEET 2 AF9 6 THR E 101 ILE E 105 1 O LYS E 102 N LEU E 11
SHEET 3 AF9 6 THR E 84 GLN E 89 -1 N TYR E 85 O THR E 101
SHEET 4 AF9 6 MET E 32 GLN E 37 -1 N HIS E 33 O GLN E 88
SHEET 5 AF9 6 LYS E 44 HIS E 48 -1 O LYS E 44 N GLN E 36
SHEET 6 AF9 6 ASN E 52 LEU E 53 -1 O ASN E 52 N HIS E 48
SHEET 1 AG1 4 ILE E 10 ALA E 13 0
SHEET 2 AG1 4 THR E 101 ILE E 105 1 O LYS E 102 N LEU E 11
SHEET 3 AG1 4 THR E 84 GLN E 89 -1 N TYR E 85 O THR E 101
SHEET 4 AG1 4 THR E 96 PHE E 97 -1 O THR E 96 N GLN E 89
SHEET 1 AG2 4 SER E 113 PHE E 117 0
SHEET 2 AG2 4 THR E 128 PHE E 138 -1 O VAL E 132 N PHE E 117
SHEET 3 AG2 4 TYR E 172 SER E 181 -1 O LEU E 174 N LEU E 135
SHEET 4 AG2 4 SER E 158 VAL E 162 -1 N SER E 161 O SER E 175
SHEET 1 AG3 3 LYS E 144 LYS E 148 0
SHEET 2 AG3 3 ALA E 192 THR E 196 -1 O THR E 196 N LYS E 144
SHEET 3 AG3 3 VAL E 204 LYS E 206 -1 O THR E 205 N CYS E 193
SHEET 1 AG4 4 GLN H 3 GLN H 6 0
SHEET 2 AG4 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5
SHEET 3 AG4 4 THR H 78 LEU H 83 -1 O ILE H 81 N ILE H 20
SHEET 4 AG4 4 ALA H 68 ASP H 73 -1 N THR H 69 O GLN H 82
SHEET 1 AG5 6 GLU H 10 VAL H 12 0
SHEET 2 AG5 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12
SHEET 3 AG5 6 ALA H 92 PHE H 99 -1 N TYR H 94 O THR H 110
SHEET 4 AG5 6 ASN H 33 SER H 40 -1 N GLN H 39 O VAL H 93
SHEET 5 AG5 6 LYS H 43 VAL H 51 -1 O ILE H 48 N TRP H 36
SHEET 6 AG5 6 THR H 58 TYR H 60 -1 O ASN H 59 N VAL H 50
SHEET 1 AG6 4 GLU H 10 VAL H 12 0
SHEET 2 AG6 4 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12
SHEET 3 AG6 4 ALA H 92 PHE H 99 -1 N TYR H 94 O THR H 110
SHEET 4 AG6 4 VAL H 105 TRP H 106 -1 O VAL H 105 N ARG H 98
SHEET 1 AG7 4 SER H 123 LEU H 127 0
SHEET 2 AG7 4 THR H 138 TYR H 148 -1 O GLY H 142 N LEU H 127
SHEET 3 AG7 4 TYR H 179 PRO H 188 -1 O LEU H 181 N VAL H 145
SHEET 4 AG7 4 HIS H 167 THR H 168 -1 N HIS H 167 O VAL H 184
SHEET 1 AG8 4 THR H 134 SER H 135 0
SHEET 2 AG8 4 THR H 138 TYR H 148 -1 O THR H 138 N SER H 135
SHEET 3 AG8 4 TYR H 179 PRO H 188 -1 O LEU H 181 N VAL H 145
SHEET 4 AG8 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180
SHEET 1 AG9 3 VAL H 153 TRP H 157 0
SHEET 2 AG9 3 TYR H 197 HIS H 203 -1 O ASN H 200 N SER H 156
SHEET 3 AG9 3 THR H 208 VAL H 214 -1 O VAL H 214 N TYR H 197
SHEET 1 AH1 4 GLN F 3 GLN F 6 0
SHEET 2 AH1 4 VAL F 18 SER F 25 -1 O LYS F 23 N GLN F 5
SHEET 3 AH1 4 THR F 78 LEU F 83 -1 O ALA F 79 N CYS F 22
SHEET 4 AH1 4 ALA F 68 ASP F 73 -1 N THR F 71 O TYR F 80
SHEET 1 AH2 6 GLU F 10 VAL F 12 0
SHEET 2 AH2 6 THR F 110 VAL F 114 1 O THR F 111 N GLU F 10
SHEET 3 AH2 6 ALA F 92 PHE F 99 -1 N ALA F 92 O VAL F 112
SHEET 4 AH2 6 ASN F 33 GLN F 39 -1 N ASN F 35 O THR F 97
SHEET 5 AH2 6 GLU F 46 ILE F 52 -1 O ILE F 48 N TRP F 36
SHEET 6 AH2 6 THR F 57 TYR F 60 -1 O ASN F 59 N VAL F 50
SHEET 1 AH3 4 GLU F 10 VAL F 12 0
SHEET 2 AH3 4 THR F 110 VAL F 114 1 O THR F 111 N GLU F 10
SHEET 3 AH3 4 ALA F 92 PHE F 99 -1 N ALA F 92 O VAL F 112
SHEET 4 AH3 4 PHE F 103 TRP F 106 -1 O VAL F 105 N ARG F 98
SHEET 1 AH4 4 VAL F 124 LEU F 127 0
SHEET 2 AH4 4 THR F 138 TYR F 148 -1 O GLY F 142 N LEU F 127
SHEET 3 AH4 4 TYR F 179 PRO F 188 -1 O VAL F 187 N ALA F 139
SHEET 4 AH4 4 VAL F 166 THR F 168 -1 N HIS F 167 O VAL F 184
SHEET 1 AH5 4 THR F 134 SER F 135 0
SHEET 2 AH5 4 THR F 138 TYR F 148 -1 O THR F 138 N SER F 135
SHEET 3 AH5 4 TYR F 179 PRO F 188 -1 O VAL F 187 N ALA F 139
SHEET 4 AH5 4 VAL F 172 LEU F 173 -1 N VAL F 172 O SER F 180
SHEET 1 AH6 3 THR F 154 TRP F 157 0
SHEET 2 AH6 3 TYR F 197 HIS F 203 -1 O ASN F 202 N THR F 154
SHEET 3 AH6 3 THR F 208 VAL F 214 -1 O VAL F 214 N TYR F 197
SHEET 1 AH7 4 LEU G 4 SER G 7 0
SHEET 2 AH7 4 MET G 21 ALA G 25 -1 O ARG G 24 N SER G 5
SHEET 3 AH7 4 SER G 69 LEU G 72 -1 O LEU G 72 N MET G 21
SHEET 4 AH7 4 GLY G 63 SER G 66 -1 N SER G 64 O SER G 71
SHEET 1 AH8 5 ILE G 10 SER G 12 0
SHEET 2 AH8 5 THR G 101 GLU G 104 1 O LYS G 102 N LEU G 11
SHEET 3 AH8 5 THR G 84 GLN G 89 -1 N TYR G 85 O THR G 101
SHEET 4 AH8 5 MET G 32 GLN G 37 -1 N HIS G 33 O GLN G 88
SHEET 5 AH8 5 LYS G 44 LEU G 47 -1 O LYS G 44 N GLN G 36
SHEET 1 AH9 4 ILE G 10 SER G 12 0
SHEET 2 AH9 4 THR G 101 GLU G 104 1 O LYS G 102 N LEU G 11
SHEET 3 AH9 4 THR G 84 GLN G 89 -1 N TYR G 85 O THR G 101
SHEET 4 AH9 4 THR G 96 PHE G 97 -1 O THR G 96 N GLN G 89
SHEET 1 AI1 3 ILE I 20 LYS I 23 0
SHEET 2 AI1 3 THR I 78 ILE I 81 -1 O ALA I 79 N CYS I 22
SHEET 3 AI1 3 LEU I 70 ASP I 73 -1 N ASP I 73 O THR I 78
SHEET 1 AI2 5 THR I 58 TYR I 60 0
SHEET 2 AI2 5 LEU I 45 VAL I 51 -1 N VAL I 50 O ASN I 59
SHEET 3 AI2 5 ASN I 33 GLN I 39 -1 N TRP I 36 O ILE I 48
SHEET 4 AI2 5 ALA I 92 PHE I 99 -1 O TYR I 95 N MET I 37
SHEET 5 AI2 5 VAL I 105 TRP I 106 -1 O VAL I 105 N ARG I 98
SHEET 1 AI3 5 THR I 58 TYR I 60 0
SHEET 2 AI3 5 LEU I 45 VAL I 51 -1 N VAL I 50 O ASN I 59
SHEET 3 AI3 5 ASN I 33 GLN I 39 -1 N TRP I 36 O ILE I 48
SHEET 4 AI3 5 ALA I 92 PHE I 99 -1 O TYR I 95 N MET I 37
SHEET 5 AI3 5 THR I 110 VAL I 112 -1 O VAL I 112 N ALA I 92
SHEET 1 AI4 4 LEU J 4 SER J 5 0
SHEET 2 AI4 4 THR J 19 VAL J 28 -1 O ARG J 23 N SER J 5
SHEET 3 AI4 4 GLY J 66 ILE J 73 -1 O PHE J 69 N CYS J 22
SHEET 4 AI4 4 PHE J 60 SER J 63 -1 N SER J 63 O SER J 70
SHEET 1 AI5 5 ASN J 51 LEU J 52 0
SHEET 2 AI5 5 SER J 40 HIS J 47 -1 N HIS J 47 O ASN J 51
SHEET 3 AI5 5 HIS J 32 LYS J 37 -1 N TRP J 33 O LEU J 46
SHEET 4 AI5 5 PHE J 85 GLN J 88 -1 O GLN J 87 N HIS J 32
SHEET 5 AI5 5 THR J 95 PHE J 96 -1 O THR J 95 N GLN J 88
SHEET 1 AI6 2 GLN K 3 LEU K 4 0
SHEET 2 AI6 2 ALA K 24 SER K 25 -1 O SER K 25 N GLN K 3
SHEET 1 AI7 3 VAL K 18 SER K 21 0
SHEET 2 AI7 3 TYR K 80 LEU K 83 -1 O LEU K 83 N VAL K 18
SHEET 3 AI7 3 THR K 69 THR K 71 -1 N THR K 69 O GLN K 82
SHEET 1 AI8 5 THR K 58 TYR K 60 0
SHEET 2 AI8 5 LEU K 45 VAL K 51 -1 N VAL K 50 O ASN K 59
SHEET 3 AI8 5 ILE K 34 GLN K 39 -1 N ILE K 34 O VAL K 51
SHEET 4 AI8 5 ALA K 92 ARG K 98 -1 O VAL K 93 N GLN K 39
SHEET 5 AI8 5 VAL K 105 TRP K 106 -1 O VAL K 105 N ARG K 98
SHEET 1 AI9 5 THR K 58 TYR K 60 0
SHEET 2 AI9 5 LEU K 45 VAL K 51 -1 N VAL K 50 O ASN K 59
SHEET 3 AI9 5 ILE K 34 GLN K 39 -1 N ILE K 34 O VAL K 51
SHEET 4 AI9 5 ALA K 92 ARG K 98 -1 O VAL K 93 N GLN K 39
SHEET 5 AI9 5 THR K 110 VAL K 112 -1 O THR K 110 N TYR K 94
SSBOND 1 CYS A 326 CYS A 337 1555 1555 2.06
SSBOND 2 CYS A 383 CYS A 395 1555 1555 2.07
SSBOND 3 CYS A 445 CYS A 448 1555 1555 2.06
SSBOND 4 CYS A 455 CYS A 473 1555 1555 2.07
SSBOND 5 CYS A 650 CYS A 763 1555 1555 2.06
SSBOND 6 CYS B 326 CYS B 337 1555 1555 2.05
SSBOND 7 CYS B 383 CYS B 395 1555 1555 2.06
SSBOND 8 CYS B 445 CYS B 448 1555 1555 2.05
SSBOND 9 CYS B 455 CYS B 473 1555 1555 2.07
SSBOND 10 CYS B 650 CYS B 763 1555 1555 2.06
SSBOND 11 CYS C 326 CYS C 337 1555 1555 2.06
SSBOND 12 CYS C 383 CYS C 395 1555 1555 2.02
SSBOND 13 CYS C 445 CYS C 448 1555 1555 2.05
SSBOND 14 CYS C 455 CYS C 473 1555 1555 2.03
SSBOND 15 CYS C 650 CYS C 763 1555 1555 2.04
SSBOND 16 CYS D 326 CYS D 337 1555 1555 2.05
SSBOND 17 CYS D 383 CYS D 395 1555 1555 1.99
SSBOND 18 CYS D 445 CYS D 448 1555 1555 2.04
SSBOND 19 CYS D 455 CYS D 473 1555 1555 2.05
SSBOND 20 CYS D 650 CYS D 763 1555 1555 2.06
SSBOND 21 CYS L 23 CYS L 87 1555 1555 2.08
SSBOND 22 CYS L 133 CYS L 193 1555 1555 2.03
SSBOND 23 CYS E 23 CYS E 87 1555 1555 2.04
SSBOND 24 CYS E 133 CYS E 193 1555 1555 2.04
SSBOND 25 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 26 CYS H 143 CYS H 199 1555 1555 2.05
SSBOND 27 CYS F 22 CYS F 96 1555 1555 2.05
SSBOND 28 CYS F 143 CYS F 199 1555 1555 2.04
SSBOND 29 CYS G 23 CYS G 87 1555 1555 2.06
SSBOND 30 CYS I 22 CYS I 96 1555 1555 2.04
SSBOND 31 CYS J 22 CYS J 86 1555 1555 2.03
SSBOND 32 CYS K 22 CYS K 96 1555 1555 2.06
LINK ND2 ASN A 83 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 90 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN A 227 C1 NAG A 803 1555 1555 1.46
LINK ND2 ASN A 319 C1 NAG A 804 1555 1555 1.45
LINK ND2 ASN A 521 C1 NAG A 805 1555 1555 1.45
LINK ND2 ASN B 83 C1 NAG B 801 1555 1555 1.44
LINK ND2 ASN B 90 C1 NAG B 802 1555 1555 1.45
LINK ND2 ASN B 227 C1 NAG B 803 1555 1555 1.46
LINK ND2 ASN B 521 C1 NAG B 804 1555 1555 1.45
LINK ND2 ASN C 83 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN C 90 C1 NAG C 802 1555 1555 1.46
LINK ND2 ASN C 148 C1 NAG C 803 1555 1555 1.45
LINK ND2 ASN C 227 C1 NAG C 804 1555 1555 1.44
LINK ND2 ASN C 319 C1 NAG C 805 1555 1555 1.44
LINK ND2 ASN C 521 C1 NAG C 806 1555 1555 1.44
LINK ND2 ASN D 83 C1 NAG D 805 1555 1555 1.44
LINK ND2 ASN D 90 C1 NAG D 801 1555 1555 1.44
LINK ND2 ASN D 217 C1 NAG D 802 1555 1555 1.44
LINK ND2 ASN D 227 C1 NAG D 806 1555 1555 1.45
LINK ND2 ASN D 319 C1 NAG D 803 1555 1555 1.46
LINK ND2 ASN D 521 C1 NAG D 804 1555 1555 1.45
CISPEP 1 GLY A 475 PRO A 476 0 4.59
CISPEP 2 GLY B 475 PRO B 476 0 6.79
CISPEP 3 GLY C 475 PRO C 476 0 3.86
CISPEP 4 GLY D 475 PRO D 476 0 5.25
CISPEP 5 SER L 7 PRO L 8 0 -15.42
CISPEP 6 HIS L 93 PRO L 94 0 4.09
CISPEP 7 SER E 7 PRO E 8 0 -4.48
CISPEP 8 HIS E 93 PRO E 94 0 7.85
CISPEP 9 TYR E 139 PRO E 140 0 21.66
CISPEP 10 PHE H 149 PRO H 150 0 -8.43
CISPEP 11 GLU H 151 PRO H 152 0 12.76
CISPEP 12 PHE F 149 PRO F 150 0 -6.78
CISPEP 13 GLU F 151 PRO F 152 0 -5.87
CISPEP 14 SER G 7 PRO G 8 0 -13.98
CISPEP 15 HIS G 93 PRO G 94 0 10.67
CISPEP 16 HIS J 92 PRO J 93 0 2.48
SITE 1 AC1 3 GLU A 235 TRP A 251 GLU B 235
SITE 1 AC2 5 HIS A 124 PHE A 206 GLY A 207 ARG A 356
SITE 2 AC2 5 9K4 A 813
SITE 1 AC3 3 ASP A 134 ASN A 136 LYS A 137
SITE 1 AC4 3 TYR A 239 THR A 707 TYR B 239
SITE 1 AC5 4 LYS A 513 PHE A 560 ARG A 561 THR A 566
SITE 1 AC6 5 GLN A 528 ILE A 530 ASP A 546 VAL A 576
SITE 2 AC6 5 SER A 578
SITE 1 AC7 5 TRP A 735 TYR A 736 THR A 737 SER B 721
SITE 2 AC7 5 LYS B 722
SITE 1 AC8 16 SER A 101 TYR A 118 ARG A 123 HIS A 124
SITE 2 AC8 16 GLU A 203 GLU A 204 PHE A 355 TYR A 548
SITE 3 AC8 16 SER A 631 TYR A 632 VAL A 657 TYR A 663
SITE 4 AC8 16 TYR A 667 ASN A 711 VAL A 712 PEG A 807
SITE 1 AC9 7 ALA B 549 SER B 553 PHE B 579 ASP B 580
SITE 2 AC9 7 GLY B 581 SER B 584 GLN B 607
SITE 1 AD1 17 ASP B 98 SER B 101 TYR B 118 ARG B 123
SITE 2 AD1 17 GLU B 203 GLU B 204 PHE B 355 TYR B 548
SITE 3 AD1 17 SER B 631 TYR B 632 VAL B 657 TYR B 663
SITE 4 AD1 17 TYR B 667 ASN B 711 VAL B 712 HIS B 741
SITE 5 AD1 17 CYS G 30
SITE 1 AD2 4 ASN C 90 GLU C 94 NAG C 802 ASP F 31
SITE 1 AD3 5 ASP C 102 GLU C 115 TYR C 118 TYR C 126
SITE 2 AD3 5 9K4 C 812
SITE 1 AD4 2 ARG C 123 SER C 631
SITE 1 AD5 4 ASP C 102 GLU C 115 TRP C 152 ILE C 153
SITE 1 AD6 5 PHE C 385 ARG C 389 GLN C 393 VAL C 394
SITE 2 AD6 5 CYS C 395
SITE 1 AD7 15 TYR C 118 ARG C 123 GLU C 203 GLU C 204
SITE 2 AD7 15 PHE C 355 TYR C 548 SER C 631 TYR C 632
SITE 3 AD7 15 VAL C 657 TYR C 663 TYR C 667 ASN C 711
SITE 4 AD7 15 VAL C 712 HIS C 741 EDO C 808
SITE 1 AD8 5 GLU C 739 THR C 747 LYS D 722 VAL D 725
SITE 2 AD8 5 ASP D 726
SITE 1 AD9 11 TYR D 118 ARG D 123 GLU D 203 GLU D 204
SITE 2 AD9 11 SER D 631 TYR D 632 TYR D 663 TYR D 667
SITE 3 AD9 11 ASN D 711 VAL D 712 CYS L 30
SITE 1 AE1 2 ASN A 83 SER A 85
SITE 1 AE2 5 GLU A 71 ASN A 72 ASN A 73 ASN A 90
SITE 2 AE2 5 GLU A 94
SITE 1 AE3 1 ASN A 227
SITE 1 AE4 3 ASN A 319 SER A 347 LYS A 597
SITE 1 AE5 2 ASN A 521 ARG A 582
SITE 1 AE6 1 ASN B 83
SITE 1 AE7 3 GLU B 71 ASN B 73 ASN B 90
SITE 1 AE8 3 ASN B 227 THR B 229 LYS B 265
SITE 1 AE9 2 ASN B 521 ARG B 582
SITE 1 AF1 3 LEU C 76 ASN C 83 SER C 85
SITE 1 AF2 4 GLU C 71 ASN C 73 ASN C 90 EDO C 807
SITE 1 AF3 2 ASN C 148 ASN C 149
SITE 1 AF4 3 ASN C 227 THR C 229 LYS C 265
SITE 1 AF5 1 ASN C 319
SITE 1 AF6 1 ASN C 521
SITE 1 AF7 1 ASN D 83
SITE 1 AF8 4 GLU D 71 ASN D 73 ASN D 90 GLU D 94
SITE 1 AF9 1 ASN D 217
SITE 1 AG1 3 ASN D 227 THR D 229 LYS D 265
SITE 1 AG2 1 ASN D 319
SITE 1 AG3 2 ASN D 521 ARG D 582
CRYST1 120.325 123.229 129.018 62.34 77.21 75.91 P 1 4
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 0.008311 -0.002085 -0.001091 0.00000
SCALE2 0.000000 0.008367 -0.004028 0.00000
SCALE3 0.000000 0.000000 0.008821 0.00000
TER 5930 LEU A 766
TER 11783 LEU B 766
TER 17713 LEU C 766
TER 23635 SER D 765
TER 25214 PHE L 208
TER 26761 SER E 207
TER 28401 LYS H 217
TER 30041 LYS F 217
TER 30789 GLU G 104
TER 31689 SER I 116
TER 32359 GLY J 99
TER 33220 THR K 113
MASTER 1060 0 39 87 331 0 59 633868 12 634 364
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