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HEADER HYDROLASE,SIGNALING PROTEIN 03-AUG-10 3O95
TITLE CRYSTAL STRUCTURE OF HUMAN DPP4 BOUND TO TAK-100
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN
COMPND 5 CD26, TP103, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2, ADABP;
COMPND 6 EC: 3.4.14.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADCP2, CD26, DPP4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS PROTEASE AND 8-BLADED BETA-PROPELLER DOMAIN, AMINOPEPTIDASE, CELL
KEYWDS 2 MEMBRANE, GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED,
KEYWDS 3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE, SIGNALING PROTEIN,
KEYWDS 4 HYDROLASE,SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.YANO,K.AERTGEERTS
REVDAT 1 26-JAN-11 3O95 0
JRNL AUTH Y.MIYAMOTO,Y.BANNO,T.YAMASHITA,T.FUJIMOTO,S.OI,Y.MORITOH,
JRNL AUTH 2 T.ASAKAWA,O.KATAOKA,H.YASHIRO,K.TAKEUCHI,N.SUZUKI,K.IKEDO,
JRNL AUTH 3 T.KOSAKA,S.TSUBOTANI,A.TANI,M.SASAKI,M.FUNAMI,M.AMANO,
JRNL AUTH 4 Y.YAMAMOTO,K.AERTGEERTS,J.YANO,H.MAEZAKI
JRNL TITL DISCOVERY OF A 3-PYRIDYLACETIC ACID DERIVATIVE (TAK-100) AS
JRNL TITL 2 A POTENT, SELECTIVE AND ORALLY ACTIVE DIPEPTIDYL PEPTIDASE
JRNL TITL 3 IV (DPP-4) INHIBITOR.
JRNL REF J.MED.CHEM. 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21218817
JRNL DOI 10.1021/JM101236H
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 89524
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4489
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) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5773
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 300
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23873
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 510
REMARK 3 SOLVENT ATOMS : 487
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.81000
REMARK 3 B22 (A**2) : 1.80000
REMARK 3 B33 (A**2) : 0.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.43000
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): 0.391
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.298
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.208
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25129 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34227 ; 1.237 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2909 ; 6.404 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1236 ;34.095 ;23.956
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3987 ;18.310 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 119 ;17.975 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3646 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19249 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 12445 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 17064 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1225 ; 0.146 ; 0.200
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): 58 ; 0.199 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.105 ; 0.200
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): 14783 ; 0.348 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23540 ; 0.629 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12056 ; 0.884 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10687 ; 1.527 ; 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3O95 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 92
REMARK 200 PH : 8-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI (220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89585
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 2000, 100 MM BICINE, PH 8-
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 61.66750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 118540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 61.18692
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -61.66750
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 131.12145
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 ALA A 27
REMARK 465 ASP A 28
REMARK 465 PRO A 29
REMARK 465 GLY A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 HIS A 38
REMARK 465 SER A 39
REMARK 465 ALA B 27
REMARK 465 ASP B 28
REMARK 465 PRO B 29
REMARK 465 GLY B 30
REMARK 465 GLY B 31
REMARK 465 SER B 32
REMARK 465 HIS B 33
REMARK 465 ALA C 27
REMARK 465 ASP C 28
REMARK 465 PRO C 29
REMARK 465 GLY C 30
REMARK 465 GLY C 31
REMARK 465 SER C 32
REMARK 465 HIS C 33
REMARK 465 HIS C 34
REMARK 465 HIS C 35
REMARK 465 HIS C 36
REMARK 465 HIS C 37
REMARK 465 HIS C 38
REMARK 465 SER C 39
REMARK 465 ARG C 40
REMARK 465 ALA D 27
REMARK 465 ASP D 28
REMARK 465 PRO D 29
REMARK 465 GLY D 30
REMARK 465 GLY D 31
REMARK 465 SER D 32
REMARK 465 HIS D 33
REMARK 465 HIS D 34
REMARK 465 HIS D 35
REMARK 465 HIS D 36
REMARK 465 HIS D 37
REMARK 465 HIS D 38
REMARK 465 SER D 39
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 SER A 64 -155.82 -136.61
REMARK 500 LYS A 71 46.98 -103.87
REMARK 500 GLU A 73 -153.80 96.19
REMARK 500 SER A 106 113.38 -166.72
REMARK 500 ASP A 110 2.16 -69.28
REMARK 500 GLN A 123 -107.13 -116.28
REMARK 500 ARG A 140 55.01 81.26
REMARK 500 ILE A 193 -53.61 -127.06
REMARK 500 SER A 209 42.15 38.53
REMARK 500 SER A 242 -163.91 60.20
REMARK 500 VAL A 279 -61.59 -99.08
REMARK 500 GLN A 320 43.75 -76.17
REMARK 500 LEU A 340 112.03 -37.28
REMARK 500 ASN A 420 40.68 -96.76
REMARK 500 ASP A 438 91.06 -174.89
REMARK 500 ASN A 450 89.34 -169.04
REMARK 500 PRO A 531 157.92 -48.56
REMARK 500 TYR A 547 -68.56 -124.37
REMARK 500 ARG A 597 45.88 -141.21
REMARK 500 THR A 600 -89.47 -122.66
REMARK 500 SER A 630 -120.10 63.88
REMARK 500 ASP A 678 -107.60 -122.59
REMARK 500 ASN A 710 -76.03 -97.94
REMARK 500 ASP A 739 -154.19 -101.63
REMARK 500 SER A 745 -68.09 -24.85
REMARK 500 SER B 64 -144.96 -117.02
REMARK 500 GLN B 72 -75.36 -110.74
REMARK 500 ASN B 74 -6.08 73.60
REMARK 500 TYR B 83 -76.81 -94.66
REMARK 500 ASN B 85 83.58 -28.30
REMARK 500 VAL B 88 120.34 -31.56
REMARK 500 LEU B 90 108.57 -162.24
REMARK 500 PHE B 95 64.92 -103.33
REMARK 500 GLN B 123 -114.18 -121.83
REMARK 500 TRP B 124 -153.44 -78.47
REMARK 500 GLU B 146 52.36 38.72
REMARK 500 HIS B 162 43.97 -143.87
REMARK 500 ASP B 192 -11.97 69.84
REMARK 500 ASP B 200 -167.43 -100.34
REMARK 500 SER B 242 -162.58 66.73
REMARK 500 GLN B 320 48.89 -90.10
REMARK 500 THR B 401 45.75 -82.98
REMARK 500 ASN B 420 40.01 -103.95
REMARK 500 LEU B 449 -71.88 -56.94
REMARK 500 GLN B 455 19.85 -141.09
REMARK 500 ASN B 487 12.79 -142.81
REMARK 500 LEU B 491 -72.38 -98.37
REMARK 500 ASN B 506 33.68 -96.16
REMARK 500 GLU B 521 -5.36 69.17
REMARK 500 TYR B 547 -63.13 -125.64
REMARK 500
REMARK 500 THIS ENTRY HAS 130 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 781 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH B 789 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH D 786 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH C 795 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH C 798 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH C 800 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B 807 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH B 814 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH D 821 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A 832 DISTANCE = 5.25 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 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2812
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 01T A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 01T B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2293
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 01T C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 5201
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 01T D 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O9V RELATED DB: PDB
DBREF 3O95 A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3O95 B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3O95 C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3O95 D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3O95 ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 3O95 PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 3O95 SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 3O95 PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 3O95 SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 3O95 PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 3O95 SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 3O95 ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 3O95 PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 3O95 GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 3O95 SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 3O95 HIS D 38 UNP P27487 EXPRESSION TAG
SEQRES 1 A 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 A 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 A 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 A 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 A 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 A 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 A 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 A 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 A 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 A 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 A 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 A 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 A 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 A 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 A 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 A 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 A 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 A 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 A 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 A 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 A 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 A 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 A 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 A 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 A 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 A 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 A 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 A 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 A 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 A 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 A 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 A 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 A 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 A 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 A 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 A 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 A 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 A 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 A 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 A 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 A 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 A 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 A 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 A 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 A 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 A 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 A 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 A 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 A 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 A 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 A 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 A 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 A 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 A 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 A 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 A 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 B 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 B 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 B 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 B 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 B 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 B 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 B 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 B 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 B 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 B 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 B 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 B 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 B 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 B 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 B 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 B 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 B 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 B 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 B 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 B 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 B 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 B 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 B 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 B 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 B 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 B 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 B 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 B 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 B 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 B 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 B 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 B 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 B 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 B 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 B 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 B 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 B 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 B 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 B 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 B 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 B 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 B 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 B 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 B 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 B 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 B 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 B 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 B 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 B 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 B 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 B 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 B 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 B 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 B 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 B 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 C 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 C 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 C 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 C 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 C 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 C 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 C 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 C 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 C 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 C 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 C 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 C 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 C 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 C 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 C 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 C 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 C 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 C 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 C 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 C 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 C 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 C 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 C 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 C 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 C 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 C 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 C 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 C 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 C 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 C 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 C 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 C 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 C 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 C 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 C 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 C 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 C 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 C 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 C 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 C 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 C 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 C 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 C 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 C 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 C 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 C 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 C 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 C 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 C 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 C 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 C 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 C 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 C 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 C 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 C 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 C 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 D 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 D 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 D 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 D 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 D 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 D 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 D 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 D 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 D 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 D 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 D 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 D 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 D 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 D 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 D 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 D 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 D 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 D 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 D 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 D 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 D 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 D 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 D 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 D 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 D 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 D 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 D 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 D 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 D 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 D 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 D 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 D 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 D 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 D 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 D 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 D 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 D 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 D 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 D 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 D 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 D 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 D 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 D 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 D 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 D 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 D 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 D 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 D 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 D 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 D 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 D 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 D 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 D 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 D 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 D 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 D 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
MODRES 3O95 ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN D 229 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN D 219 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN D 150 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN C 321 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN C 229 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN D 520 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN B 321 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN D 281 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN C 150 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN C 281 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN B 281 ASN GLYCOSYLATION SITE
MODRES 3O95 ASN A 281 ASN GLYCOSYLATION SITE
HET NAG A1501 14
HET NAG A1502 14
HET NAG A1503 14
HET NAG A1504 14
HET NAG A2191 14
HET NAG A2291 14
HET NAG A2292 14
HET NAG A2811 14
HET NAG A2812 14
HET NAG A3211 14
HET 01T A 1 26
HET NAG B 901 14
HET NAG B 902 14
HET NAG B1501 14
HET NAG B2291 14
HET NAG B2292 14
HET NAG B2811 14
HET NAG B3211 14
HET 01T B 1 26
HET NAG C2292 14
HET NAG C2291 14
HET NAG C2293 14
HET NAG C1501 14
HET NAG C2811 14
HET NAG C3211 14
HET 01T C 1 26
HET NAG D1501 14
HET NAG D2191 14
HET NAG D2291 14
HET NAG D2292 14
HET NAG D2811 14
HET NAG D5201 14
HET 01T D 1 26
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 01T [5-(AMINOMETHYL)-6-(2,2-DIMETHYLPROPYL)-2-ETHYL-4-(4-
HETNAM 2 01T METHYLPHENYL)PYRIDIN-3-YL]ACETIC ACID
HETSYN 01T TAK-100
FORMUL 5 NAG 29(C8 H15 N O6)
FORMUL 11 01T 4(C22 H30 N2 O2)
FORMUL 29 HOH *487(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 PRO A 290 ILE A 295 1 6
HELIX 4 4 LEU A 340 GLN A 344 5 5
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 ASN A 497 GLN A 505 1 9
HELIX 7 7 ASN A 562 THR A 570 1 9
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 ALA A 593 ASN A 595 5 3
HELIX 10 10 THR A 600 SER A 614 1 15
HELIX 11 11 SER A 630 GLY A 641 1 12
HELIX 12 12 ARG A 658 TYR A 662 5 5
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 HIS A 712 VAL A 726 1 15
HELIX 17 17 SER A 744 PHE A 763 1 20
HELIX 18 18 THR B 44 LYS B 50 1 7
HELIX 19 19 ASP B 200 VAL B 207 1 8
HELIX 20 20 ASP B 274 LEU B 276 5 3
HELIX 21 21 PRO B 290 ILE B 295 1 6
HELIX 22 22 VAL B 341 GLN B 344 5 4
HELIX 23 23 GLU B 421 MET B 425 5 5
HELIX 24 24 ASN B 497 LEU B 504 1 8
HELIX 25 25 ASN B 562 THR B 570 1 9
HELIX 26 26 GLY B 587 HIS B 592 1 6
HELIX 27 27 ALA B 593 ASN B 595 5 3
HELIX 28 28 THR B 600 LYS B 615 1 16
HELIX 29 29 SER B 630 GLY B 641 1 12
HELIX 30 30 ARG B 658 TYR B 662 5 5
HELIX 31 31 ASP B 663 GLY B 672 1 10
HELIX 32 32 ASN B 679 SER B 686 1 8
HELIX 33 33 THR B 687 VAL B 698 5 12
HELIX 34 34 HIS B 712 VAL B 726 1 15
HELIX 35 35 SER B 744 PHE B 763 1 20
HELIX 36 36 THR C 44 LYS C 50 1 7
HELIX 37 37 ASP C 200 GLU C 206 1 7
HELIX 38 38 PRO C 290 ILE C 295 1 6
HELIX 39 39 VAL C 341 GLN C 344 5 4
HELIX 40 40 GLU C 421 MET C 425 5 5
HELIX 41 41 ASN C 497 LEU C 504 1 8
HELIX 42 42 ASN C 562 THR C 570 1 9
HELIX 43 43 GLY C 587 HIS C 592 1 6
HELIX 44 44 ALA C 593 ASN C 595 5 3
HELIX 45 45 THR C 600 LYS C 615 1 16
HELIX 46 46 SER C 630 GLY C 643 1 14
HELIX 47 47 ARG C 658 TYR C 662 5 5
HELIX 48 48 ASP C 663 GLY C 672 1 10
HELIX 49 49 ASN C 679 SER C 686 1 8
HELIX 50 50 VAL C 688 VAL C 698 5 11
HELIX 51 51 HIS C 712 VAL C 726 1 15
HELIX 52 52 SER C 744 PHE C 763 1 20
HELIX 53 53 THR D 44 ASN D 51 1 8
HELIX 54 54 ASP D 200 VAL D 207 1 8
HELIX 55 55 ASP D 274 LEU D 276 5 3
HELIX 56 56 PRO D 290 ILE D 295 1 6
HELIX 57 57 LEU D 340 GLN D 344 5 5
HELIX 58 58 GLU D 421 MET D 425 5 5
HELIX 59 59 SER D 437 TYR D 439 5 3
HELIX 60 60 ASN D 497 GLN D 505 1 9
HELIX 61 61 ASN D 562 THR D 570 1 9
HELIX 62 62 GLY D 587 HIS D 592 1 6
HELIX 63 63 ALA D 593 ASN D 595 5 3
HELIX 64 64 THR D 600 LYS D 615 1 16
HELIX 65 65 SER D 630 GLY D 641 1 12
HELIX 66 66 ARG D 658 TYR D 662 5 5
HELIX 67 67 ASP D 663 GLY D 672 1 10
HELIX 68 68 ASN D 679 SER D 686 1 8
HELIX 69 69 VAL D 688 VAL D 698 5 11
HELIX 70 70 PHE D 713 VAL D 726 1 14
HELIX 71 71 SER D 744 PHE D 763 1 20
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 ARG A 61 TRP A 62 0
SHEET 2 B 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ILE A 76 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 B 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 THR A 152 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N GLN A 153
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O VAL A 271 N LEU A 223
SHEET 4 F 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 ASP A 331 -1 O VAL A 324 N TRP A 315
SHEET 4 H 4 ARG A 336 ASN A 338 -1 O ARG A 336 N ASP A 331
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 I 4 TYR A 322 ASP A 331 -1 O VAL A 324 N TRP A 315
SHEET 4 I 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 L 4 GLY A 490 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O SER A 577 N GLN A 527
SHEET 4 M 8 TYR A 540 ASP A 545 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 ARG B 61 TRP B 62 0
SHEET 2 O 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ILE B 76 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 O 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 P 4 ASP B 104 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 S 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 U 4 HIS B 298 TRP B 305 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O CYS B 328 N ILE B 311
SHEET 4 U 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 TRP B 305 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 V 4 TYR B 322 TYR B 330 -1 O CYS B 328 N ILE B 311
SHEET 4 V 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 ASP B 438 CYS B 444 -1 O LYS B 441 N GLN B 435
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AA 4 ARG C 61 TRP C 62 0
SHEET 2 AA 4 TYR C 68 LYS C 71 -1 O LEU C 69 N ARG C 61
SHEET 3 AA 4 ILE C 76 PHE C 79 -1 O PHE C 79 N TYR C 68
SHEET 4 AA 4 SER C 86 LEU C 90 -1 O LEU C 90 N ILE C 76
SHEET 1 AB 4 ASP C 104 ILE C 107 0
SHEET 2 AB 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AB 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AB 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AC 4 TRP C 154 TRP C 157 0
SHEET 2 AC 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AC 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AC 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AD 3 ILE C 194 ASN C 196 0
SHEET 2 AD 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AE 4 ILE C 194 ASN C 196 0
SHEET 2 AE 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 4 THR C 265 ASN C 272 -1 O THR C 265 N ASN C 229
SHEET 4 AE 4 ILE C 285 ILE C 287 -1 O ILE C 287 N PHE C 268
SHEET 1 AF 2 LEU C 235 PHE C 240 0
SHEET 2 AF 2 LYS C 250 PRO C 255 -1 O VAL C 252 N TYR C 238
SHEET 1 AG 4 HIS C 298 THR C 307 0
SHEET 2 AG 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AG 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AH 4 HIS C 298 THR C 307 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AH 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AI 4 HIS C 363 PHE C 364 0
SHEET 2 AI 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AI 4 ARG C 382 GLN C 388 -1 O HIS C 383 N ILE C 375
SHEET 4 AI 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AJ 4 VAL C 404 LEU C 410 0
SHEET 2 AJ 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AJ 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AJ 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AK 4 TYR C 457 PHE C 461 0
SHEET 2 AK 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 AK 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AK 4 GLY C 490 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AL 8 SER C 511 LEU C 519 0
SHEET 2 AL 8 THR C 522 LEU C 530 -1 O TYR C 526 N ASP C 515
SHEET 3 AL 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AL 8 TYR C 540 ASP C 545 1 N ASP C 545 O ALA C 576
SHEET 5 AL 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AL 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AL 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AL 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AM 4 ARG D 61 TRP D 62 0
SHEET 2 AM 4 GLU D 67 LYS D 71 -1 O LEU D 69 N ARG D 61
SHEET 3 AM 4 ILE D 76 ASN D 80 -1 O PHE D 79 N TYR D 68
SHEET 4 AM 4 SER D 87 LEU D 90 -1 O LEU D 90 N ILE D 76
SHEET 1 AN 3 ASP D 104 ILE D 107 0
SHEET 2 AN 3 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AN 3 TYR D 128 ASP D 136 -1 O TYR D 135 N ILE D 114
SHEET 1 AO 4 TRP D 154 TRP D 157 0
SHEET 2 AO 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 AO 4 ASP D 171 LYS D 175 -1 O TYR D 173 N TYR D 166
SHEET 4 AO 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AP 3 ILE D 194 ASN D 196 0
SHEET 2 AP 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AP 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AQ 4 ILE D 194 ASN D 196 0
SHEET 2 AQ 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AQ 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AQ 4 ILE D 285 GLN D 286 -1 O ILE D 285 N VAL D 270
SHEET 1 AR 2 LEU D 235 PHE D 240 0
SHEET 2 AR 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AS 4 HIS D 298 THR D 307 0
SHEET 2 AS 4 ARG D 310 ARG D 317 -1 O ARG D 310 N ALA D 306
SHEET 3 AS 4 TYR D 322 TYR D 330 -1 O CYS D 328 N ILE D 311
SHEET 4 AS 4 TRP D 337 ASN D 338 -1 O ASN D 338 N ASP D 329
SHEET 1 AT 4 HIS D 298 THR D 307 0
SHEET 2 AT 4 ARG D 310 ARG D 317 -1 O ARG D 310 N ALA D 306
SHEET 3 AT 4 TYR D 322 TYR D 330 -1 O CYS D 328 N ILE D 311
SHEET 4 AT 4 HIS D 345 MET D 348 -1 O GLU D 347 N SER D 323
SHEET 1 AU 4 HIS D 363 PHE D 364 0
SHEET 2 AU 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AU 4 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AU 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AV 4 VAL D 404 LEU D 410 0
SHEET 2 AV 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AV 4 ASN D 430 GLN D 435 -1 O ILE D 434 N LEU D 415
SHEET 4 AV 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AW 4 CYS D 454 PHE D 461 0
SHEET 2 AW 4 TYR D 467 PRO D 475 -1 O GLY D 474 N GLN D 455
SHEET 3 AW 4 LEU D 479 SER D 484 -1 O THR D 481 N LEU D 470
SHEET 4 AW 4 GLY D 490 GLU D 495 -1 O LEU D 494 N TYR D 480
SHEET 1 AX 8 SER D 511 ILE D 518 0
SHEET 2 AX 8 LYS D 523 LEU D 530 -1 O TYR D 526 N ASP D 515
SHEET 3 AX 8 ILE D 574 ASP D 579 -1 O VAL D 575 N ILE D 529
SHEET 4 AX 8 TYR D 540 VAL D 546 1 N ASP D 545 O ALA D 576
SHEET 5 AX 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 544
SHEET 6 AX 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AX 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AX 8 GLN D 731 TYR D 735 1 O GLN D 731 N LEU D 702
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.06
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.04
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.06
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.06
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.06
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.06
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.04
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.06
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.04
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.05
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.06
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.04
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.04
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.05
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.05
LINK ND2 ASN B 85 C1 NAG B 901 1555 1555 1.43
LINK O4 NAG D2291 C1 NAG D2292 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG A2291 1555 1555 1.44
LINK ND2 ASN D 229 C1 NAG D2291 1555 1555 1.44
LINK ND2 ASN D 219 C1 NAG D2191 1555 1555 1.45
LINK O4 NAG A2291 C1 NAG A2292 1555 1555 1.45
LINK O4 NAG A1503 C1 NAG A1504 1555 1555 1.45
LINK ND2 ASN D 150 C1 NAG D1501 1555 1555 1.45
LINK O4 NAG B 901 C1 NAG B 902 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A1501 1555 1555 1.45
LINK O4 NAG C2292 C1 NAG C2293 1555 1555 1.45
LINK O4 NAG A1501 C1 NAG A1502 1555 1555 1.45
LINK C1 NAG C2292 O4 NAG C2291 1555 1555 1.45
LINK ND2 ASN B 229 C1 NAG B2291 1555 1555 1.45
LINK ND2 ASN C 321 C1 NAG C3211 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG A2191 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG A3211 1555 1555 1.45
LINK ND2 ASN C 229 C1 NAG C2291 1555 1555 1.45
LINK ND2 ASN D 520 C1 NAG D5201 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B3211 1555 1555 1.45
LINK ND2 ASN A 85 C1 NAG A1503 1555 1555 1.45
LINK O4 NAG B2291 C1 NAG B2292 1555 1555 1.46
LINK O4 NAG A2811 C1 NAG A2812 1555 1555 1.46
LINK ND2 ASN D 281 C1 NAG D2811 1555 1555 1.46
LINK ND2 ASN C 150 C1 NAG C1501 1555 1555 1.46
LINK ND2 ASN B 150 C1 NAG B1501 1555 1555 1.46
LINK ND2 ASN C 281 C1 NAG C2811 1555 1555 1.46
LINK ND2 ASN B 281 C1 NAG B2811 1555 1555 1.46
LINK ND2 ASN A 281 C1 NAG A2811 1555 1555 1.47
CISPEP 1 GLY A 474 PRO A 475 0 0.04
CISPEP 2 GLY B 474 PRO B 475 0 5.26
CISPEP 3 GLY C 474 PRO C 475 0 5.49
CISPEP 4 GLY D 474 PRO D 475 0 7.44
SITE 1 AC1 5 ARG A 147 ASN A 150 HOH A 778 HOH A 902
SITE 2 AC1 5 NAG A1502
SITE 1 AC2 1 NAG A1501
SITE 1 AC3 4 ASN A 85 SER A 86 SER A 87 NAG A1504
SITE 1 AC4 1 NAG A1503
SITE 1 AC5 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC6 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC6 5 NAG A2292
SITE 1 AC7 3 THR A 231 HOH A 898 NAG A2291
SITE 1 AC8 3 TRP A 187 ASN A 281 NAG A2812
SITE 1 AC9 1 NAG A2811
SITE 1 BC1 5 ILE A 319 ASN A 321 SER A 349 THR A 350
SITE 2 BC1 5 HOH A 878
SITE 1 BC2 13 ARG A 125 GLU A 205 GLU A 206 PHE A 357
SITE 2 BC2 13 TYR A 547 SER A 630 VAL A 656 TYR A 662
SITE 3 BC2 13 TYR A 666 VAL A 711 HIS A 740 HOH A 775
SITE 4 BC2 13 HOH A 792
SITE 1 BC3 8 ASN B 85 SER B 87 HOH B 829 HOH B 839
SITE 2 BC3 8 HOH B 849 HOH B 877 HOH B 885 NAG B 902
SITE 1 BC4 5 TYR B 83 HOH B 849 HOH B 853 HOH B 885
SITE 2 BC4 5 NAG B 901
SITE 1 BC5 5 ARG B 147 ILE B 148 ASN B 150 HOH B 838
SITE 2 BC5 5 HOH B 854
SITE 1 BC6 5 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 BC6 5 NAG B2292
SITE 1 BC7 2 GLU B 232 NAG B2291
SITE 1 BC8 4 TRP B 187 ASN B 281 HOH B 842 HOH B 869
SITE 1 BC9 4 ILE B 319 ASN B 321 SER B 349 HOH B 862
SITE 1 CC1 11 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 CC1 11 TYR B 547 SER B 630 VAL B 656 TYR B 662
SITE 3 CC1 11 TYR B 666 HIS B 740 HOH B 794
SITE 1 CC2 2 NAG C2291 NAG C2293
SITE 1 CC3 5 ILE C 194 ASN C 229 THR C 231 GLU C 232
SITE 2 CC3 5 NAG C2292
SITE 1 CC4 1 NAG C2292
SITE 1 CC5 5 ARG C 147 ILE C 148 ASN C 150 HOH C 785
SITE 2 CC5 5 HOH C 808
SITE 1 CC6 4 ASN C 281 HOH C 805 HOH C 807 HOH C 833
SITE 1 CC7 1 ASN C 321
SITE 1 CC8 11 ARG C 125 GLU C 205 GLU C 206 SER C 209
SITE 2 CC8 11 PHE C 357 TYR C 547 SER C 630 VAL C 656
SITE 3 CC8 11 TYR C 662 TYR C 666 HIS C 740
SITE 1 CC9 3 ASN D 150 HOH D 773 HOH D 825
SITE 1 DC1 6 ASN D 219 THR D 221 GLN D 308 GLU D 309
SITE 2 DC1 6 HOH D 832 HOH D 865
SITE 1 DC2 8 ILE D 194 GLN D 227 ASN D 229 THR D 231
SITE 2 DC2 8 GLU D 232 LYS D 267 HOH D 876 NAG D2292
SITE 1 DC3 2 GLU D 232 NAG D2291
SITE 1 DC4 5 TRP D 187 ASN D 281 HOH D 833 HOH D 845
SITE 2 DC4 5 HOH D 853
SITE 1 DC5 4 LEU D 519 ASN D 520 ARG D 581 HOH D 858
SITE 1 DC6 11 ARG D 125 GLU D 205 GLU D 206 SER D 209
SITE 2 DC6 11 PHE D 357 TYR D 547 SER D 630 VAL D 656
SITE 3 DC6 11 TYR D 662 TYR D 666 HIS D 740
CRYST1 121.718 123.335 144.419 90.00 114.78 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008216 0.000000 0.003793 0.00000
SCALE2 0.000000 0.008108 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007627 0.00000
TER 5958 PRO A 766
TER 11972 PRO B 766
TER 17919 PRO C 766
TER 23877 PRO D 766
MASTER 531 0 33 71 199 0 54 624870 4 570 228
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