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HEADER HYDROLASE,SIGNALING PROTEIN 04-AUG-10 3O9V
TITLE CRYSTAL STRUCTURE OF HUMAN DPP4 BOUND TO TAK-986
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 09-FEB-11 3O9V 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. 2.75 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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 95320
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5026
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6763
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 355
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23879
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 372
REMARK 3 SOLVENT ATOMS : 451
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.08000
REMARK 3 B22 (A**2) : 0.97000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
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): 0.371
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.279
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.288
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24988 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 16632 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34021 ; 1.222 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 40156 ; 0.875 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2910 ; 6.349 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1236 ;34.267 ;23.940
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3988 ;17.821 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;17.155 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3606 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27624 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5376 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4925 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 17046 ; 0.203 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11980 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 13174 ; 0.095 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 797 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.100 ; 0.200
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): 21 ; 0.180 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.270 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.199 ; 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): 14865 ; 0.397 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5876 ; 0.061 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23545 ; 0.684 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11941 ; 0.925 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10476 ; 1.495 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O9V 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 RCSB060847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-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 : 5.0.2
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 (111)
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 : 100525
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
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: PDB ENTRY 1R9M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 2000, 100 MM BICINE, PH 8-
REMARK 280 8.5, SITTING DROP, VAPOR DIFFUSION, 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 61.44300
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: 15580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 120160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 50.0 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 61.86616
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 61.44300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 131.76702
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.0 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: 7140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 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 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU D 146 CB CG CD OE1 OE2
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 ND2 ASN B 85 C2 NAG B 851 2.19
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 HIS A 66 20.81 -149.91
REMARK 500 LYS A 71 55.43 -107.01
REMARK 500 GLU A 73 62.26 63.89
REMARK 500 ASN A 74 36.67 34.56
REMARK 500 VAL A 78 67.86 -114.59
REMARK 500 GLU A 82 -73.59 -67.54
REMARK 500 GLN A 123 -109.77 -111.80
REMARK 500 TRP A 124 -146.45 -84.06
REMARK 500 GLU A 146 23.54 85.08
REMARK 500 THR A 156 134.29 -176.50
REMARK 500 ASP A 192 -1.77 72.57
REMARK 500 ILE A 193 -57.96 -123.90
REMARK 500 SER A 242 -155.78 61.17
REMARK 500 TYR A 256 115.07 -166.45
REMARK 500 ALA A 259 124.09 -35.50
REMARK 500 GLN A 320 45.43 -84.64
REMARK 500 GLU A 332 -100.35 -70.70
REMARK 500 ASN A 420 36.17 -99.69
REMARK 500 ASP A 438 89.07 -166.58
REMARK 500 ASN A 450 78.34 -152.94
REMARK 500 ASN A 487 -32.87 -151.68
REMARK 500 ASP A 488 -16.20 110.39
REMARK 500 GLN A 508 98.76 -59.47
REMARK 500 ASP A 515 -175.60 -172.89
REMARK 500 TYR A 547 -68.10 -133.86
REMARK 500 GLN A 586 14.48 -140.14
REMARK 500 THR A 600 -85.19 -117.12
REMARK 500 SER A 630 -124.90 60.41
REMARK 500 ASP A 678 -101.51 -110.52
REMARK 500 ASN A 710 -70.98 -93.78
REMARK 500 GLN A 714 -53.16 -27.54
REMARK 500 ASP A 739 -163.91 -110.12
REMARK 500 GLN B 72 -77.44 -67.78
REMARK 500 ASN B 74 -17.80 60.75
REMARK 500 GLU B 82 -71.20 -66.15
REMARK 500 GLN B 123 -114.00 -127.44
REMARK 500 TRP B 124 -153.99 -82.53
REMARK 500 HIS B 162 43.25 -145.67
REMARK 500 ASP B 192 -1.97 67.52
REMARK 500 VAL B 207 -61.91 -105.78
REMARK 500 SER B 242 -165.22 61.96
REMARK 500 GLN B 320 43.42 -86.62
REMARK 500 THR B 401 54.69 -95.27
REMARK 500 THR B 411 -165.89 -122.28
REMARK 500 ASP B 438 97.41 -163.47
REMARK 500 PRO B 478 134.14 -31.93
REMARK 500 ASP B 488 10.19 81.87
REMARK 500 TYR B 547 -65.77 -122.72
REMARK 500 ARG B 597 36.78 -157.74
REMARK 500 THR B 600 -95.86 -103.70
REMARK 500
REMARK 500 THIS ENTRY HAS 120 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 772 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH C 778 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH D 790 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH D 791 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH D 795 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH C 797 DISTANCE = 5.00 ANGSTROMS
REMARK 525 HOH B 798 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH A 801 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH D 806 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 805 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH A 817 DISTANCE = 5.36 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10T A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10T B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 851
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10T C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10T D 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2811
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O95 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DPP4 BOUND TO TAK-100
DBREF 3O9V A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3O9V B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3O9V C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3O9V D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3O9V ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 3O9V PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 3O9V SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 3O9V PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 3O9V SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 3O9V PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 3O9V SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 3O9V ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 3O9V PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 3O9V GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 3O9V SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 3O9V HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 3O9V 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 3O9V ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN A 281 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN B 281 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN C 150 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN C 229 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN C 281 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN D 150 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN D 229 ASN GLYCOSYLATION SITE
MODRES 3O9V ASN D 281 ASN GLYCOSYLATION SITE
HET 10T A 1 23
HET NAG A1501 14
HET NAG A2291 14
HET NAG A2292 14
HET NAG A2811 14
HET NAG A2812 14
HET NAG A3211 14
HET 10T B 1 23
HET NAG B 851 14
HET NAG B1501 14
HET NAG B2191 14
HET NAG B2291 14
HET NAG B2292 14
HET NAG B2811 14
HET 10T C 1 23
HET NAG C1501 14
HET NAG C2291 14
HET NAG C2292 14
HET NAG C2811 14
HET 10T D 1 23
HET NAG D1501 14
HET NAG D2291 14
HET NAG D2292 14
HET NAG D2811 14
HETNAM 10T 5-(AMINOMETHYL)-2-METHYL-4-(4-METHYLPHENYL)-6-(2-
HETNAM 2 10T METHYLPROPYL)PYRIDINE-3-CARBOXIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN 10T TAK-986
FORMUL 5 10T 4(C19 H24 N2 O2)
FORMUL 6 NAG 20(C8 H15 N O6)
FORMUL 24 HOH *451(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 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 LEU A 504 1 8
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 LYS A 615 1 16
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 HIS A 712 VAL A 726 1 15
HELIX 18 18 SER A 744 PHE A 763 1 20
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 ASP B 274 LEU B 276 5 3
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 LEU B 504 1 8
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 VAL B 688 VAL B 698 5 11
HELIX 35 35 HIS B 712 GLY B 727 1 16
HELIX 36 36 SER B 744 PHE B 763 1 20
HELIX 37 37 THR C 44 LYS C 50 1 7
HELIX 38 38 ASP C 200 GLU C 206 1 7
HELIX 39 39 PRO C 290 ILE C 295 1 6
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 641 1 12
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 GLY C 727 1 16
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 GLU D 206 1 7
HELIX 55 55 PRO D 290 ILE D 295 1 6
HELIX 56 56 VAL D 341 GLN D 344 5 4
HELIX 57 57 GLU D 421 MET D 425 5 5
HELIX 58 58 ASN D 497 GLN D 505 1 9
HELIX 59 59 ASN D 562 THR D 570 1 9
HELIX 60 60 GLY D 587 HIS D 592 1 6
HELIX 61 61 ALA D 593 ASN D 595 5 3
HELIX 62 62 THR D 600 LYS D 615 1 16
HELIX 63 63 SER D 630 GLY D 641 1 12
HELIX 64 64 ARG D 658 TYR D 662 5 5
HELIX 65 65 ASP D 663 GLY D 672 1 10
HELIX 66 66 ASN D 679 SER D 686 1 8
HELIX 67 67 VAL D 688 VAL D 698 5 11
HELIX 68 68 HIS D 712 VAL D 726 1 15
HELIX 69 69 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 TYR A 68 LYS A 71 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ILE A 76 LEU A 77 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 VAL A 88 LEU A 90 -1 O LEU A 90 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 3 LEU A 164 TRP A 168 0
SHEET 2 D 3 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 3 D 3 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 LYS A 267 N GLN A 227
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 LYS A 250 N PHE A 240
SHEET 1 H 4 HIS A 298 TRP A 305 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 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 TRP A 305 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 TYR A 330 -1 O ASP A 326 N LEU A 313
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 ALA A 409
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 LEU A 479 N CYS A 472
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 VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
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 GLU A 699 N GLY A 650
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 PHE B 89 N ILE B 76
SHEET 1 P 4 ILE B 102 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 ASP B 133 N LEU B 116
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 ALA B 165 N THR B 156
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
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 GLN B 286 -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 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
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 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
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 PHE B 387 N PHE B 371
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 ILE B 434 N LEU B 415
SHEET 4 X 4 ASP B 438 CYS B 444 -1 O ASP B 438 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 ARG B 471 N SER B 458
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 Y 4 GLY B 490 GLU B 495 -1 O LEU B 491 N LEU B 482
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
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 ASP B 545 O ALA B 576
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O TRP B 627 N VAL B 546
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O ILE B 651 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 2 LYS C 41 THR C 42 0
SHEET 2 AA 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 AB 3 ARG C 61 TRP C 62 0
SHEET 2 AB 3 GLU C 67 TYR C 70 -1 O LEU C 69 N ARG C 61
SHEET 3 AB 3 LEU C 77 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 1 AC 3 ASP C 104 ILE C 107 0
SHEET 2 AC 3 PHE C 113 LYS C 122 -1 O GLU C 117 N ASP C 104
SHEET 3 AC 3 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 1 AD 4 TRP C 154 TRP C 157 0
SHEET 2 AD 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
SHEET 3 AD 4 ASP C 171 LYS C 175 -1 O TYR C 173 N TYR C 166
SHEET 4 AD 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AE 3 ILE C 194 ASN C 196 0
SHEET 2 AE 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AF 4 ILE C 194 ASN C 196 0
SHEET 2 AF 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AF 4 THR C 265 ASN C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AF 4 ILE C 285 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AG 2 LEU C 235 PHE C 240 0
SHEET 2 AG 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AH 4 HIS C 298 THR C 307 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O ARG C 310 N ALA C 306
SHEET 3 AH 4 TYR C 322 ASP C 331 -1 O VAL C 324 N TRP C 315
SHEET 4 AH 4 ARG C 336 CYS C 339 -1 O ARG C 336 N ASP C 331
SHEET 1 AI 4 HIS C 298 THR C 307 0
SHEET 2 AI 4 ARG C 310 ARG C 317 -1 O ARG C 310 N ALA C 306
SHEET 3 AI 4 TYR C 322 ASP C 331 -1 O VAL C 324 N TRP C 315
SHEET 4 AI 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AJ 4 HIS C 363 PHE C 364 0
SHEET 2 AJ 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AJ 4 ARG C 382 GLN C 388 -1 O HIS C 383 N ILE C 375
SHEET 4 AJ 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AK 4 VAL C 404 LEU C 410 0
SHEET 2 AK 4 TYR C 414 SER C 419 -1 O ILE C 418 N GLY C 406
SHEET 3 AK 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AK 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AL 4 TYR C 457 PHE C 461 0
SHEET 2 AL 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AL 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AL 4 GLY C 490 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AM 8 SER C 511 LEU C 519 0
SHEET 2 AM 8 THR C 522 LEU C 530 -1 O TYR C 526 N ASP C 515
SHEET 3 AM 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AM 8 TYR C 540 ASP C 545 1 N ASP C 545 O ALA C 576
SHEET 5 AM 8 VAL C 619 TRP C 629 1 O ASP C 620 N TYR C 540
SHEET 6 AM 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AM 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AM 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AN 2 LYS D 41 THR D 42 0
SHEET 2 AN 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AO 4 ARG D 61 TRP D 62 0
SHEET 2 AO 4 GLU D 67 LYS D 71 -1 O LEU D 69 N ARG D 61
SHEET 3 AO 4 ILE D 76 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AO 4 VAL D 88 LEU D 90 -1 O LEU D 90 N ILE D 76
SHEET 1 AP 3 ASP D 104 ILE D 107 0
SHEET 2 AP 3 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AP 3 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 1 AQ 4 THR D 152 TRP D 157 0
SHEET 2 AQ 4 LEU D 164 TRP D 168 -1 O VAL D 167 N GLN D 153
SHEET 3 AQ 4 ASP D 171 LYS D 175 -1 O TYR D 173 N TYR D 166
SHEET 4 AQ 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AR 3 ILE D 194 ASN D 196 0
SHEET 2 AR 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AR 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AS 4 ILE D 194 ASN D 196 0
SHEET 2 AS 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AS 4 THR D 265 ASN D 272 -1 O VAL D 271 N LEU D 223
SHEET 4 AS 4 ILE D 285 GLN D 286 -1 O ILE D 285 N VAL D 270
SHEET 1 AT 2 LEU D 235 PHE D 240 0
SHEET 2 AT 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AU 4 HIS D 298 THR D 307 0
SHEET 2 AU 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AU 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AU 4 TRP D 337 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 1 AV 4 HIS D 298 THR D 307 0
SHEET 2 AV 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AV 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AV 4 HIS D 345 MET D 348 -1 O GLU D 347 N SER D 323
SHEET 1 AW 4 HIS D 363 PHE D 364 0
SHEET 2 AW 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AW 4 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AW 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AX 4 VAL D 404 LEU D 410 0
SHEET 2 AX 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AX 4 ASN D 430 GLN D 435 -1 O ILE D 434 N LEU D 415
SHEET 4 AX 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AY 4 CYS D 454 PHE D 461 0
SHEET 2 AY 4 TYR D 467 PRO D 475 -1 O ARG D 471 N SER D 458
SHEET 3 AY 4 LEU D 479 SER D 484 -1 O THR D 481 N LEU D 470
SHEET 4 AY 4 GLY D 490 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AZ 8 SER D 511 LEU D 519 0
SHEET 2 AZ 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AZ 8 ILE D 574 ASP D 579 -1 O VAL D 575 N ILE D 529
SHEET 4 AZ 8 TYR D 540 ASP D 545 1 N ASP D 545 O ALA D 576
SHEET 5 AZ 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 542
SHEET 6 AZ 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AZ 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AZ 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 339 CYS A 328 1555 1555 2.04
SSBOND 2 CYS A 394 CYS A 385 1555 1555 2.06
SSBOND 3 CYS A 447 CYS A 444 1555 1555 2.04
SSBOND 4 CYS A 472 CYS A 454 1555 1555 2.08
SSBOND 5 CYS A 762 CYS A 649 1555 1555 2.04
SSBOND 6 CYS B 339 CYS B 328 1555 1555 2.05
SSBOND 7 CYS B 394 CYS B 385 1555 1555 2.04
SSBOND 8 CYS B 447 CYS B 444 1555 1555 2.04
SSBOND 9 CYS B 472 CYS B 454 1555 1555 2.05
SSBOND 10 CYS B 762 CYS B 649 1555 1555 2.08
SSBOND 11 CYS C 339 CYS C 328 1555 1555 2.05
SSBOND 12 CYS C 394 CYS C 385 1555 1555 2.05
SSBOND 13 CYS C 447 CYS C 444 1555 1555 2.05
SSBOND 14 CYS C 472 CYS C 454 1555 1555 2.08
SSBOND 15 CYS C 762 CYS C 649 1555 1555 2.07
SSBOND 16 CYS D 339 CYS D 328 1555 1555 2.05
SSBOND 17 CYS D 394 CYS D 385 1555 1555 2.05
SSBOND 18 CYS D 447 CYS D 444 1555 1555 2.06
SSBOND 19 CYS D 472 CYS D 454 1555 1555 2.08
SSBOND 20 CYS D 762 CYS D 649 1555 1555 2.04
LINK C1 NAG A1501 ND2 ASN A 150 1555 1555 1.46
LINK C1 NAG A2291 ND2 ASN A 229 1555 1555 1.45
LINK C1 NAG A2811 ND2 ASN A 281 1555 1555 1.47
LINK C1 NAG A3211 ND2 ASN A 321 1555 1555 1.45
LINK C1 NAG B 851 ND2 ASN B 85 1555 1555 1.47
LINK C1 NAG B1501 ND2 ASN B 150 1555 1555 1.47
LINK C1 NAG B2191 ND2 ASN B 219 1555 1555 1.46
LINK C1 NAG B2291 ND2 ASN B 229 1555 1555 1.45
LINK C1 NAG B2811 ND2 ASN B 281 1555 1555 1.47
LINK C1 NAG C1501 ND2 ASN C 150 1555 1555 1.48
LINK C1 NAG C2291 ND2 ASN C 229 1555 1555 1.46
LINK C1 NAG C2811 ND2 ASN C 281 1555 1555 1.46
LINK C1 NAG D1501 ND2 ASN D 150 1555 1555 1.46
LINK C1 NAG D2291 ND2 ASN D 229 1555 1555 1.46
LINK C1 NAG D2811 ND2 ASN D 281 1555 1555 1.47
LINK O4 NAG D2291 C1 NAG D2292 1555 1555 1.44
LINK O4 NAG B2291 C1 NAG B2292 1555 1555 1.44
LINK O4 NAG A2291 C1 NAG A2292 1555 1555 1.45
LINK O4 NAG C2291 C1 NAG C2292 1555 1555 1.45
LINK O4 NAG A2811 C1 NAG A2812 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 4.66
CISPEP 2 GLY B 474 PRO B 475 0 2.08
CISPEP 3 GLY C 474 PRO C 475 0 3.84
CISPEP 4 GLY D 474 PRO D 475 0 11.47
SITE 1 AC1 8 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 8 SER A 630 VAL A 656 TYR A 662 VAL A 711
SITE 1 AC2 3 ASN A 150 HOH A 829 HOH A 860
SITE 1 AC3 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC3 5 NAG A2292
SITE 1 AC4 2 GLU A 232 NAG A2291
SITE 1 AC5 4 VAL A 279 ASN A 281 HOH A 858 NAG A2812
SITE 1 AC6 1 NAG A2811
SITE 1 AC7 2 ASN A 321 SER A 349
SITE 1 AC8 12 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 AC8 12 TYR B 547 SER B 630 VAL B 656 TYR B 662
SITE 3 AC8 12 TYR B 666 ASN B 710 HIS B 740 HOH B 860
SITE 1 AC9 2 ASN B 85 SER B 87
SITE 1 BC1 6 ILE B 148 ASN B 150 HOH B 778 HOH B 789
SITE 2 BC1 6 HOH B 818 HOH B 870
SITE 1 BC2 5 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC2 5 HOH B 832
SITE 1 BC3 4 ASN B 229 THR B 231 GLU B 232 NAG B2292
SITE 1 BC4 2 GLU B 232 NAG B2291
SITE 1 BC5 3 TRP B 187 ASN B 281 HOH B 876
SITE 1 BC6 9 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 BC6 9 SER C 630 VAL C 656 TYR C 662 TYR C 666
SITE 3 BC6 9 HOH C 806
SITE 1 BC7 5 ARG C 147 ILE C 148 ASN C 150 HOH C 807
SITE 2 BC7 5 HOH C 827
SITE 1 BC8 4 ASN C 229 THR C 231 GLU C 232 NAG C2292
SITE 1 BC9 2 GLU C 232 NAG C2291
SITE 1 CC1 2 TRP C 187 ASN C 281
SITE 1 CC2 10 ARG D 125 GLU D 205 GLU D 206 ARG D 358
SITE 2 CC2 10 TYR D 547 SER D 630 VAL D 656 TYR D 662
SITE 3 CC2 10 TYR D 666 HIS D 740
SITE 1 CC3 2 ASN D 150 HOH D 826
SITE 1 CC4 5 ASN D 229 THR D 231 GLU D 232 LYS D 267
SITE 2 CC4 5 NAG D2292
SITE 1 CC5 3 GLU D 232 HOH D 868 NAG D2291
SITE 1 CC6 3 TRP D 187 ASN D 281 HOH D 846
CRYST1 122.166 122.886 144.909 90.00 114.59 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 0.008186 0.000000 0.003746 0.00000
SCALE2 0.000000 0.008138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007589 0.00000
TER 5958 PRO A 766
TER 11972 PRO B 766
TER 17930 PRO C 766
TER 23883 PRO D 766
MASTER 514 0 24 69 200 0 36 624702 4 427 228
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