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HEADER HYDROLASE/HYDROLASE INHIBITOR 27-JAN-14 3WQH
TITLE CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH ANAGLIPTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 39-766;
COMPND 5 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 7 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV
COMPND 8 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL
COMPND 9 PEPTIDASE IV SOLUBLE FORM;
COMPND 10 EC: 3.4.14.5;
COMPND 11 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: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: BOMBYX MORI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7091;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS DIABETES, BETA-PROPELLER, AMINOPEPTIDASE, MEMBRANE, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.S.WATANABE,S.OKADA,T.MOTOYAMA,R.TAKAHASHI,H.ADACHI,M.OKA
REVDAT 1 15-JUL-15 3WQH 0
JRNL AUTH Y.S.WATANABE,Y.YASUDA,Y.KOJIMA,S.OKADA,T.MOTOYAMA,
JRNL AUTH 2 R.TAKAHASHI,M.OKA
JRNL TITL ANAGLIPTIN, A POTENT DIPEPTIDYL PEPTIDASE IV INHIBITOR: ITS
JRNL TITL 2 SINGLE-CRYSTAL STRUCTURE AND ENZYME INTERACTIONS.
JRNL REF J ENZYME INHIB MED CHEM 1 2015
JRNL REFN ESSN 1475-6374
JRNL PMID 26147347
JRNL DOI 10.3109/14756366.2014.1002402
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PRIMEX 2.2
REMARK 3 AUTHORS : SCHRODINGER,LLC
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) : 47.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)/RMS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45508
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2275
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4550
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 228
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11926
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 239
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 56.52
REMARK 3 SOLVENT VOLUME (%) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.853
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.376
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETERS AND TOPOLOGY.
REMARK 3 FORCE FIELD : NULL
REMARK 3 PLANARITY WEIGHT : NULL
REMARK 3 SOLVENT MODEL : NULL
REMARK 3
REMARK 3 CLASH COUNT PER 100 RESIDUES.
REMARK 3 SEVERE : NULL
REMARK 3 OTHER : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3WQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB096664.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45509
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 49.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.1000
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) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 3BJM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 4000, 15% PEG 1000, 0.15M NA/K
REMARK 280 -PHOSPHATE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 209.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 209.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.49500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 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 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 GLY A 37
REMARK 465 PRO A 38
REMARK 465 GLY B 37
REMARK 465 PRO B 38
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 40 -20.72 87.85
REMARK 500 ASN A 51 47.95 77.34
REMARK 500 GLU A 73 -117.15 77.13
REMARK 500 ASN A 92 6.58 94.05
REMARK 500 SER A 93 -112.45 88.78
REMARK 500 THR A 94 26.61 -151.48
REMARK 500 PHE A 95 -57.30 -151.90
REMARK 500 PHE A 98 -16.13 -144.65
REMARK 500 ASN A 119 41.59 74.45
REMARK 500 GLN A 123 -112.76 -101.68
REMARK 500 TRP A 124 -144.68 -87.21
REMARK 500 ARG A 140 43.29 77.52
REMARK 500 ASN A 151 1.68 94.70
REMARK 500 HIS A 162 25.80 -149.03
REMARK 500 ILE A 185 -30.52 -133.89
REMARK 500 GLU A 191 115.79 -38.27
REMARK 500 ILE A 193 -74.57 -126.98
REMARK 500 ALA A 213 41.54 -141.08
REMARK 500 SER A 242 -162.14 71.92
REMARK 500 GLN A 320 42.91 -88.07
REMARK 500 PHE A 357 -41.45 -137.79
REMARK 500 ASP A 393 -171.21 74.42
REMARK 500 TRP A 402 169.54 170.46
REMARK 500 ASP A 413 -6.53 -141.51
REMARK 500 LYS A 423 -3.62 74.50
REMARK 500 LYS A 441 75.59 -107.37
REMARK 500 ASN A 450 75.14 -160.59
REMARK 500 SER A 473 28.25 -146.80
REMARK 500 ASN A 520 -107.50 -133.03
REMARK 500 TYR A 547 -68.59 -124.05
REMARK 500 ALA A 548 1.48 81.15
REMARK 500 CYS A 551 18.59 80.23
REMARK 500 ASN A 572 42.18 70.84
REMARK 500 TYR A 585 16.51 83.49
REMARK 500 ARG A 596 32.68 74.91
REMARK 500 ARG A 597 31.65 -164.70
REMARK 500 THR A 600 -87.17 -107.16
REMARK 500 SER A 630 -104.62 83.62
REMARK 500 ALA A 654 53.85 35.97
REMARK 500 PRO A 674 35.12 -75.44
REMARK 500 ASP A 678 -94.34 -120.00
REMARK 500 ASN A 679 26.16 -142.16
REMARK 500 ASN A 710 -86.31 -101.93
REMARK 500 ASP A 739 -157.66 -85.66
REMARK 500 ASN B 51 42.99 75.36
REMARK 500 GLU B 73 11.04 81.30
REMARK 500 PHE B 95 14.06 92.43
REMARK 500 GLN B 123 -104.50 -100.24
REMARK 500 TRP B 124 -141.65 -94.45
REMARK 500 ASN B 151 34.30 79.77
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 92 SER A 93 137.56
REMARK 500 PHE A 95 ASP A 96 -136.30
REMARK 500 ILE A 742 ALA A 743 -148.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 51 24.2 L L OUTSIDE RANGE
REMARK 500 ASN A 92 19.8 L L OUTSIDE RANGE
REMARK 500 SER A 93 21.4 L L OUTSIDE RANGE
REMARK 500 ARG A 140 24.9 L L OUTSIDE RANGE
REMARK 500 ASN A 151 22.3 L L OUTSIDE RANGE
REMARK 500 ASN A 170 24.8 L L OUTSIDE RANGE
REMARK 500 ASP A 192 23.5 L L OUTSIDE RANGE
REMARK 500 ASN A 497 25.0 L L OUTSIDE RANGE
REMARK 500 ALA A 548 23.6 L L OUTSIDE RANGE
REMARK 500 SER A 630 24.6 L L OUTSIDE RANGE
REMARK 500 ASP A 737 24.0 L L OUTSIDE RANGE
REMARK 500 ASN B 74 24.0 L L OUTSIDE RANGE
REMARK 500 PHE B 95 22.1 L L OUTSIDE RANGE
REMARK 500 ASN B 170 24.9 L L OUTSIDE RANGE
REMARK 500 ASP B 192 25.0 L L OUTSIDE RANGE
REMARK 500 GLU B 464 24.5 L L OUTSIDE RANGE
REMARK 500 ASP B 488 24.6 L L OUTSIDE RANGE
REMARK 500 GLU B 521 23.7 L L OUTSIDE RANGE
REMARK 500 ALA B 548 23.6 L L OUTSIDE RANGE
REMARK 500 TYR B 585 24.9 L L OUTSIDE RANGE
REMARK 500 SER B 630 23.0 L L OUTSIDE RANGE
REMARK 500 ASP B 737 22.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKK A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKK B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 801 BOUND
REMARK 800 TO ASN A 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 802 BOUND
REMARK 800 TO ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 803 BOUND
REMARK 800 TO ASN A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 804 BOUND
REMARK 800 TO ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 805 BOUND
REMARK 800 TO ASN A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 806 BOUND
REMARK 800 TO ASN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 801 BOUND
REMARK 800 TO ASN B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 802 BOUND
REMARK 800 TO ASN B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 803 BOUND
REMARK 800 TO ASN B 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 804 BOUND
REMARK 800 TO ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 805 BOUND
REMARK 800 TO ASN B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 806 BOUND
REMARK 800 TO ASN B 321
DBREF 3WQH A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3WQH B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3WQH GLY A 37 UNP P27487 EXPRESSION TAG
SEQADV 3WQH PRO A 38 UNP P27487 EXPRESSION TAG
SEQADV 3WQH GLY B 37 UNP P27487 EXPRESSION TAG
SEQADV 3WQH PRO B 38 UNP P27487 EXPRESSION TAG
SEQRES 1 A 730 GLY PRO SER ARG LYS THR TYR THR LEU THR ASP TYR LEU
SEQRES 2 A 730 LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP
SEQRES 3 A 730 ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN
SEQRES 4 A 730 ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL
SEQRES 5 A 730 PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER
SEQRES 6 A 730 ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE
SEQRES 7 A 730 LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER
SEQRES 8 A 730 TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG
SEQRES 9 A 730 GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN
SEQRES 10 A 730 TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR
SEQRES 11 A 730 VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN
SEQRES 12 A 730 LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP
SEQRES 13 A 730 ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU
SEQRES 14 A 730 GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO
SEQRES 15 A 730 ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR
SEQRES 16 A 730 GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU
SEQRES 17 A 730 SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO
SEQRES 18 A 730 LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL
SEQRES 19 A 730 VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR
SEQRES 20 A 730 SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY
SEQRES 21 A 730 ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU
SEQRES 22 A 730 ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR
SEQRES 23 A 730 SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY
SEQRES 24 A 730 ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET
SEQRES 25 A 730 SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU
SEQRES 26 A 730 PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE
SEQRES 27 A 730 ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE
SEQRES 28 A 730 GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY
SEQRES 29 A 730 THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP
SEQRES 30 A 730 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO
SEQRES 31 A 730 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR
SEQRES 32 A 730 THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU
SEQRES 33 A 730 ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA
SEQRES 34 A 730 LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO
SEQRES 35 A 730 LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU
SEQRES 36 A 730 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 A 730 GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 A 730 ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU
SEQRES 39 A 730 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 A 730 LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 A 730 THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 A 730 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 A 730 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 A 730 ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 A 730 ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN
SEQRES 46 A 730 LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 A 730 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 A 730 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 A 730 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 A 730 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 A 730 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 A 730 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 A 730 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 A 730 VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 A 730 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 A 730 TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 57 A 730 LEU PRO
SEQRES 1 B 730 GLY PRO SER ARG LYS THR TYR THR LEU THR ASP TYR LEU
SEQRES 2 B 730 LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP
SEQRES 3 B 730 ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN
SEQRES 4 B 730 ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL
SEQRES 5 B 730 PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER
SEQRES 6 B 730 ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE
SEQRES 7 B 730 LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER
SEQRES 8 B 730 TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG
SEQRES 9 B 730 GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN
SEQRES 10 B 730 TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR
SEQRES 11 B 730 VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN
SEQRES 12 B 730 LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP
SEQRES 13 B 730 ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU
SEQRES 14 B 730 GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO
SEQRES 15 B 730 ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR
SEQRES 16 B 730 GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU
SEQRES 17 B 730 SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO
SEQRES 18 B 730 LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL
SEQRES 19 B 730 VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR
SEQRES 20 B 730 SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY
SEQRES 21 B 730 ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU
SEQRES 22 B 730 ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR
SEQRES 23 B 730 SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY
SEQRES 24 B 730 ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET
SEQRES 25 B 730 SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU
SEQRES 26 B 730 PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE
SEQRES 27 B 730 ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE
SEQRES 28 B 730 GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY
SEQRES 29 B 730 THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP
SEQRES 30 B 730 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO
SEQRES 31 B 730 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR
SEQRES 32 B 730 THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU
SEQRES 33 B 730 ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA
SEQRES 34 B 730 LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO
SEQRES 35 B 730 LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU
SEQRES 36 B 730 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 B 730 GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 B 730 ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU
SEQRES 39 B 730 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 B 730 LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 B 730 THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 B 730 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 B 730 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 B 730 ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 B 730 ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN
SEQRES 46 B 730 LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 B 730 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 B 730 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 B 730 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 B 730 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 B 730 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 B 730 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 B 730 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 B 730 VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 B 730 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 B 730 TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 57 B 730 LEU PRO
MODRES 3WQH ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN A 281 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN B 321 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3WQH ASN B 281 ASN GLYCOSYLATION SITE
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 15
HET SKK A 808 28
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET SKK B 807 28
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SKK N-[2-({2-[(2S)-2-CYANOPYRROLIDIN-1-YL]-2-
HETNAM 2 SKK OXOETHYL}AMINO)-2-METHYLPROPYL]-2-METHYLPYRAZOLO[1,5-
HETNAM 3 SKK A]PYRIMIDINE-6-CARBOXAMIDE
HETSYN SKK ANAGLIPTIN
FORMUL 3 NAG 13(C8 H15 N O6)
FORMUL 10 SKK 2(C19 H25 N7 O2)
FORMUL 18 HOH *104(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 LYS A 463 ALA A 465 5 3
HELIX 7 7 ASN A 497 GLN A 505 1 9
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 MET A 616 1 17
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 PHE A 713 ASP A 725 1 13
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 LYS B 463 ALA B 465 5 3
HELIX 26 26 ASN B 497 GLN B 505 1 9
HELIX 27 27 ASN B 562 THR B 570 1 9
HELIX 28 28 GLY B 587 HIS B 592 1 6
HELIX 29 29 ALA B 593 ASN B 595 5 3
HELIX 30 30 THR B 600 MET B 616 1 17
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 ARG B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 SER B 686 1 8
HELIX 35 35 VAL B 688 VAL B 698 5 11
HELIX 36 36 HIS B 712 ASP B 725 1 14
HELIX 37 37 SER B 744 PHE B 763 1 20
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 B 4 ILE A 102 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 ILE A 102 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 ILE A 148 THR A 152 -1 O THR A 152 N ALA A 130
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
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 PHE A 269 N TYR A 225
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 ASN A 338 -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 HIS A 345 N MET A 325
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 ILE A 434 N LEU A 415
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 GLN A 469 N SER A 460
SHEET 3 L 4 TYR A 480 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 L 4 GLY A 490 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 M 8 SER A 511 ILE A 518 0
SHEET 2 M 8 LYS A 523 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 ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O TRP A 627 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 ILE A 703 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 4 LEU B 60 TRP B 62 0
SHEET 2 N 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 N 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 O 4 ASP B 104 ILE B 107 0
SHEET 2 O 4 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 O 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 O 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 P 4 TRP B 154 TRP B 157 0
SHEET 2 P 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 P 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 P 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 Q 3 ILE B 194 ASN B 196 0
SHEET 2 Q 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 4 ILE B 194 ASN B 196 0
SHEET 2 R 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 4 THR B 265 ASN B 272 -1 O VAL B 271 N LEU B 223
SHEET 4 R 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 S 2 LEU B 235 PHE B 240 0
SHEET 2 S 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 T 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 U 4 HIS B 298 THR B 307 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 VAL B 324 N TRP B 315
SHEET 4 U 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 V 4 HIS B 363 PHE B 364 0
SHEET 2 V 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 V 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 V 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 W 4 VAL B 404 LEU B 410 0
SHEET 2 W 4 TYR B 414 SER B 419 -1 O ILE B 418 N ILE B 405
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 W 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 X 4 TYR B 457 PHE B 461 0
SHEET 2 X 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 X 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 X 4 GLY B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Y 8 SER B 511 LEU B 519 0
SHEET 2 Y 8 THR B 522 LEU B 530 -1 O MET B 528 N LYS B 513
SHEET 3 Y 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Y 8 TYR B 540 VAL B 546 1 N LEU B 543 O ALA B 576
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Y 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Y 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Y 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.01
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.07
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.04
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.08
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.04
LINK ND2 ASN A 321 C1 NAG A 806 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG A 804 1555 1555 1.45
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 281 C1 NAG A 805 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B 806 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN B 229 C1 NAG B 804 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B 805 1555 1555 1.46
CISPEP 1 GLY A 474 PRO A 475 0 8.14
CISPEP 2 GLY B 474 PRO B 475 0 12.70
SITE 1 AC1 3 NAG A 804 SER B 690 ASN B 694
SITE 1 AC2 12 ARG A 125 GLU A 205 GLU A 206 PHE A 357
SITE 2 AC2 12 TYR A 547 TYR A 585 SER A 630 TYR A 631
SITE 3 AC2 12 TYR A 662 TYR A 666 ASN A 710 HOH A 913
SITE 1 AC3 11 GLU B 205 GLU B 206 PHE B 357 ARG B 358
SITE 2 AC3 11 TYR B 547 TYR B 585 SER B 630 TYR B 631
SITE 3 AC3 11 TYR B 662 TYR B 666 ASN B 710
SITE 1 AC4 6 VAL A 78 ASN A 85 SER A 86 SER A 87
SITE 2 AC4 6 GLN A 388 THR A 395
SITE 1 AC5 4 ASN A 119 ASN A 150 ILE A 518 HOH A 941
SITE 1 AC6 3 ASN A 219 THR A 221 GLU A 309
SITE 1 AC7 6 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC7 6 LYS A 267 NAG A 807
SITE 1 AC8 2 TRP A 187 ASN A 281
SITE 1 AC9 2 ASN A 321 ARG A 596
SITE 1 BC1 6 VAL B 78 ASN B 85 SER B 86 SER B 87
SITE 2 BC1 6 GLN B 388 THR B 395
SITE 1 BC2 8 HIS B 100 TYR B 118 SER B 131 TYR B 132
SITE 2 BC2 8 ASP B 133 ARG B 147 ILE B 148 ASN B 150
SITE 1 BC3 5 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC3 5 HOH B1026
SITE 1 BC4 4 ASN B 229 THR B 231 GLU B 232 LYS B 267
SITE 1 BC5 3 TRP B 187 VAL B 279 ASN B 281
SITE 1 BC6 3 ASN B 321 MET B 348 ARG B 596
CRYST1 65.160 68.990 419.600 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015347 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014495 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002383 0.00000
TER 5964 PRO A 766
TER 11928 PRO B 766
MASTER 424 0 15 37 102 0 24 612269 2 271 114
END |