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HEADER HYDROLASE/HYDROLASE INHIBITOR 13-JAN-11 3QBJ
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 6 TP103, DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: 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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS DIABETES MELLITUS, DIPEPTIDYL-PEPTIDASE IV INHIBITOR, HYPOGLYCEMIC
KEYWDS 2 AGENT, PYRROLIDINES, SPRAGUE-DAWLEY, STRUCTURE-ACTIVITY
KEYWDS 3 RELATIONSHIP, HYDROLASE, GLYCOSYLATION, HYDROLASE-HYDROLASE
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.P.LIU
REVDAT 1 25-JAN-12 3QBJ 0
JRNL AUTH S.P.LIU
JRNL TITL CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH
JRNL TITL 2 INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.3
REMARK 3 NUMBER OF REFLECTIONS : 78758
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 3918
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.27
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.26
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3919
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2440
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3724
REMARK 3 BIN R VALUE (WORKING SET) : 0.2432
REMARK 3 BIN FREE R VALUE : 0.2588
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.98
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 195
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11914
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 18.50950
REMARK 3 B22 (A**2) : -35.32870
REMARK 3 B33 (A**2) : 16.81920
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.46
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.896
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12483 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17004 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4116 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 321 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1816 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12483 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1632 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 13264 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.99
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A 39 A 796
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7180 16.3799 27.6709
REMARK 3 T TENSOR
REMARK 3 T11: -0.2752 T22: 0.3103
REMARK 3 T33: -0.1729 T12: 0.0095
REMARK 3 T13: 0.0039 T23: 0.1827
REMARK 3 L TENSOR
REMARK 3 L11: 0.6264 L22: 0.4177
REMARK 3 L33: 1.8418 L12: -0.0404
REMARK 3 L13: -0.1631 L23: -0.4122
REMARK 3 S TENSOR
REMARK 3 S11: 0.0411 S12: 0.2268 S13: 0.1080
REMARK 3 S21: -0.0336 S22: 0.0268 S23: 0.0086
REMARK 3 S31: 0.0228 S32: -0.0822 S33: -0.0679
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: B 39 B 796
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0608 -2.5173 78.4587
REMARK 3 T TENSOR
REMARK 3 T11: -0.2700 T22: -0.1414
REMARK 3 T33: -0.2778 T12: 0.0125
REMARK 3 T13: 0.0217 T23: 0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 0.9531 L22: 0.5814
REMARK 3 L33: 2.0308 L12: 0.1197
REMARK 3 L13: -0.4564 L23: -0.4377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0852 S13: 0.0250
REMARK 3 S21: 0.0850 S22: 0.1245 S23: 0.0564
REMARK 3 S31: 0.0884 S32: -0.2422 S33: -0.1265
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QBJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
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 : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79656
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 42.409
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.3
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : 0.10100
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : 0.39200
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 32.87550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 212.08000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.54100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 212.08000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.87550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.54100
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: 6970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 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 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 ASP A 38
REMARK 465 LEU A 767
REMARK 465 VAL A 768
REMARK 465 PRO A 769
REMARK 465 ARG A 770
REMARK 465 GLY A 771
REMARK 465 SER A 772
REMARK 465 HIS A 773
REMARK 465 HIS A 774
REMARK 465 HIS A 775
REMARK 465 HIS A 776
REMARK 465 HIS A 777
REMARK 465 HIS A 778
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 THR B 36
REMARK 465 ALA B 37
REMARK 465 ASP B 38
REMARK 465 LEU B 767
REMARK 465 VAL B 768
REMARK 465 PRO B 769
REMARK 465 ARG B 770
REMARK 465 GLY B 771
REMARK 465 SER B 772
REMARK 465 HIS B 773
REMARK 465 HIS B 774
REMARK 465 HIS B 775
REMARK 465 HIS B 776
REMARK 465 HIS B 777
REMARK 465 HIS B 778
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 O4 NAG A 796 O5 NAG A 798 2.17
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 ARG A 40 -145.02 -115.40
REMARK 500 SER A 64 -168.04 -165.25
REMARK 500 HIS A 66 -2.41 -145.08
REMARK 500 GLN A 72 68.08 -100.68
REMARK 500 GLU A 73 107.91 48.91
REMARK 500 GLN A 123 -100.58 -113.16
REMARK 500 TRP A 124 -151.78 -95.39
REMARK 500 ASN A 151 36.69 70.53
REMARK 500 HIS A 162 30.42 -144.13
REMARK 500 ILE A 193 -62.77 -121.84
REMARK 500 VAL A 207 -60.82 -103.20
REMARK 500 SER A 242 -154.83 61.83
REMARK 500 GLN A 320 28.85 -70.06
REMARK 500 SER A 333 30.40 -95.82
REMARK 500 SER A 334 -29.89 -160.34
REMARK 500 LYS A 392 -73.60 -46.05
REMARK 500 ASP A 393 -143.71 -115.75
REMARK 500 ASN A 450 82.50 -161.33
REMARK 500 TYR A 547 -72.47 -131.77
REMARK 500 ARG A 596 14.00 59.63
REMARK 500 ARG A 597 44.86 -141.38
REMARK 500 THR A 600 -89.55 -118.14
REMARK 500 SER A 630 -113.58 61.96
REMARK 500 ALA A 654 54.05 39.92
REMARK 500 ASP A 678 -95.52 -91.61
REMARK 500 ASN A 710 -68.97 -98.54
REMARK 500 GLU B 73 102.56 41.84
REMARK 500 GLN B 123 -100.18 -113.27
REMARK 500 TRP B 124 -151.19 -95.47
REMARK 500 ASN B 151 36.68 70.12
REMARK 500 HIS B 162 30.08 -144.77
REMARK 500 ILE B 193 -62.64 -121.69
REMARK 500 VAL B 207 -60.76 -103.19
REMARK 500 SER B 242 -156.53 61.23
REMARK 500 GLN B 320 34.83 -69.39
REMARK 500 SER B 334 -31.56 -157.76
REMARK 500 LYS B 392 -71.92 -47.22
REMARK 500 ASP B 393 -143.50 -115.20
REMARK 500 ASN B 450 82.78 -160.09
REMARK 500 TYR B 547 -71.38 -133.10
REMARK 500 ARG B 597 54.68 -142.56
REMARK 500 THR B 600 -89.53 -118.25
REMARK 500 SER B 630 -114.83 65.04
REMARK 500 ASP B 678 -97.28 -115.67
REMARK 500 ASN B 710 -68.07 -97.38
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 ARG A 40 23.1 L L OUTSIDE RANGE
REMARK 500 LYS A 41 23.6 L L OUTSIDE RANGE
REMARK 500 ILE A 389 22.0 L L OUTSIDE RANGE
REMARK 500 LYS A 392 22.1 L L OUTSIDE RANGE
REMARK 500 HIS A 682 24.9 L L OUTSIDE RANGE
REMARK 500 LYS B 41 23.7 L L OUTSIDE RANGE
REMARK 500 ASN B 92 23.7 L L OUTSIDE RANGE
REMARK 500 VAL B 202 25.0 L L OUTSIDE RANGE
REMARK 500 GLN B 320 24.8 L L OUTSIDE RANGE
REMARK 500 ILE B 389 21.5 L L OUTSIDE RANGE
REMARK 500 LYS B 392 23.6 L L OUTSIDE RANGE
REMARK 500 VAL B 486 24.0 L L OUTSIDE RANGE
REMARK 500 VAL B 558 22.3 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 794
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 796
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 798
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 799
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXZ A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 794
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 796
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXZ B 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F8S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH INHIBITOR
DBREF 3QBJ A 31 766 UNP P27487 DPP4_HUMAN 31 766
DBREF 3QBJ B 31 766 UNP P27487 DPP4_HUMAN 31 766
SEQADV 3QBJ ALA A 150 UNP P27487 ASN 150 ENGINEERED MUTATION
SEQADV 3QBJ ALA A 520 UNP P27487 ASN 520 ENGINEERED MUTATION
SEQADV 3QBJ LEU A 767 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ VAL A 768 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ PRO A 769 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ ARG A 770 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ GLY A 771 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ SER A 772 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS A 774 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS A 775 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS A 776 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS A 777 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS A 778 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ ALA B 150 UNP P27487 ASN 150 ENGINEERED MUTATION
SEQADV 3QBJ ALA B 520 UNP P27487 ASN 520 ENGINEERED MUTATION
SEQADV 3QBJ LEU B 767 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ VAL B 768 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ PRO B 769 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ ARG B 770 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ GLY B 771 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ SER B 772 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS B 773 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS B 774 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS B 775 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS B 776 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS B 777 UNP P27487 EXPRESSION TAG
SEQADV 3QBJ HIS B 778 UNP P27487 EXPRESSION TAG
SEQRES 1 A 748 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 A 748 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 A 748 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 A 748 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 A 748 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 A 748 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 A 748 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 A 748 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 A 748 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 A 748 ILE PRO ALA ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 A 748 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 A 748 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 A 748 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 A 748 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 A 748 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 A 748 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 A 748 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 A 748 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 A 748 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 A 748 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 A 748 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 A 748 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 A 748 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 A 748 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 A 748 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 A 748 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 A 748 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 A 748 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 A 748 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 A 748 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 A 748 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 A 748 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 A 748 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 A 748 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 A 748 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 A 748 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 A 748 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 A 748 LYS LYS LEU ASP PHE ILE ILE LEU ALA GLU THR LYS PHE
SEQRES 39 A 748 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 A 748 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 A 748 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 A 748 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 A 748 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 A 748 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 A 748 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 A 748 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 A 748 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 A 748 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 A 748 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 A 748 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 A 748 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 A 748 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 A 748 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 A 748 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 A 748 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 A 748 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 A 748 ILE LYS GLN CYS PHE SER LEU PRO LEU VAL PRO ARG GLY
SEQRES 58 A 748 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 748 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 B 748 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 B 748 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 B 748 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 B 748 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 B 748 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 B 748 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 B 748 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 B 748 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 B 748 ILE PRO ALA ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 B 748 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 B 748 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 B 748 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 B 748 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 B 748 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 B 748 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 B 748 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 B 748 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 B 748 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 B 748 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 B 748 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 B 748 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 B 748 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 B 748 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 B 748 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 B 748 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 B 748 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 B 748 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 B 748 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 B 748 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 B 748 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 B 748 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 B 748 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 B 748 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 B 748 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 B 748 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 B 748 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 B 748 LYS LYS LEU ASP PHE ILE ILE LEU ALA GLU THR LYS PHE
SEQRES 39 B 748 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 B 748 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 B 748 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 B 748 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 B 748 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 B 748 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 B 748 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 B 748 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 B 748 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 B 748 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 B 748 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 B 748 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 B 748 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 B 748 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 B 748 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 B 748 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 B 748 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 B 748 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 B 748 ILE LYS GLN CYS PHE SER LEU PRO LEU VAL PRO ARG GLY
SEQRES 58 B 748 SER HIS HIS HIS HIS HIS HIS
MODRES 3QBJ ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3QBJ ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3QBJ ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3QBJ ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3QBJ ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3QBJ ASN A 321 ASN GLYCOSYLATION SITE
HET NAG A 794 14
HET NAG A 797 14
HET NAG A 796 14
HET NAG A 798 14
HET BMA A 802 11
HET MAN A 803 11
HET NAG A 799 14
HET NAG A 800 14
HET NXZ A 900 25
HET NAG B 794 14
HET NAG B 797 14
HET NAG B 796 14
HET NXZ B 900 25
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM NXZ 1-[(3S,4S)-4-AMINO-1-(6-PHENYLPYRIMIDIN-4-YL)
HETNAM 2 NXZ PYRROLIDIN-3-YL]PIPERIDIN-2-ONE
FORMUL 3 NAG 9(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN C6 H12 O6
FORMUL 7 NXZ 2(C19 H23 N5 O)
FORMUL 11 HOH *71(H2 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 SER A 93 ASP A 96 5 4
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 LEU A 340 GLN A 344 5 5
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 LYS A 463 ALA A 465 5 3
HELIX 8 8 ASN A 497 ASN A 506 1 10
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 PHE A 713 ASP A 725 1 13
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 LYS B 50 1 7
HELIX 21 21 SER B 93 ASP B 96 5 4
HELIX 22 22 ASP B 200 VAL B 207 1 8
HELIX 23 23 PRO B 290 ILE B 295 1 6
HELIX 24 24 LEU B 340 GLN B 344 5 5
HELIX 25 25 GLU B 421 MET B 425 5 5
HELIX 26 26 LYS B 463 ALA B 465 5 3
HELIX 27 27 ASN B 497 ASN B 506 1 10
HELIX 28 28 ASN B 562 THR B 570 1 9
HELIX 29 29 GLY B 587 HIS B 592 1 6
HELIX 30 30 ALA B 593 ASN B 595 5 3
HELIX 31 31 THR B 600 MET B 616 1 17
HELIX 32 32 SER B 630 GLY B 641 1 12
HELIX 33 33 ARG B 658 TYR B 662 5 5
HELIX 34 34 ASP B 663 GLY B 672 1 10
HELIX 35 35 ASN B 679 SER B 686 1 8
HELIX 36 36 VAL B 688 VAL B 698 5 11
HELIX 37 37 PHE B 713 ASP B 725 1 13
HELIX 38 38 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 LYS A 71 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 A 4 SER A 86 GLU A 91 -1 O LEU A 90 N ILE A 76
SHEET 1 B 4 ASP A 104 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 TRP A 154 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 E 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 G 4 HIS A 298 TRP A 305 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 G 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
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 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 CYS A 394 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 4 LEU B 60 TRP B 62 0
SHEET 2 M 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 M 4 ASN B 75 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 M 4 SER B 86 GLU B 91 -1 O PHE B 89 N ILE B 76
SHEET 1 N 4 ASP B 104 ILE B 107 0
SHEET 2 N 4 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 N 4 TYR B 128 ASP B 136 -1 O ASP B 133 N LEU B 116
SHEET 4 N 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 TRP B 154 TRP B 157 0
SHEET 2 O 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 O 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 O 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 P 3 ILE B 194 ASN B 196 0
SHEET 2 P 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 P 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 Q 4 ILE B 194 ASN B 196 0
SHEET 2 Q 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 Q 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 R 2 LEU B 235 PHE B 240 0
SHEET 2 R 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 S 4 HIS B 298 TRP B 305 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 S 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 S 4 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 1 T 4 HIS B 298 TRP B 305 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 ASP B 326 N LEU B 313
SHEET 4 T 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 U 4 HIS B 363 PHE B 364 0
SHEET 2 U 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 U 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 U 4 CYS B 394 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 V 4 VAL B 404 LEU B 410 0
SHEET 2 V 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 V 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 W 4 TYR B 457 PHE B 461 0
SHEET 2 W 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 W 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 W 4 LYS B 489 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 X 8 SER B 511 LEU B 519 0
SHEET 2 X 8 THR B 522 LEU B 530 -1 O TYR B 526 N ASP B 515
SHEET 3 X 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 X 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 X 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 544
SHEET 6 X 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 X 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 X 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 2.06
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.06
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.08
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.06
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.10
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
LINK O4 NAG A 796 C1 NAG A 798 1555 1555 1.38
LINK ND2 ASN A 219 C1 NAG A 799 1555 1555 1.43
LINK ND2 ASN A 85 C1 NAG A 794 1555 1555 1.45
LINK O4 NAG A 798 C1 BMA A 802 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG A 796 1555 1555 1.46
LINK O4 NAG B 794 C1 NAG B 797 1555 1555 1.46
LINK ND2 ASN B 229 C1 NAG B 796 1555 1555 1.46
LINK ND2 ASN B 85 C1 NAG B 794 1555 1555 1.46
LINK O4 NAG A 794 C1 NAG A 797 1555 1555 1.49
LINK ND2 ASN A 321 C1 NAG A 800 1555 1555 1.52
LINK O3 BMA A 802 C1 MAN A 803 1555 1555 1.54
CISPEP 1 GLY A 474 PRO A 475 0 2.36
CISPEP 2 GLY B 474 PRO B 475 0 1.74
SITE 1 AC1 8 VAL A 78 ASN A 85 SER A 86 SER A 87
SITE 2 AC1 8 TYR A 386 GLN A 388 THR A 395 NAG A 797
SITE 1 AC2 1 NAG A 794
SITE 1 AC3 6 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC3 6 LYS A 267 NAG A 798
SITE 1 AC4 3 GLU A 232 NAG A 796 BMA A 802
SITE 1 AC5 2 NAG A 798 MAN A 803
SITE 1 AC6 2 BMA A 802 SER B 690
SITE 1 AC7 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC8 2 ASN A 321 SER A 349
SITE 1 AC9 11 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC9 11 PHE A 357 ARG A 358 TYR A 547 TYR A 662
SITE 3 AC9 11 TYR A 666 ASN A 710 VAL A 711
SITE 1 BC1 9 GLU B 67 VAL B 78 ASN B 85 SER B 86
SITE 2 BC1 9 SER B 87 TYR B 386 GLN B 388 THR B 395
SITE 3 BC1 9 NAG B 797
SITE 1 BC2 2 LYS B 391 NAG B 794
SITE 1 BC3 5 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 BC3 5 LYS B 267
SITE 1 BC4 11 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 BC4 11 PHE B 357 ARG B 358 TYR B 547 TYR B 662
SITE 3 BC4 11 TYR B 666 ASN B 710 VAL B 711
CRYST1 65.751 69.082 424.160 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 0.015209 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002358 0.00000
TER 5958 PRO A 766
TER 11916 PRO B 766
MASTER 454 0 13 38 98 0 22 612183 2 224 116
END |