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HEADER HYDROLASE 31-MAR-16 5J3J
TITLE CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH HL1
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,TP103;
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: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HUMAN DPP-IV, PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.WU,H.LI,Z.ZHAO,L.ZHU,H.XU,S.LI
REVDAT 1 05-APR-17 5J3J 0
JRNL AUTH F.WU,H.LI,Z.ZHAO,L.ZHU,H.XU,S.LI
JRNL TITL CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH HL1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 42328
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) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2248
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) : 2879
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.3530
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 : 131
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.78000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : 0.58000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.07000
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): 0.455
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.330
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.303
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.863
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.798
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12411 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11181 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16901 ; 0.952 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25670 ; 0.675 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1452 ; 5.794 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 616 ;33.857 ;23.961
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1992 ;13.355 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;13.611 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1787 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14040 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3076 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5814 ; 0.909 ; 3.343
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5813 ; 0.909 ; 3.342
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7264 ; 1.649 ; 5.012
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7265 ; 1.649 ; 5.013
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6597 ; 0.605 ; 3.397
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6598 ; 0.604 ; 3.397
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9638 ; 1.127 ; 5.061
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 14182 ; 2.687 ;26.232
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 14173 ; 2.682 ;26.235
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 : NULL
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 5J3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44595
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 57.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 8, 18% PEG 3350, 200MM
REMARK 280 NACL, EVAPORATION, TEMPERATURE 289K
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 63.41000
REMARK 290 SMTRY3 2 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: 5680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 HIS A 773
REMARK 465 GLY B 767
REMARK 465 HIS B 768
REMARK 465 HIS B 769
REMARK 465 HIS B 770
REMARK 465 HIS B 771
REMARK 465 HIS B 772
REMARK 465 HIS B 773
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 631 CE1 TYR A 631 CZ -0.087
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 ASN A 51 50.88 72.91
REMARK 500 ASN A 74 -28.43 68.64
REMARK 500 TYR A 83 -58.67 -125.01
REMARK 500 ASN A 85 97.43 -32.65
REMARK 500 SER A 93 -111.75 -74.91
REMARK 500 THR A 94 -68.13 57.12
REMARK 500 PHE A 95 37.19 -97.59
REMARK 500 GLN A 123 -108.30 -104.52
REMARK 500 TRP A 124 -158.35 -88.33
REMARK 500 TYR A 128 -175.40 -170.60
REMARK 500 ARG A 140 50.15 36.67
REMARK 500 HIS A 162 31.00 -147.23
REMARK 500 ILE A 193 -61.62 -137.22
REMARK 500 VAL A 207 -62.60 -127.26
REMARK 500 SER A 242 -162.79 66.92
REMARK 500 SER A 275 40.70 -103.38
REMARK 500 GLN A 320 40.47 -91.16
REMARK 500 ASN A 450 86.74 -163.36
REMARK 500 GLN A 508 85.89 -69.27
REMARK 500 PRO A 510 -169.97 -77.51
REMARK 500 TYR A 547 -64.88 -130.30
REMARK 500 ARG A 596 12.19 58.03
REMARK 500 ARG A 597 47.89 -145.84
REMARK 500 THR A 600 -92.27 -99.35
REMARK 500 SER A 630 -123.01 81.28
REMARK 500 ASP A 678 -89.97 -106.69
REMARK 500 ASN A 679 18.25 -146.45
REMARK 500 ASN A 710 -74.34 -104.18
REMARK 500 GLN A 714 -54.24 -26.02
REMARK 500 ASN B 51 49.64 35.66
REMARK 500 GLU B 73 15.24 59.35
REMARK 500 ASN B 74 -9.14 78.21
REMARK 500 ASN B 85 80.27 -0.22
REMARK 500 GLN B 123 -101.33 -107.86
REMARK 500 TRP B 124 -145.73 -95.52
REMARK 500 LEU B 137 -60.77 71.65
REMARK 500 HIS B 162 40.24 -156.48
REMARK 500 LYS B 190 116.69 -164.72
REMARK 500 ILE B 193 -63.32 -125.07
REMARK 500 VAL B 207 -63.31 -125.23
REMARK 500 SER B 242 -164.23 68.54
REMARK 500 SER B 275 43.58 -83.67
REMARK 500 THR B 307 -158.13 -135.94
REMARK 500 GLN B 320 37.46 -90.14
REMARK 500 ARG B 358 165.19 177.66
REMARK 500 THR B 365 -177.53 -69.03
REMARK 500 ASN B 377 -164.11 -77.55
REMARK 500 ASN B 420 41.72 -107.94
REMARK 500 GLU B 521 -28.93 66.33
REMARK 500 TYR B 547 -65.73 -126.92
REMARK 500
REMARK 500 THIS ENTRY HAS 58 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 A 959 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 937 DISTANCE = 6.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HL1 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HL1 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 803 through MAN B 806 bound to ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 802 bound
REMARK 800 to ASN B 281
DBREF 5J3J A 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 5J3J B 40 766 UNP P27487 DPP4_HUMAN 40 766
SEQADV 5J3J GLY A 767 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS A 772 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 5J3J GLY B 767 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS B 768 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS B 769 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS B 770 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS B 771 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS B 772 UNP P27487 EXPRESSION TAG
SEQADV 5J3J HIS B 773 UNP P27487 EXPRESSION TAG
SEQRES 1 A 734 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 A 734 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 A 734 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 A 734 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 A 734 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 A 734 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 A 734 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 A 734 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 A 734 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 A 734 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 A 734 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 A 734 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 A 734 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 A 734 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 A 734 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 A 734 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 A 734 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 A 734 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 A 734 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 A 734 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 A 734 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 A 734 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 A 734 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 A 734 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 A 734 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 A 734 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 A 734 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 A 734 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 A 734 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 A 734 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 A 734 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 A 734 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 A 734 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 A 734 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 A 734 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 A 734 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 A 734 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 A 734 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 A 734 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 A 734 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 A 734 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 A 734 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 A 734 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 A 734 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 A 734 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 A 734 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 A 734 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 A 734 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 A 734 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 A 734 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 A 734 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 A 734 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 A 734 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 A 734 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 A 734 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 A 734 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO GLY
SEQRES 57 A 734 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 734 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 B 734 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 B 734 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 B 734 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 B 734 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 B 734 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 B 734 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 B 734 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 B 734 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 B 734 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 B 734 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 B 734 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 B 734 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 B 734 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 B 734 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 B 734 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 B 734 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 B 734 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 B 734 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 B 734 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 B 734 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 B 734 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 B 734 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 B 734 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 B 734 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 B 734 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 B 734 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 B 734 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 B 734 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 B 734 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 B 734 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 B 734 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 B 734 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 B 734 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 B 734 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 B 734 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 B 734 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 B 734 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 B 734 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 B 734 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 B 734 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 B 734 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 B 734 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 B 734 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 B 734 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 B 734 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 B 734 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 B 734 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 B 734 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 B 734 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 B 734 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 B 734 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 B 734 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 B 734 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 B 734 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 B 734 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO GLY
SEQRES 57 B 734 HIS HIS HIS HIS HIS HIS
HET HL1 A 801 28
HET NAG A 802 14
HET HL1 B 801 28
HET NAG B 802 14
HET NAG B 803 14
HET MAN B 804 11
HET MAN B 805 11
HET MAN B 806 11
HETNAM HL1 (2~{S},3~{R})-8,9-DIMETHOXY-3-[2,4,5-TRIS(FLUORANYL)
HETNAM 2 HL1 PHENYL]-2,3-DIHYDRO-1~{H}-BENZO[F]CHROMEN-2-AMINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
FORMUL 3 HL1 2(C21 H18 F3 N O3)
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 7 MAN 3(C6 H12 O6)
FORMUL 8 HOH *96(H2 O)
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 ASP A 200 VAL A 207 1 8
HELIX 3 AA3 PRO A 290 ILE A 295 1 6
HELIX 4 AA4 VAL A 341 GLN A 344 5 4
HELIX 5 AA5 GLU A 421 MET A 425 5 5
HELIX 6 AA6 ASN A 497 LEU A 504 1 8
HELIX 7 AA7 ASN A 562 THR A 570 1 9
HELIX 8 AA8 GLY A 587 HIS A 592 1 6
HELIX 9 AA9 ALA A 593 ASN A 595 5 3
HELIX 10 AB1 THR A 600 LYS A 615 1 16
HELIX 11 AB2 SER A 630 GLY A 641 1 12
HELIX 12 AB3 ARG A 658 TYR A 662 5 5
HELIX 13 AB4 ASP A 663 GLY A 672 1 10
HELIX 14 AB5 ASN A 679 SER A 686 1 8
HELIX 15 AB6 VAL A 688 VAL A 698 5 11
HELIX 16 AB7 HIS A 712 VAL A 726 1 15
HELIX 17 AB8 SER A 744 PHE A 763 1 20
HELIX 18 AB9 THR B 44 LYS B 50 1 7
HELIX 19 AC1 GLU B 91 ASP B 96 5 6
HELIX 20 AC2 ASP B 200 VAL B 207 1 8
HELIX 21 AC3 PRO B 290 ILE B 295 1 6
HELIX 22 AC4 VAL B 341 GLN B 344 5 4
HELIX 23 AC5 GLU B 421 MET B 425 5 5
HELIX 24 AC6 ASN B 497 GLN B 505 1 9
HELIX 25 AC7 ASN B 562 THR B 570 1 9
HELIX 26 AC8 GLY B 587 HIS B 592 1 6
HELIX 27 AC9 ALA B 593 ASN B 595 5 3
HELIX 28 AD1 THR B 600 MET B 616 1 17
HELIX 29 AD2 SER B 630 GLY B 643 1 14
HELIX 30 AD3 ARG B 658 TYR B 662 5 5
HELIX 31 AD4 ASP B 663 GLY B 672 1 10
HELIX 32 AD5 ASN B 679 SER B 686 1 8
HELIX 33 AD6 THR B 687 VAL B 698 5 12
HELIX 34 AD7 HIS B 712 VAL B 726 1 15
HELIX 35 AD8 SER B 744 PHE B 763 1 20
SHEET 1 AA1 2 LYS A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 AA2 4 LEU A 60 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA2 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AA3 4 ILE A 102 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 TRP A 154 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 AA4 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASN A 272 -1 O VAL A 271 N LEU A 223
SHEET 4 AA6 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O VAL A 324 N TRP A 315
SHEET 4 AA8 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA9 4 TYR A 322 ASP A 331 -1 O VAL A 324 N TRP A 315
SHEET 4 AA9 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AB1 4 PRO A 362 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AB1 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB2 4 VAL A 404 LEU A 410 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB3 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB4 8 SER A 511 LEU A 519 0
SHEET 2 AB4 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 AB4 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB5 4 ARG B 61 TRP B 62 0
SHEET 2 AB5 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 AB5 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 AB5 4 SER B 87 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 AB6 3 ILE B 102 ILE B 107 0
SHEET 2 AB6 3 ILE B 114 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB6 3 TYR B 128 TYR B 135 -1 O THR B 129 N VAL B 121
SHEET 1 AB7 4 TRP B 154 TRP B 157 0
SHEET 2 AB7 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 AB7 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 AB7 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB8 3 ILE B 194 ASN B 196 0
SHEET 2 AB8 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB8 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AB9 4 ILE B 194 ASN B 196 0
SHEET 2 AB9 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB9 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 AB9 4 ILE B 285 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 AC1 2 LEU B 235 PHE B 240 0
SHEET 2 AC1 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AC2 4 HIS B 298 TRP B 305 0
SHEET 2 AC2 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AC2 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 AC2 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 AC3 4 HIS B 298 TRP B 305 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AC3 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 AC3 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 AC4 4 HIS B 363 PHE B 364 0
SHEET 2 AC4 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC4 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 AC4 4 LYS B 391 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC5 4 VAL B 404 LEU B 410 0
SHEET 2 AC5 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC5 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC5 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC6 4 CYS B 454 PHE B 461 0
SHEET 2 AC6 4 TYR B 467 PRO B 475 -1 O ARG B 471 N SER B 458
SHEET 3 AC6 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 AC6 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC7 8 LYS B 513 LEU B 519 0
SHEET 2 AC7 8 THR B 522 ILE B 529 -1 O PHE B 524 N ILE B 517
SHEET 3 AC7 8 ILE B 574 PHE B 578 -1 O SER B 577 N GLN B 527
SHEET 4 AC7 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 AC7 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 AC7 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AC7 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AC7 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 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.03
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.04
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.04
LINK ND2 ASN A 229 C1 NAG A 802 1555 1555 1.46
LINK ND2 ASN B 229 C1 NAG B 803 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B 802 1555 1555 1.46
LINK O4 NAG B 803 C1 MAN B 804 1555 1555 1.44
LINK O3 MAN B 804 C1 MAN B 805 1555 1555 1.46
LINK O3 MAN B 805 C1 MAN B 806 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 0.33
CISPEP 2 GLY B 474 PRO B 475 0 3.30
SITE 1 AC1 15 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC1 15 PHE A 357 ARG A 358 TYR A 547 SER A 630
SITE 3 AC1 15 TYR A 631 VAL A 656 TYR A 662 TYR A 666
SITE 4 AC1 15 ASN A 710 VAL A 711 HIS A 740
SITE 1 AC2 15 ARG B 125 GLU B 205 GLU B 206 VAL B 207
SITE 2 AC2 15 SER B 209 PHE B 357 ARG B 358 TYR B 547
SITE 3 AC2 15 SER B 630 TYR B 631 VAL B 656 TYR B 662
SITE 4 AC2 15 TYR B 666 ASN B 710 VAL B 711
SITE 1 AC3 4 ASN A 229 THR A 231 GLU A 232 LYS A 267
SITE 1 AC4 5 SER A 690 ILE B 194 ASN B 229 GLU B 232
SITE 2 AC4 5 LYS B 267
SITE 1 AC5 3 VAL B 279 ASN B 281 HOH B 901
CRYST1 65.360 126.820 112.620 90.00 99.95 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015300 0.000000 0.002684 0.00000
SCALE2 0.000000 0.007885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009015 0.00000
TER 5958 PRO A 766
TER 11916 PRO B 766
MASTER 377 0 8 35 99 0 12 612141 2 154 114
END |