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HEADER HYDROLASE 29-APR-22 7XNM
TITLE STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE 4 INHIBITORY PEPTIDE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 5 EC: 3.4.14.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ILE-LEU-ALA-PRO-PRO-GLU-ARG;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: CRASSOSTREA GIGAS;
SOURCE 8 ORGANISM_TAXID: 29159
KEYWDS A SERINE PROTEASE SUBFAMILY, DIABETES MELLITUS TYPE 2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.Y.LI,M.J.CAO
REVDAT 1 17-MAY-23 7XNM 0
JRNL AUTH W.Y.LI,M.J.CAO
JRNL TITL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE 4 INHIBITORY
JRNL TITL 2 PEPTIDE COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 26023
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.680
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.4800 - 8.5500 0.99 1806 150 0.2139 0.2828
REMARK 3 2 8.5500 - 6.8200 1.00 1747 146 0.2221 0.3194
REMARK 3 3 6.8100 - 5.9600 1.00 1758 146 0.2331 0.2920
REMARK 3 4 5.9600 - 5.4200 1.00 1735 145 0.2243 0.2828
REMARK 3 5 5.4200 - 5.0300 1.00 1734 144 0.1995 0.2899
REMARK 3 6 5.0300 - 4.7400 1.00 1722 143 0.1999 0.2914
REMARK 3 7 4.7400 - 4.5000 1.00 1718 143 0.1865 0.2537
REMARK 3 8 4.5000 - 4.3100 1.00 1746 144 0.2009 0.3033
REMARK 3 9 4.3100 - 4.1400 1.00 1729 145 0.2167 0.2823
REMARK 3 10 4.1400 - 4.0000 1.00 1685 140 0.2279 0.3061
REMARK 3 11 4.0000 - 3.8700 0.99 1713 142 0.2539 0.3405
REMARK 3 12 3.8700 - 3.7600 0.99 1728 144 0.2599 0.3156
REMARK 3 13 3.7600 - 3.6600 0.98 1679 141 0.2786 0.3473
REMARK 3 14 3.6600 - 3.5800 0.90 1524 126 0.2702 0.3429
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.464
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.616
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.02
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 12577
REMARK 3 ANGLE : 0.676 17117
REMARK 3 CHIRALITY : 0.058 1858
REMARK 3 PLANARITY : 0.005 2162
REMARK 3 DIHEDRAL : 10.001 1757
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -35.6352 37.8055 -8.1625
REMARK 3 T TENSOR
REMARK 3 T11: 0.4407 T22: 0.5075
REMARK 3 T33: 0.5167 T12: -0.0042
REMARK 3 T13: -0.0525 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.1437 L22: 0.2707
REMARK 3 L33: 0.8906 L12: -0.0964
REMARK 3 L13: -0.1430 L23: -0.0210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0220 S12: 0.2882 S13: -0.0408
REMARK 3 S21: -0.0365 S22: -0.0402 S23: 0.0104
REMARK 3 S31: -0.0354 S32: -0.1866 S33: 0.0133
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7XNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-21
REMARK 200 TEMPERATURE (KELVIN) : 190
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97894
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SILICON CRYSTAL (111)
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26023
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.575
REMARK 200 RESOLUTION RANGE LOW (A) : 29.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 2.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.60
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1WCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M AMMONIUM CHLORIDE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 128.67000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.80850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 128.67000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.80850
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K
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 PRO A 766
REMARK 465 SER B 39
REMARK 465 ARG B 40
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 194 CG1 CG2 CD1
REMARK 470 THR A 231 OG1 CG2
REMARK 470 GLU A 378 CG CD OE1 OE2
REMARK 470 LYS A 489 CG CD CE NZ
REMARK 470 LYS A 523 CG CD CE NZ
REMARK 470 TYR B 70 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 436 CG CD1 CD2
REMARK 470 LYS B 441 CG CD CE NZ
REMARK 470 LEU B 494 CG CD1 CD2
REMARK 470 LYS B 648 CG CD CE NZ
REMARK 470 LEU B 759 CG CD1 CD2
REMARK 470 ILE C 1 CG1 CG2 CD1
REMARK 470 ARG C 7 CG CD NE CZ NH1 NH2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLU A 97
REMARK 475 LEU A 98
REMARK 475 GLY A 99
REMARK 475 TYR A 100
REMARK 475 GLU B 97
REMARK 475 LEU B 98
REMARK 475 GLY B 99
REMARK 475 TYR B 100
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 39 CB OG
REMARK 480 ARG A 40 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU A 145 CB CG CD OE1 OE2
REMARK 480 ARG A 147 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 391 NZ
REMARK 480 LYS A 399 CD CE NZ
REMARK 480 LYS A 464 CG CD CE NZ
REMARK 480 SER A 484 CB OG
REMARK 480 LYS A 513 CG CD CE NZ
REMARK 480 LYS A 539 CD CE NZ
REMARK 480 LYS A 622 CD CE NZ
REMARK 480 GLU B 145 CB CG CD OE1 OE2
REMARK 480 ARG B 147 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 391 NZ
REMARK 480 LYS B 399 CD CE NZ
REMARK 480 LYS B 464 CG CD CE NZ
REMARK 480 SER B 484 CB OG
REMARK 480 LYS B 489 CD CE NZ
REMARK 480 LYS B 513 CG CD CE NZ
REMARK 480 LYS B 523 CG CD CE NZ
REMARK 480 LYS B 539 CD CE NZ
REMARK 480 LYS B 622 CD CE NZ
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 PHE A 57 -162.42 -121.13
REMARK 500 TYR A 58 94.76 -161.83
REMARK 500 SER A 64 -151.15 -147.22
REMARK 500 HIS A 66 6.73 -153.68
REMARK 500 ASN A 74 -17.06 92.63
REMARK 500 PHE A 89 -66.81 -93.32
REMARK 500 SER A 93 -8.38 65.53
REMARK 500 GLU A 97 26.52 43.02
REMARK 500 SER A 101 -166.61 -162.37
REMARK 500 GLN A 123 -97.86 -92.67
REMARK 500 TRP A 124 -121.26 -100.83
REMARK 500 TYR A 128 144.01 -174.34
REMARK 500 GLU A 146 77.82 55.15
REMARK 500 ASN A 151 48.94 72.00
REMARK 500 HIS A 162 39.07 -146.50
REMARK 500 ILE A 185 -64.36 -103.17
REMARK 500 VAL A 193 -73.11 -129.08
REMARK 500 VAL A 198 -166.12 -127.94
REMARK 500 ASP A 230 33.20 -83.23
REMARK 500 SER A 242 -135.81 63.86
REMARK 500 PRO A 255 85.35 -62.14
REMARK 500 LYS A 258 -178.52 -68.54
REMARK 500 ASN A 279 50.85 -106.18
REMARK 500 PRO A 290 170.91 -59.05
REMARK 500 VAL A 306 -70.63 -96.89
REMARK 500 ARG A 343 34.67 -85.64
REMARK 500 ARG A 356 -67.88 -95.94
REMARK 500 ASN A 377 -147.78 -91.26
REMARK 500 SER A 392 -75.34 -67.99
REMARK 500 ASN A 420 35.49 -97.49
REMARK 500 LYS A 423 -3.92 63.43
REMARK 500 GLU A 448 47.66 -94.26
REMARK 500 PRO A 451 10.03 -66.04
REMARK 500 LEU A 491 -88.79 46.45
REMARK 500 ASP A 515 -146.02 -141.38
REMARK 500 THR A 557 41.70 -89.33
REMARK 500 LEU A 561 93.90 -66.03
REMARK 500 HIS A 592 41.81 -78.10
REMARK 500 ARG A 597 54.18 -162.55
REMARK 500 THR A 600 -74.78 -113.74
REMARK 500 SER A 630 -117.31 60.84
REMARK 500 LYS A 648 -38.45 -131.75
REMARK 500 ASP A 678 -82.72 -112.63
REMARK 500 ASN A 679 47.21 -155.43
REMARK 500 ALA A 707 53.01 -118.58
REMARK 500 ASN A 710 -79.59 -92.17
REMARK 500 MET A 733 103.82 -168.65
REMARK 500 ASP A 739 -158.50 -80.82
REMARK 500 GLN B 61 91.27 -163.51
REMARK 500 SER B 64 -158.45 -104.63
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7XNM A 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 7XNM B 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 7XNM C 1 7 PDB 7XNM 7XNM 1 7
DBREF 7XNM D 1 7 PDB 7XNM 7XNM 1 7
SEQRES 1 A 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 A 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 A 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 A 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 A 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 A 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 A 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 A 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 A 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 A 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 A 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 A 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 A 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 B 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 B 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 B 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 B 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 B 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 B 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 B 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 B 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 B 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 B 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 B 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 B 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 7 ILE LEU ALA PRO PRO GLU ARG
SEQRES 1 D 7 ILE LEU ALA PRO PRO GLU ARG
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG A 801 14
HET NAG A 802 14
HET NAG B 801 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 5 NAG 17(C8 H15 N O6)
FORMUL 5 BMA C6 H12 O6
FORMUL 5 MAN C6 H12 O6
HELIX 1 AA1 THR A 44 LYS A 50 1 7
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 GLU A 421 MET A 425 5 5
HELIX 5 AA5 ASN A 497 GLN A 505 1 9
HELIX 6 AA6 SER A 562 THR A 570 1 9
HELIX 7 AA7 GLY A 587 HIS A 592 1 6
HELIX 8 AA8 THR A 600 SER A 614 1 15
HELIX 9 AA9 SER A 630 GLY A 641 1 12
HELIX 10 AB1 LYS A 658 TYR A 662 5 5
HELIX 11 AB2 ASP A 663 MET A 671 1 9
HELIX 12 AB3 ASN A 679 ARG A 684 1 6
HELIX 13 AB4 THR A 687 LYS A 696 5 10
HELIX 14 AB5 HIS A 712 ASP A 725 1 14
HELIX 15 AB6 SER A 744 PHE A 763 1 20
HELIX 16 AB7 THR B 44 LYS B 50 1 7
HELIX 17 AB8 ASP B 200 VAL B 207 1 8
HELIX 18 AB9 PRO B 290 ILE B 295 1 6
HELIX 19 AC1 SER B 340 ALA B 342 5 3
HELIX 20 AC2 GLU B 421 MET B 425 5 5
HELIX 21 AC3 ASN B 497 ASP B 506 1 10
HELIX 22 AC4 SER B 562 THR B 570 1 9
HELIX 23 AC5 GLY B 587 HIS B 592 1 6
HELIX 24 AC6 THR B 600 LYS B 615 1 16
HELIX 25 AC7 TYR B 631 GLY B 641 1 11
HELIX 26 AC8 LYS B 658 TYR B 662 5 5
HELIX 27 AC9 ASP B 663 MET B 671 1 9
HELIX 28 AD1 ASN B 679 ASN B 685 1 7
HELIX 29 AD2 SER B 686 ARG B 691 5 6
HELIX 30 AD3 ALA B 692 VAL B 698 5 7
HELIX 31 AD4 HIS B 712 ASP B 725 1 14
HELIX 32 AD5 SER B 744 PHE B 763 1 20
SHEET 1 AA1 4 GLN A 61 TRP A 62 0
SHEET 2 AA1 4 GLU A 67 GLN A 72 -1 O LEU A 69 N GLN A 61
SHEET 3 AA1 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 AA1 4 SER A 86 LEU A 90 -1 O SER A 87 N LEU A 78
SHEET 1 AA2 3 TYR A 105 VAL A 107 0
SHEET 2 AA2 3 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA2 3 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 1 AA3 4 TRP A 154 TRP A 157 0
SHEET 2 AA3 4 LEU A 164 VAL A 167 -1 O ALA A 165 N THR A 156
SHEET 3 AA3 4 ILE A 172 VAL A 174 -1 O TYR A 173 N TYR A 166
SHEET 4 AA3 4 GLN A 183 ARG A 184 -1 O GLN A 183 N VAL A 174
SHEET 1 AA4 3 ILE A 194 ASN A 196 0
SHEET 2 AA4 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA4 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA5 4 ILE A 194 ASN A 196 0
SHEET 2 AA5 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 4 THR A 265 ASP A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 AA5 4 SER A 284 ILE A 287 -1 O TYR A 285 N VAL A 270
SHEET 1 AA6 2 LEU A 235 PHE A 240 0
SHEET 2 AA6 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AA7 4 HIS A 298 THR A 307 0
SHEET 2 AA7 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA7 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 AA7 4 TRP A 337 ILE A 338 -1 O ILE A 338 N ASP A 329
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA8 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 AA8 4 GLN A 344 ILE A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AA9 4 HIS A 363 PHE A 364 0
SHEET 2 AA9 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AA9 4 LYS A 382 GLN A 388 -1 O CYS A 385 N LYS A 373
SHEET 4 AA9 4 CYS A 394 PHE A 396 -1 O THR A 395 N HIS A 386
SHEET 1 AB1 4 VAL A 404 LEU A 410 0
SHEET 2 AB1 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB1 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB1 4 VAL A 442 CYS A 444 -1 O THR A 443 N ARG A 433
SHEET 1 AB2 4 CYS A 454 PHE A 461 0
SHEET 2 AB2 4 TYR A 467 PRO A 475 -1 O PHE A 473 N TYR A 456
SHEET 3 AB2 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 AB2 4 ARG A 492 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB3 8 SER A 511 LEU A 519 0
SHEET 2 AB3 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 AB3 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB3 8 TYR A 540 VAL A 546 1 N LEU A 543 O ALA A 576
SHEET 5 AB3 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 AB3 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB3 8 LEU A 701 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 AB3 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 AB4 3 GLU B 67 LYS B 71 0
SHEET 2 AB4 3 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 3 AB4 3 SER B 86 LEU B 90 -1 O SER B 87 N LEU B 78
SHEET 1 AB5 4 THR B 102 VAL B 107 0
SHEET 2 AB5 4 ILE B 114 LYS B 122 -1 O GLU B 117 N ASN B 103
SHEET 3 AB5 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 AB5 4 GLN B 141 LEU B 142 -1 N GLN B 141 O ASP B 136
SHEET 1 AB6 4 TRP B 154 THR B 156 0
SHEET 2 AB6 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 AB6 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 AB6 4 GLN B 183 ARG B 184 -1 O GLN B 183 N VAL B 174
SHEET 1 AB7 4 ILE B 194 ASN B 196 0
SHEET 2 AB7 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB7 4 THR B 265 ASP B 272 -1 O VAL B 271 N LEU B 223
SHEET 4 AB7 4 SER B 284 ILE B 287 -1 O ILE B 287 N PHE B 268
SHEET 1 AB8 2 LEU B 235 PHE B 240 0
SHEET 2 AB8 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AB9 4 HIS B 298 THR B 307 0
SHEET 2 AB9 4 ARG B 310 ARG B 317 -1 O GLN B 314 N CYS B 301
SHEET 3 AB9 4 TYR B 322 ASP B 329 -1 O ASP B 326 N LEU B 313
SHEET 4 AB9 4 GLN B 344 ILE B 348 -1 O GLU B 347 N SER B 323
SHEET 1 AC1 4 HIS B 363 PHE B 364 0
SHEET 2 AC1 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC1 4 LYS B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 AC1 4 LYS B 391 PHE B 396 -1 O THR B 395 N HIS B 386
SHEET 1 AC2 3 VAL B 404 LEU B 410 0
SHEET 2 AC2 3 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC2 3 ASN B 430 LEU B 431 -1 O ASN B 430 N SER B 419
SHEET 1 AC3 3 VAL B 404 LEU B 410 0
SHEET 2 AC3 3 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC3 3 ILE B 434 GLN B 435 -1 O ILE B 434 N LEU B 415
SHEET 1 AC4 3 CYS B 454 SER B 458 0
SHEET 2 AC4 3 GLN B 469 PRO B 475 -1 O GLY B 474 N GLN B 455
SHEET 3 AC4 3 LEU B 479 LEU B 482 -1 O LEU B 479 N CYS B 472
SHEET 1 AC5 8 SER B 511 LEU B 519 0
SHEET 2 AC5 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 AC5 8 ILE B 574 ASP B 579 -1 O VAL B 575 N ILE B 529
SHEET 4 AC5 8 TYR B 540 GLU B 545 1 N PRO B 541 O ILE B 574
SHEET 5 AC5 8 VAL B 619 SER B 630 1 O ASP B 620 N TYR B 540
SHEET 6 AC5 8 ILE B 651 PRO B 655 1 O ILE B 651 N GLY B 628
SHEET 7 AC5 8 LEU B 701 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 AC5 8 GLN B 731 TYR B 735 1 O MET B 733 N HIS B 704
SSBOND 1 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 2 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 3 CYS A 454 CYS A 472 1555 1555 2.03
SSBOND 4 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 5 CYS B 385 CYS B 394 1555 1555 2.03
SSBOND 6 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 7 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 8 CYS B 649 CYS B 762 1555 1555 2.03
LINK ND2 ASN A 92 C1 NAG A 802 1555 1555 1.46
LINK ND2 ASN A 229 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN A 279 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 685 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 150 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG B 801 1555 1555 1.45
LINK ND2 ASN B 279 C1 NAG K 1 1555 1555 1.46
LINK ND2 ASN B 321 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN B 685 C1 NAG I 1 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.47
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.46
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.43
CISPEP 1 GLY A 474 PRO A 475 0 8.15
CISPEP 2 GLY B 474 PRO B 475 0 2.28
CRYST1 257.340 75.617 121.679 90.00 110.20 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003886 0.000000 0.001430 0.00000
SCALE2 0.000000 0.013225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008757 0.00000
TER 5942 LEU A 765
TER 11868 PRO B 766
TER 11915 ARG C 7
TER 11971 ARG D 7
MASTER 364 0 19 32 90 0 0 612227 4 286 114
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