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HEADER MEMBRANE PROTEIN 30-SEP-14 4WJL
TITLE STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE 10 (DPPY): A MODULATOR OF
TITLE 2 NEURONAL KV4 CHANNELS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INACTIVE DIPEPTIDYL PEPTIDASE 10;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 65-783;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 3,DPRP-3,DIPEPTIDYL
COMPND 6 PEPTIDASE X,DPP X,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 2,DPL2;
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: DPP10, DPRP3, KIAA1492;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: SF9
KEYWDS INACTIVE DIPEPTIDYL PEPTIDASE 10, DPP4 STRUCTURE HOMOLOGUE,
KEYWDS 2 ALPHA/BETA HYDROLASE, BETA-PROPELLER, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.A.BEZERRA,E.DOBROVETSKY,A.SEITOVA,S.FEDOSYUK,S.DHE-PAGANON,K.GRUBER
REVDAT 1 18-MAR-15 4WJL 0
JRNL AUTH G.A.BEZERRA,E.DOBROVETSKY,A.SEITOVA,S.FEDOSYUK,
JRNL AUTH 2 S.DHE-PAGANON,K.GRUBER
JRNL TITL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE 10 (DPPY): A
JRNL TITL 2 MODULATOR OF NEURONAL KV4 CHANNELS.
JRNL REF SCI REP V. 5 8769 2015
JRNL REFN ESSN 2045-2322
JRNL PMID 25740212
JRNL DOI 10.1038/SREP08769
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 28967
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1476
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 66.5585 - 7.5582 1.00 2666 140 0.2176 0.2363
REMARK 3 2 7.5582 - 6.0004 1.00 2560 126 0.2241 0.2279
REMARK 3 3 6.0004 - 5.2423 1.00 2512 150 0.1942 0.2499
REMARK 3 4 5.2423 - 4.7631 1.00 2479 137 0.1654 0.2169
REMARK 3 5 4.7631 - 4.4218 1.00 2489 146 0.1630 0.1792
REMARK 3 6 4.4218 - 4.1611 1.00 2480 129 0.1801 0.2401
REMARK 3 7 4.1611 - 3.9528 1.00 2490 136 0.2074 0.2442
REMARK 3 8 3.9528 - 3.7807 1.00 2458 132 0.2179 0.2602
REMARK 3 9 3.7807 - 3.6352 1.00 2470 133 0.2500 0.3078
REMARK 3 10 3.6352 - 3.5098 1.00 2425 131 0.2552 0.2922
REMARK 3 11 3.5098 - 3.4000 1.00 2462 116 0.2804 0.3134
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 71.01
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 74.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.27940
REMARK 3 B22 (A**2) : 9.61090
REMARK 3 B33 (A**2) : -5.33150
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 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 : 0.008 12146
REMARK 3 ANGLE : 1.362 16474
REMARK 3 CHIRALITY : 0.102 1856
REMARK 3 PLANARITY : 0.007 2053
REMARK 3 DIHEDRAL : 20.860 4530
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 67:407 OR RESSEQ
REMARK 3 412:782 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 67:407 OR RESSEQ
REMARK 3 412:782 )
REMARK 3 ATOM PAIRS NUMBER : 5752
REMARK 3 RMSD : 0.052
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000203920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97943
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29019
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 111.388
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.22600
REMARK 200 FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.77500
REMARK 200 R SYM FOR SHELL (I) : 0.77500
REMARK 200 FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: 1XFD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS FORMED WITHIN 2-4 WEEKS USING
REMARK 280 100 MICROMETERS OF RESERVOIR SOLUTION CONSISTING OF 20%(W/V) PEG
REMARK 280 1500, 0.2 M MGCL2, 0.1 M SODIUM CACODYLATE PH 5.5., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.45500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.12500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.86500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.12500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.45500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.86500
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: 7230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 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 SER A 65
REMARK 465 GLU A 783
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 LYS A 97 CG CD CE NZ
REMARK 470 ILE A 413 CB CG1 CG2 CD1
REMARK 470 LYS A 553 CG CD CE NZ
REMARK 470 LYS B 97 CG CD CE NZ
REMARK 470 ILE B 413 CB CG1 CG2 CD1
REMARK 470 LYS B 553 CG CD CE NZ
REMARK 470 LYS B 669 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 119 C2 NAG A 802 1.61
REMARK 500 ND2 ASN A 119 N2 NAG A 802 1.78
REMARK 500 O ASN B 710 N HIS B 712 2.01
REMARK 500 ND2 ASN B 119 C2 NAG B 802 2.07
REMARK 500 O TYR B 477 O CYS B 493 2.08
REMARK 500 O TYR A 477 O CYS A 493 2.11
REMARK 500 O GLN B 407 O LYS B 409 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 PRO A 533 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO A 695 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO B 533 C - N - CA ANGL. DEV. = 10.5 DEGREES
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 PHE A 79 -157.86 -79.57
REMARK 500 VAL A 80 86.22 70.61
REMARK 500 ILE A 89 -72.12 -131.24
REMARK 500 SER A 98 73.88 59.68
REMARK 500 GLU A 99 -62.92 -101.01
REMARK 500 ASN A 111 -4.30 74.80
REMARK 500 GLU A 118 -164.45 -126.10
REMARK 500 ASN A 119 37.09 -73.17
REMARK 500 PHE A 122 -61.19 -159.68
REMARK 500 PHE A 125 64.10 30.00
REMARK 500 LYS A 126 69.17 39.34
REMARK 500 ILE A 148 -65.02 -131.02
REMARK 500 PHE A 149 -79.17 -120.86
REMARK 500 HIS A 150 -66.09 -132.96
REMARK 500 ARG A 165 -38.75 -34.20
REMARK 500 GLU A 174 -13.72 75.07
REMARK 500 ALA A 183 -73.47 -132.48
REMARK 500 ALA A 184 -144.87 47.04
REMARK 500 ILE A 221 -61.93 -132.33
REMARK 500 ALA A 272 -165.73 -73.18
REMARK 500 SER A 316 -7.04 84.55
REMARK 500 THR A 330 -58.44 -128.47
REMARK 500 LYS A 359 -63.68 -121.33
REMARK 500 THR A 366 -79.32 -117.29
REMARK 500 SER A 369 -167.17 -73.49
REMARK 500 ARG A 379 -19.75 74.53
REMARK 500 GLN A 392 -5.57 63.13
REMARK 500 ARG A 395 -3.22 88.73
REMARK 500 LYS A 409 -140.94 53.56
REMARK 500 GLU A 411 -144.54 52.00
REMARK 500 GLN A 412 -162.90 36.69
REMARK 500 ILE A 413 87.70 98.80
REMARK 500 TRP A 423 167.65 171.89
REMARK 500 SER A 446 141.25 -179.64
REMARK 500 THR A 457 -73.37 -56.04
REMARK 500 ILE A 466 -60.54 -98.64
REMARK 500 PHE A 470 -68.11 -132.52
REMARK 500 LYS A 472 -110.33 60.33
REMARK 500 CYS A 493 -72.48 -73.81
REMARK 500 GLU A 494 -1.78 65.05
REMARK 500 THR A 506 -73.75 -56.26
REMARK 500 PRO A 509 75.14 -64.61
REMARK 500 LYS A 511 -14.02 68.66
REMARK 500 TYR A 512 -119.88 42.50
REMARK 500 LYS A 529 -73.21 -48.84
REMARK 500 ILE A 530 74.63 58.82
REMARK 500 ASP A 541 -126.81 50.46
REMARK 500 ASP A 592 -4.97 90.04
REMARK 500 ARG A 617 -13.18 69.49
REMARK 500 SER A 663 -28.53 40.28
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 412 ILE A 413 -147.25
REMARK 500 GLN B 407 SER B 408 139.24
REMARK 500 ASN B 710 VAL B 711 139.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN A 412 -15.05
REMARK 500 GLN B 412 16.21
REMARK 500 PRO B 695 -10.68
REMARK 500 ASN B 710 10.29
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 Mono-Saccharide NAG A 801 bound
REMARK 800 to ASN A 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 803 through MAN A 806 bound to ASN A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 807 through NAG A 808 bound to ASN A 342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 801 bound
REMARK 800 to ASN B 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 802 through NAG B 803 bound to ASN B 119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 804 through BMA B 806 bound to ASN B 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 807 through NAG B 808 bound to ASN B 342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 809 bound
REMARK 800 to ASN B 748
DBREF 4WJL A 65 783 UNP Q8N608 DPP10_HUMAN 15 733
DBREF 4WJL B 65 783 UNP Q8N608 DPP10_HUMAN 15 733
SEQADV 4WJL MET A 288 UNP Q8N608 VAL 238 VARIANT
SEQADV 4WJL ILE A 401 UNP Q8N608 VAL 351 VARIANT
SEQADV 4WJL MET B 288 UNP Q8N608 VAL 238 VARIANT
SEQADV 4WJL ILE B 401 UNP Q8N608 VAL 351 VARIANT
SEQRES 1 A 719 SER GLU THR ARG LEU SER LEU GLU ASP LEU PHE ARG LYS
SEQRES 2 A 719 ASP PHE VAL LEU HIS ASP PRO GLU ALA ARG TRP ILE ASN
SEQRES 3 A 719 ASP THR ASP VAL VAL TYR LYS SER GLU ASN GLY HIS VAL
SEQRES 4 A 719 ILE LYS LEU ASN ILE GLU THR ASN ALA THR THR LEU LEU
SEQRES 5 A 719 LEU GLU ASN THR THR PHE VAL THR PHE LYS ALA SER ARG
SEQRES 6 A 719 HIS SER VAL SER PRO ASP LEU LYS TYR VAL LEU LEU ALA
SEQRES 7 A 719 TYR ASP VAL LYS GLN ILE PHE HIS TYR SER TYR THR ALA
SEQRES 8 A 719 SER TYR VAL ILE TYR ASN ILE HIS THR ARG GLU VAL TRP
SEQRES 9 A 719 GLU LEU ASN PRO PRO GLU VAL GLU ASP SER VAL LEU GLN
SEQRES 10 A 719 TYR ALA ALA TRP GLY VAL GLN GLY GLN GLN LEU ILE TYR
SEQRES 11 A 719 ILE PHE GLU ASN ASN ILE TYR TYR GLN PRO ASP ILE LYS
SEQRES 12 A 719 SER SER SER LEU ARG LEU THR SER SER GLY LYS GLU GLU
SEQRES 13 A 719 ILE ILE PHE ASN GLY ILE ALA ASP TRP LEU TYR GLU GLU
SEQRES 14 A 719 GLU LEU LEU HIS SER HIS ILE ALA HIS TRP TRP SER PRO
SEQRES 15 A 719 ASP GLY GLU ARG LEU ALA PHE LEU MET ILE ASN ASP SER
SEQRES 16 A 719 LEU VAL PRO THR MET VAL ILE PRO ARG PHE THR GLY ALA
SEQRES 17 A 719 LEU TYR PRO LYS GLY LYS GLN TYR PRO TYR PRO LYS ALA
SEQRES 18 A 719 GLY GLN MET ASN PRO THR ILE LYS LEU TYR VAL VAL ASN
SEQRES 19 A 719 LEU TYR GLY PRO THR HIS THR LEU GLU LEU MET PRO PRO
SEQRES 20 A 719 ASP SER PHE LYS SER ARG GLU TYR TYR ILE THR MET VAL
SEQRES 21 A 719 LYS TRP VAL SER ASN THR LYS THR VAL VAL ARG TRP LEU
SEQRES 22 A 719 ASN ARG ALA GLN ASN ILE SER ILE LEU THR VAL CYS GLU
SEQRES 23 A 719 THR THR THR GLY ALA CYS SER LYS LYS TYR GLU MET THR
SEQRES 24 A 719 SER ASP THR TRP LEU SER GLN GLN ASN GLU GLU PRO VAL
SEQRES 25 A 719 PHE SER ARG ASP GLY SER LYS PHE PHE MET THR VAL PRO
SEQRES 26 A 719 VAL LYS GLN GLY GLY ARG GLY GLU PHE HIS HIS ILE ALA
SEQRES 27 A 719 MET PHE LEU ILE GLN SER LYS SER GLU GLN ILE THR VAL
SEQRES 28 A 719 ARG HIS LEU THR SER GLY ASN TRP GLU VAL ILE LYS ILE
SEQRES 29 A 719 LEU ALA TYR ASP GLU THR THR GLN LYS ILE TYR PHE LEU
SEQRES 30 A 719 SER THR GLU SER SER PRO ARG GLY ARG GLN LEU TYR SER
SEQRES 31 A 719 ALA SER THR GLU GLY LEU LEU ASN ARG GLN CYS ILE SER
SEQRES 32 A 719 CYS ASN PHE MET LYS GLU GLN CYS THR TYR PHE ASP ALA
SEQRES 33 A 719 SER PHE SER PRO MET ASN GLN HIS PHE LEU LEU PHE CYS
SEQRES 34 A 719 GLU GLY PRO ARG VAL PRO VAL VAL SER LEU HIS SER THR
SEQRES 35 A 719 ASP ASN PRO ALA LYS TYR PHE ILE LEU GLU SER ASN SER
SEQRES 36 A 719 MET LEU LYS GLU ALA ILE LEU LYS LYS LYS ILE GLY LYS
SEQRES 37 A 719 PRO GLU ILE LYS ILE LEU HIS ILE ASP ASP TYR GLU LEU
SEQRES 38 A 719 PRO LEU GLN LEU SER LEU PRO LYS ASP PHE MET ASP ARG
SEQRES 39 A 719 ASN GLN TYR ALA LEU LEU LEU ILE MET ASP GLU GLU PRO
SEQRES 40 A 719 GLY GLY GLN LEU VAL THR ASP LYS PHE HIS ILE ASP TRP
SEQRES 41 A 719 ASP SER VAL LEU ILE ASP MET ASP ASN VAL ILE VAL ALA
SEQRES 42 A 719 ARG PHE ASP GLY ARG GLY SER GLY PHE GLN GLY LEU LYS
SEQRES 43 A 719 ILE LEU GLN GLU ILE HIS ARG ARG LEU GLY SER VAL GLU
SEQRES 44 A 719 VAL LYS ASP GLN ILE THR ALA VAL LYS PHE LEU LEU LYS
SEQRES 45 A 719 LEU PRO TYR ILE ASP SER LYS ARG LEU SER ILE PHE GLY
SEQRES 46 A 719 LYS GLY TYR GLY GLY TYR ILE ALA SER MET ILE LEU LYS
SEQRES 47 A 719 SER ASP GLU LYS LEU PHE LYS CYS GLY SER VAL VAL ALA
SEQRES 48 A 719 PRO ILE THR ASP LEU LYS LEU TYR ALA SER ALA PHE SER
SEQRES 49 A 719 GLU ARG TYR LEU GLY MET PRO SER LYS GLU GLU SER THR
SEQRES 50 A 719 TYR GLN ALA ALA SER VAL LEU HIS ASN VAL HIS GLY LEU
SEQRES 51 A 719 LYS GLU GLU ASN ILE LEU ILE ILE HIS GLY THR ALA ASP
SEQRES 52 A 719 THR LYS VAL HIS PHE GLN HIS SER ALA GLU LEU ILE LYS
SEQRES 53 A 719 HIS LEU ILE LYS ALA GLY VAL ASN TYR THR MET GLN VAL
SEQRES 54 A 719 TYR PRO ASP GLU GLY HIS ASN VAL SER GLU LYS SER LYS
SEQRES 55 A 719 TYR HIS LEU TYR SER THR ILE LEU LYS PHE PHE SER ASP
SEQRES 56 A 719 CYS LEU LYS GLU
SEQRES 1 B 719 SER GLU THR ARG LEU SER LEU GLU ASP LEU PHE ARG LYS
SEQRES 2 B 719 ASP PHE VAL LEU HIS ASP PRO GLU ALA ARG TRP ILE ASN
SEQRES 3 B 719 ASP THR ASP VAL VAL TYR LYS SER GLU ASN GLY HIS VAL
SEQRES 4 B 719 ILE LYS LEU ASN ILE GLU THR ASN ALA THR THR LEU LEU
SEQRES 5 B 719 LEU GLU ASN THR THR PHE VAL THR PHE LYS ALA SER ARG
SEQRES 6 B 719 HIS SER VAL SER PRO ASP LEU LYS TYR VAL LEU LEU ALA
SEQRES 7 B 719 TYR ASP VAL LYS GLN ILE PHE HIS TYR SER TYR THR ALA
SEQRES 8 B 719 SER TYR VAL ILE TYR ASN ILE HIS THR ARG GLU VAL TRP
SEQRES 9 B 719 GLU LEU ASN PRO PRO GLU VAL GLU ASP SER VAL LEU GLN
SEQRES 10 B 719 TYR ALA ALA TRP GLY VAL GLN GLY GLN GLN LEU ILE TYR
SEQRES 11 B 719 ILE PHE GLU ASN ASN ILE TYR TYR GLN PRO ASP ILE LYS
SEQRES 12 B 719 SER SER SER LEU ARG LEU THR SER SER GLY LYS GLU GLU
SEQRES 13 B 719 ILE ILE PHE ASN GLY ILE ALA ASP TRP LEU TYR GLU GLU
SEQRES 14 B 719 GLU LEU LEU HIS SER HIS ILE ALA HIS TRP TRP SER PRO
SEQRES 15 B 719 ASP GLY GLU ARG LEU ALA PHE LEU MET ILE ASN ASP SER
SEQRES 16 B 719 LEU VAL PRO THR MET VAL ILE PRO ARG PHE THR GLY ALA
SEQRES 17 B 719 LEU TYR PRO LYS GLY LYS GLN TYR PRO TYR PRO LYS ALA
SEQRES 18 B 719 GLY GLN MET ASN PRO THR ILE LYS LEU TYR VAL VAL ASN
SEQRES 19 B 719 LEU TYR GLY PRO THR HIS THR LEU GLU LEU MET PRO PRO
SEQRES 20 B 719 ASP SER PHE LYS SER ARG GLU TYR TYR ILE THR MET VAL
SEQRES 21 B 719 LYS TRP VAL SER ASN THR LYS THR VAL VAL ARG TRP LEU
SEQRES 22 B 719 ASN ARG ALA GLN ASN ILE SER ILE LEU THR VAL CYS GLU
SEQRES 23 B 719 THR THR THR GLY ALA CYS SER LYS LYS TYR GLU MET THR
SEQRES 24 B 719 SER ASP THR TRP LEU SER GLN GLN ASN GLU GLU PRO VAL
SEQRES 25 B 719 PHE SER ARG ASP GLY SER LYS PHE PHE MET THR VAL PRO
SEQRES 26 B 719 VAL LYS GLN GLY GLY ARG GLY GLU PHE HIS HIS ILE ALA
SEQRES 27 B 719 MET PHE LEU ILE GLN SER LYS SER GLU GLN ILE THR VAL
SEQRES 28 B 719 ARG HIS LEU THR SER GLY ASN TRP GLU VAL ILE LYS ILE
SEQRES 29 B 719 LEU ALA TYR ASP GLU THR THR GLN LYS ILE TYR PHE LEU
SEQRES 30 B 719 SER THR GLU SER SER PRO ARG GLY ARG GLN LEU TYR SER
SEQRES 31 B 719 ALA SER THR GLU GLY LEU LEU ASN ARG GLN CYS ILE SER
SEQRES 32 B 719 CYS ASN PHE MET LYS GLU GLN CYS THR TYR PHE ASP ALA
SEQRES 33 B 719 SER PHE SER PRO MET ASN GLN HIS PHE LEU LEU PHE CYS
SEQRES 34 B 719 GLU GLY PRO ARG VAL PRO VAL VAL SER LEU HIS SER THR
SEQRES 35 B 719 ASP ASN PRO ALA LYS TYR PHE ILE LEU GLU SER ASN SER
SEQRES 36 B 719 MET LEU LYS GLU ALA ILE LEU LYS LYS LYS ILE GLY LYS
SEQRES 37 B 719 PRO GLU ILE LYS ILE LEU HIS ILE ASP ASP TYR GLU LEU
SEQRES 38 B 719 PRO LEU GLN LEU SER LEU PRO LYS ASP PHE MET ASP ARG
SEQRES 39 B 719 ASN GLN TYR ALA LEU LEU LEU ILE MET ASP GLU GLU PRO
SEQRES 40 B 719 GLY GLY GLN LEU VAL THR ASP LYS PHE HIS ILE ASP TRP
SEQRES 41 B 719 ASP SER VAL LEU ILE ASP MET ASP ASN VAL ILE VAL ALA
SEQRES 42 B 719 ARG PHE ASP GLY ARG GLY SER GLY PHE GLN GLY LEU LYS
SEQRES 43 B 719 ILE LEU GLN GLU ILE HIS ARG ARG LEU GLY SER VAL GLU
SEQRES 44 B 719 VAL LYS ASP GLN ILE THR ALA VAL LYS PHE LEU LEU LYS
SEQRES 45 B 719 LEU PRO TYR ILE ASP SER LYS ARG LEU SER ILE PHE GLY
SEQRES 46 B 719 LYS GLY TYR GLY GLY TYR ILE ALA SER MET ILE LEU LYS
SEQRES 47 B 719 SER ASP GLU LYS LEU PHE LYS CYS GLY SER VAL VAL ALA
SEQRES 48 B 719 PRO ILE THR ASP LEU LYS LEU TYR ALA SER ALA PHE SER
SEQRES 49 B 719 GLU ARG TYR LEU GLY MET PRO SER LYS GLU GLU SER THR
SEQRES 50 B 719 TYR GLN ALA ALA SER VAL LEU HIS ASN VAL HIS GLY LEU
SEQRES 51 B 719 LYS GLU GLU ASN ILE LEU ILE ILE HIS GLY THR ALA ASP
SEQRES 52 B 719 THR LYS VAL HIS PHE GLN HIS SER ALA GLU LEU ILE LYS
SEQRES 53 B 719 HIS LEU ILE LYS ALA GLY VAL ASN TYR THR MET GLN VAL
SEQRES 54 B 719 TYR PRO ASP GLU GLY HIS ASN VAL SER GLU LYS SER LYS
SEQRES 55 B 719 TYR HIS LEU TYR SER THR ILE LEU LYS PHE PHE SER ASP
SEQRES 56 B 719 CYS LEU LYS GLU
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET BMA A 805 11
HET MAN A 806 11
HET NAG A 807 14
HET NAG A 808 14
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET BMA B 806 11
HET NAG B 807 14
HET NAG B 808 14
HET NAG B 809 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 5 MAN C6 H12 O6
HELIX 1 AA1 SER A 70 PHE A 75 1 6
HELIX 2 AA2 ASP A 228 GLU A 234 1 7
HELIX 3 AA3 ASN A 518 LYS A 528 1 11
HELIX 4 AA4 ASP A 583 MET A 591 1 9
HELIX 5 AA5 ILE A 611 HIS A 616 5 6
HELIX 6 AA6 GLY A 620 LYS A 636 1 17
HELIX 7 AA7 GLY A 651 LEU A 661 1 11
HELIX 8 AA8 ASP A 679 TYR A 683 5 5
HELIX 9 AA9 ALA A 684 GLY A 693 1 10
HELIX 10 AB1 SER A 700 ALA A 705 1 6
HELIX 11 AB2 PHE A 732 ALA A 745 1 14
HELIX 12 AB3 SER A 762 LEU A 781 1 20
HELIX 13 AB4 SER B 70 PHE B 75 1 6
HELIX 14 AB5 ASP B 228 GLU B 234 1 7
HELIX 15 AB6 ASN B 518 LYS B 528 1 11
HELIX 16 AB7 ASP B 583 MET B 591 1 9
HELIX 17 AB8 ILE B 611 HIS B 616 5 6
HELIX 18 AB9 GLY B 620 LYS B 636 1 17
HELIX 19 AC1 GLY B 651 LEU B 661 1 11
HELIX 20 AC2 ASP B 679 TYR B 683 5 5
HELIX 21 AC3 ALA B 684 GLY B 693 1 10
HELIX 22 AC4 SER B 700 ALA B 705 1 6
HELIX 23 AC5 PHE B 732 ALA B 745 1 14
HELIX 24 AC6 SER B 762 LEU B 781 1 20
SHEET 1 AA1 3 ASP A 93 VAL A 94 0
SHEET 2 AA1 3 VAL A 103 ASN A 107 -1 O LEU A 106 N VAL A 94
SHEET 3 AA1 3 THR A 113 LEU A 117 -1 O THR A 114 N LYS A 105
SHEET 1 AA2 4 ARG A 129 VAL A 132 0
SHEET 2 AA2 4 TYR A 138 GLN A 147 -1 O LEU A 140 N SER A 131
SHEET 3 AA2 4 TYR A 153 ASN A 161 -1 O THR A 154 N LYS A 146
SHEET 4 AA2 4 VAL A 167 LEU A 170 -1 O TRP A 168 N ILE A 159
SHEET 1 AA3 3 LEU A 192 PHE A 196 0
SHEET 2 AA3 3 ASN A 199 GLN A 203 -1 O GLN A 203 N LEU A 192
SHEET 3 AA3 3 LEU A 211 ARG A 212 -1 O LEU A 211 N TYR A 202
SHEET 1 AA4 3 ILE A 222 ASN A 224 0
SHEET 2 AA4 3 ARG A 250 ASN A 257 -1 O ILE A 256 N PHE A 223
SHEET 3 AA4 3 HIS A 242 TRP A 244 -1 N TRP A 243 O ALA A 252
SHEET 1 AA5 4 ILE A 222 ASN A 224 0
SHEET 2 AA5 4 ARG A 250 ASN A 257 -1 O ILE A 256 N PHE A 223
SHEET 3 AA5 4 THR A 291 ASN A 298 -1 O LYS A 293 N MET A 255
SHEET 4 AA5 4 LEU A 306 GLU A 307 -1 O LEU A 306 N VAL A 296
SHEET 1 AA6 2 THR A 263 VAL A 265 0
SHEET 2 AA6 2 GLN A 279 PRO A 281 -1 O TYR A 280 N MET A 264
SHEET 1 AA7 4 TYR A 319 TRP A 326 0
SHEET 2 AA7 4 LYS A 331 ASN A 338 -1 O LEU A 337 N TYR A 320
SHEET 3 AA7 4 ILE A 343 GLU A 350 -1 O CYS A 349 N THR A 332
SHEET 4 AA7 4 ALA A 355 THR A 363 -1 O TYR A 360 N LEU A 346
SHEET 1 AA8 3 VAL A 376 PHE A 377 0
SHEET 2 AA8 3 PHE A 384 VAL A 390 -1 O PHE A 385 N VAL A 376
SHEET 3 AA8 3 PHE A 398 ALA A 402 -1 O ALA A 402 N MET A 386
SHEET 1 AA9 4 VAL A 425 TYR A 431 0
SHEET 2 AA9 4 LYS A 437 SER A 442 -1 O TYR A 439 N ALA A 430
SHEET 3 AA9 4 GLN A 451 SER A 456 -1 O TYR A 453 N PHE A 440
SHEET 4 AA9 4 ARG A 463 CYS A 465 -1 O GLN A 464 N SER A 454
SHEET 1 AB1 4 ASP A 479 PHE A 482 0
SHEET 2 AB1 4 HIS A 488 PHE A 492 -1 O LEU A 490 N SER A 481
SHEET 3 AB1 4 VAL A 501 SER A 505 -1 O SER A 502 N LEU A 491
SHEET 4 AB1 4 PHE A 513 GLU A 516 -1 O GLU A 516 N VAL A 501
SHEET 1 AB2 8 GLU A 534 ILE A 540 0
SHEET 2 AB2 8 TYR A 543 SER A 550 -1 O LEU A 549 N GLU A 534
SHEET 3 AB2 8 VAL A 594 PHE A 599 -1 O ARG A 598 N GLN A 548
SHEET 4 AB2 8 TYR A 561 ILE A 566 1 N LEU A 564 O ALA A 597
SHEET 5 AB2 8 ILE A 640 LYS A 650 1 O SER A 646 N LEU A 563
SHEET 6 AB2 8 CYS A 670 VAL A 674 1 O SER A 672 N ILE A 647
SHEET 7 AB2 8 ASN A 718 GLY A 724 1 O LEU A 720 N VAL A 673
SHEET 8 AB2 8 TYR A 749 TYR A 754 1 O THR A 750 N ILE A 719
SHEET 1 AB3 3 ASP B 93 VAL B 94 0
SHEET 2 AB3 3 VAL B 103 ASN B 107 -1 O LEU B 106 N VAL B 94
SHEET 3 AB3 3 THR B 113 LEU B 117 -1 O THR B 114 N LYS B 105
SHEET 1 AB4 4 ARG B 129 VAL B 132 0
SHEET 2 AB4 4 TYR B 138 GLN B 147 -1 O LEU B 140 N SER B 131
SHEET 3 AB4 4 TYR B 153 ASN B 161 -1 O THR B 154 N LYS B 146
SHEET 4 AB4 4 VAL B 167 LEU B 170 -1 O TRP B 168 N ILE B 159
SHEET 1 AB5 3 LEU B 192 PHE B 196 0
SHEET 2 AB5 3 ASN B 199 GLN B 203 -1 O GLN B 203 N LEU B 192
SHEET 3 AB5 3 LEU B 211 ARG B 212 -1 O LEU B 211 N TYR B 202
SHEET 1 AB6 3 ILE B 222 ASN B 224 0
SHEET 2 AB6 3 ARG B 250 ASN B 257 -1 O ILE B 256 N PHE B 223
SHEET 3 AB6 3 HIS B 242 TRP B 244 -1 N TRP B 243 O ALA B 252
SHEET 1 AB7 4 ILE B 222 ASN B 224 0
SHEET 2 AB7 4 ARG B 250 ASN B 257 -1 O ILE B 256 N PHE B 223
SHEET 3 AB7 4 THR B 291 ASN B 298 -1 O LYS B 293 N MET B 255
SHEET 4 AB7 4 LEU B 306 GLU B 307 -1 O LEU B 306 N VAL B 296
SHEET 1 AB8 2 THR B 263 VAL B 265 0
SHEET 2 AB8 2 GLN B 279 PRO B 281 -1 O TYR B 280 N MET B 264
SHEET 1 AB9 4 TYR B 319 TRP B 326 0
SHEET 2 AB9 4 LYS B 331 ASN B 338 -1 O LEU B 337 N TYR B 320
SHEET 3 AB9 4 ILE B 343 GLU B 350 -1 O CYS B 349 N THR B 332
SHEET 4 AB9 4 ALA B 355 THR B 363 -1 O TYR B 360 N LEU B 346
SHEET 1 AC1 3 VAL B 376 PHE B 377 0
SHEET 2 AC1 3 PHE B 384 VAL B 390 -1 O PHE B 385 N VAL B 376
SHEET 3 AC1 3 PHE B 398 ALA B 402 -1 O ALA B 402 N MET B 386
SHEET 1 AC2 4 VAL B 425 TYR B 431 0
SHEET 2 AC2 4 LYS B 437 SER B 442 -1 O TYR B 439 N ALA B 430
SHEET 3 AC2 4 GLN B 451 SER B 456 -1 O TYR B 453 N PHE B 440
SHEET 4 AC2 4 ARG B 463 CYS B 465 -1 O GLN B 464 N SER B 454
SHEET 1 AC3 4 ASP B 479 PHE B 482 0
SHEET 2 AC3 4 HIS B 488 PHE B 492 -1 O LEU B 490 N SER B 481
SHEET 3 AC3 4 VAL B 501 SER B 505 -1 O SER B 502 N LEU B 491
SHEET 4 AC3 4 PHE B 513 GLU B 516 -1 O PHE B 513 N LEU B 503
SHEET 1 AC4 8 GLU B 534 ILE B 540 0
SHEET 2 AC4 8 TYR B 543 SER B 550 -1 O LEU B 549 N GLU B 534
SHEET 3 AC4 8 VAL B 594 PHE B 599 -1 O ARG B 598 N GLN B 548
SHEET 4 AC4 8 TYR B 561 ILE B 566 1 N LEU B 564 O ALA B 597
SHEET 5 AC4 8 ILE B 640 LYS B 650 1 O SER B 646 N LEU B 563
SHEET 6 AC4 8 CYS B 670 VAL B 674 1 O SER B 672 N ILE B 647
SHEET 7 AC4 8 ASN B 718 GLY B 724 1 O LEU B 720 N VAL B 673
SHEET 8 AC4 8 TYR B 749 TYR B 754 1 O THR B 750 N ILE B 719
SSBOND 1 CYS A 349 CYS A 356 1555 1555 2.05
SSBOND 2 CYS A 465 CYS A 468 1555 1555 2.03
SSBOND 3 CYS A 475 CYS A 493 1555 1555 1.97
SSBOND 4 CYS A 670 CYS A 780 1555 1555 2.03
SSBOND 5 CYS B 349 CYS B 356 1555 1555 2.04
SSBOND 6 CYS B 465 CYS B 468 1555 1555 2.03
SSBOND 7 CYS B 475 CYS B 493 1555 1555 2.01
SSBOND 8 CYS B 670 CYS B 780 1555 1555 2.04
LINK ND2 ASN A 111 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 119 C1 NAG A 802 1555 1555 1.48
LINK ND2 ASN A 257 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN A 342 C1 NAG A 807 1555 1555 1.44
LINK ND2 ASN B 111 C1 NAG B 801 1555 1555 1.46
LINK ND2 ASN B 119 C1 NAG B 802 1555 1555 1.49
LINK ND2 ASN B 257 C1 NAG B 804 1555 1555 1.43
LINK ND2 ASN B 342 C1 NAG B 807 1555 1555 1.45
LINK ND2 ASN B 748 C1 NAG B 809 1555 1555 1.44
LINK O4 NAG A 803 C1 NAG A 804 1555 1555 1.45
LINK O4 NAG A 804 C1 BMA A 805 1555 1555 1.47
LINK O3 BMA A 805 C1 MAN A 806 1555 1555 1.46
LINK O4 NAG A 807 C1 NAG A 808 1555 1555 1.46
LINK O4 NAG B 802 C1 NAG B 803 1555 1555 1.46
LINK O4 NAG B 804 C1 NAG B 805 1555 1555 1.44
LINK O4 NAG B 805 C1 BMA B 806 1555 1555 1.47
LINK O4 NAG B 807 C1 NAG B 808 1555 1555 1.45
SITE 1 AC1 4 GLU A 109 ASN A 111 TYR A 512 PHE A 513
SITE 1 AC2 3 ASN A 100 HIS A 102 ASN A 119
SITE 1 AC3 7 ILE A 222 MET A 255 ASN A 257 SER A 259
SITE 2 AC3 7 LEU A 260 GLU B 523 LEU B 526
SITE 1 AC4 2 ASN A 342 GLU A 698
SITE 1 AC5 3 ASN B 111 TYR B 512 PHE B 513
SITE 1 AC6 3 ASN B 100 HIS B 102 ASN B 119
SITE 1 AC7 4 ILE B 222 MET B 255 ASN B 257 SER B 259
SITE 1 AC8 4 ASN B 342 THR B 363 SER B 364 GLU B 698
SITE 1 AC9 2 LYS A 775 ASN B 748
CRYST1 80.910 143.730 176.250 90.00 90.00 90.00 P 21 21 21 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 0.012359 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005674 0.00000
MTRIX1 1 -0.999919 -0.003172 0.012346 -40.51040 1
MTRIX2 1 0.006281 0.720166 0.693774 36.55450 1
MTRIX3 1 -0.011091 0.693795 -0.720087 -90.82720 1
TER 5795 LYS A 782
TER 11602 GLU B 783
MASTER 417 0 17 24 84 0 10 911829 2 254 112
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