| content |
HEADER HYDROLASE/HYDROLASE INHIBITOR 14-JUL-11 3SX4
TITLE CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH SA-(+)-3-
TITLE 2 (AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-6-(2-METHOXYPHENYL)- 2-METHYL-
TITLE 3 5H-PYRROLO[3,4-B]PYRIDIN-7(6H)-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 39-766;
COMPND 5 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 7 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV
COMPND 8 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL
COMPND 9 PEPTIDASE IV SOLUBLE FORM;
COMPND 10 EC: 3.4.14.5;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA
KEYWDS EXOPEPTIDASE, ALPHA/BETA HYDROLASE FOLD, BETA BARREL, BETA PROPELLER,
KEYWDS 2 DPP4, DIMER, PROTEIN:INHIBITOR COMPLEX, AMINOPEPTIDASE,
KEYWDS 3 GLYCOPROTEIN, MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE, SIGNAL-
KEYWDS 4 ANCHOR, TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.E.KLEI
REVDAT 1 26-OCT-11 3SX4 0
JRNL AUTH W.WANG,P.DEVASTHALE,A.WANG,T.HARRITY,D.EGAN,N.MORGAN,M.CAP,
JRNL AUTH 2 A.FURA,H.E.KLEI,K.KISH,C.WEIGELT,L.SUN,P.LEVESQUE,Y.X.LI,
JRNL AUTH 3 R.ZAHLER,M.S.KIRBY,L.G.HAMANN
JRNL TITL 7-OXOPYRROLOPYRIDINE-DERIVED DPP4 INHIBITORS-MITIGATION OF
JRNL TITL 2 CYP AND HERG LIABILITIES VIA INTRODUCTION OF POLAR
JRNL TITL 3 FUNCTIONALITIES IN THE ACTIVE SITE.
JRNL REF BIOORG.MED.CHEM.LETT. 2011
JRNL REFN ESSN 1464-3405
JRNL PMID 21996520
JRNL DOI 10.1016/J.BMCL.2011.09.074
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_780)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.440
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 57656
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2329
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 48.1045 - 6.6716 0.99 3640 151 0.1957 0.2865
REMARK 3 2 6.6716 - 5.2976 1.00 3476 161 0.1810 0.2483
REMARK 3 3 5.2976 - 4.6286 1.00 3431 157 0.1444 0.2021
REMARK 3 4 4.6286 - 4.2056 1.00 3420 133 0.1368 0.1958
REMARK 3 5 4.2056 - 3.9043 1.00 3409 119 0.1639 0.2123
REMARK 3 6 3.9043 - 3.6742 1.00 3361 141 0.1845 0.2732
REMARK 3 7 3.6742 - 3.4903 1.00 3370 145 0.2155 0.2931
REMARK 3 8 3.4903 - 3.3384 1.00 3381 148 0.2325 0.3169
REMARK 3 9 3.3384 - 3.2099 1.00 3327 152 0.2376 0.3018
REMARK 3 10 3.2099 - 3.0992 1.00 3349 128 0.2416 0.3086
REMARK 3 11 3.0992 - 3.0023 1.00 3334 142 0.2544 0.3594
REMARK 3 12 3.0023 - 2.9165 1.00 3362 153 0.2614 0.2909
REMARK 3 13 2.9165 - 2.8397 1.00 3297 140 0.2831 0.3744
REMARK 3 14 2.8397 - 2.7704 0.96 3198 146 0.3049 0.3698
REMARK 3 15 2.7704 - 2.7074 0.91 2998 127 0.3252 0.4333
REMARK 3 16 2.7074 - 2.6498 0.81 2745 104 0.3216 0.4199
REMARK 3 17 2.6498 - 2.5968 0.67 2229 82 0.3233 0.3892
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 : 0.31
REMARK 3 B_SOL : 30.12
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.820
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.51630
REMARK 3 B22 (A**2) : 7.51390
REMARK 3 B33 (A**2) : -14.03020
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 12464
REMARK 3 ANGLE : 1.189 16993
REMARK 3 CHIRALITY : 0.076 1813
REMARK 3 PLANARITY : 0.004 2129
REMARK 3 DIHEDRAL : 17.297 4419
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3SX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066761.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC Q315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000 (DENZO)
REMARK 200 DATA SCALING SOFTWARE : HKL2000 (SCALEPACK)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57759
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 3NOX.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GROWN IN 2 UL EQUIVOLUME
REMARK 280 MIXTURE OF PROTEIN SOLUTION (0.1 M NACL, 20 MM TRIS-HCL BUFFER PH
REMARK 280 7.8, 9.8 MG/ML PROTEIN) AND CRYSTALLIZATION SOLUTION (17% W/V PEG
REMARK 280 3350, 15% W/V GLYCEROL, 200 MM MGCL2, 100 MM TRIS-HCL BUFFER PH
REMARK 280 8.5). SUFFICIENT 100 MM LIGAND STOCK SOLUTION (NEAT DMSO) ADDED
REMARK 280 TO ACHIEVE 1 MM LIGAND CONCENTRATION. SOAKED OVERNIGHT. HARVESTED
REMARK 280 DIRECTLY AND CRYO-STORED IN LN2. 2. FOR CRYSTAL 2: OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.95250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 211.04750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.92700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 211.04750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.95250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.92700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 GLU A 37
REMARK 465 PHE A 38
REMARK 465 SER A 39
REMARK 465 PRO A 767
REMARK 465 LEU A 768
REMARK 465 GLU A 769
REMARK 465 GLN A 770
REMARK 465 LYS A 771
REMARK 465 LEU A 772
REMARK 465 ILE A 773
REMARK 465 SER A 774
REMARK 465 GLU A 775
REMARK 465 GLU A 776
REMARK 465 ASP A 777
REMARK 465 LEU A 778
REMARK 465 ASN A 779
REMARK 465 SER A 780
REMARK 465 ALA A 781
REMARK 465 VAL A 782
REMARK 465 ASP A 783
REMARK 465 HIS A 784
REMARK 465 HIS A 785
REMARK 465 HIS A 786
REMARK 465 HIS A 787
REMARK 465 HIS A 788
REMARK 465 HIS A 789
REMARK 465 GLU B 37
REMARK 465 PHE B 38
REMARK 465 SER B 39
REMARK 465 PRO B 767
REMARK 465 LEU B 768
REMARK 465 GLU B 769
REMARK 465 GLN B 770
REMARK 465 LYS B 771
REMARK 465 LEU B 772
REMARK 465 ILE B 773
REMARK 465 SER B 774
REMARK 465 GLU B 775
REMARK 465 GLU B 776
REMARK 465 ASP B 777
REMARK 465 LEU B 778
REMARK 465 ASN B 779
REMARK 465 SER B 780
REMARK 465 ALA B 781
REMARK 465 VAL B 782
REMARK 465 ASP B 783
REMARK 465 HIS B 784
REMARK 465 HIS B 785
REMARK 465 HIS B 786
REMARK 465 HIS B 787
REMARK 465 HIS B 788
REMARK 465 HIS B 789
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 ARG A 40 CD NE CZ NH1 NH2
REMARK 470 ARG A 54 NE CZ NH1 NH2
REMARK 470 LYS A 71 CD CE NZ
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 LYS A 139 CD CE NZ
REMARK 470 ARG A 140 CD NE CZ NH1 NH2
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 LYS A 175 CE NZ
REMARK 470 ASN A 179 O
REMARK 470 ASP A 243 OD1 OD2
REMARK 470 GLU A 244 CA
REMARK 470 LYS A 250 CD CE NZ
REMARK 470 ILE A 319 CD1
REMARK 470 GLU A 332 CG CD OE1 OE2
REMARK 470 GLU A 378 CG CD OE1 OE2
REMARK 470 LYS A 391 CE NZ
REMARK 470 LYS A 392 CE NZ
REMARK 470 LYS A 441 CE NZ
REMARK 470 LYS A 463 CG CD CE NZ
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 VAL A 486 CG1 CG2
REMARK 470 ASN A 487 OD1 ND2
REMARK 470 LYS A 489 CG CD CE NZ
REMARK 470 LYS A 502 CG CD CE NZ
REMARK 470 LYS A 513 CE NZ
REMARK 470 LYS A 589 CE NZ
REMARK 470 LYS A 696 CD CE NZ
REMARK 470 GLN A 761 CD OE1 NE2
REMARK 470 ARG B 40 NE CZ NH1 NH2
REMARK 470 LYS B 41 CD CE NZ
REMARK 470 ARG B 54 CZ NH1 NH2
REMARK 470 LEU B 90 CG CD1 CD2
REMARK 470 GLU B 97 CG CD OE1 OE2
REMARK 470 ASN B 138 CG OD1 ND2
REMARK 470 LYS B 139 CD CE NZ
REMARK 470 ARG B 140 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 143 CD1
REMARK 470 ARG B 147 NH1 NH2
REMARK 470 LYS B 190 CE NZ
REMARK 470 LYS B 250 CD CE NZ
REMARK 470 SER B 278 OG
REMARK 470 VAL B 279 CG1 CG2
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 LEU B 340 CG CD1 CD2
REMARK 470 LYS B 391 CD CE NZ
REMARK 470 LYS B 392 CG CD CE NZ
REMARK 470 ASP B 393 CG OD1 OD2
REMARK 470 LYS B 441 CE NZ
REMARK 470 GLU B 452 CG CD OE1 OE2
REMARK 470 LYS B 463 CE NZ
REMARK 470 LYS B 489 NZ
REMARK 470 LYS B 536 CG CD CE NZ
REMARK 470 LYS B 589 CD CE NZ
REMARK 470 LYS B 622 CD CE NZ
REMARK 470 GLN B 761 CD OE1 NE2
REMARK 470 LEU B 765 CD1 CD2
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 520 C2 NAG A 5201 2.05
REMARK 500 ND2 ASN A 150 C2 NAG A 1501 2.10
REMARK 500 NH2 ARG B 596 OD1 ASP B 678 2.14
REMARK 500 ND2 ASN B 85 C2 NAG B 851 2.18
REMARK 500 NH2 ARG A 596 OD1 ASP A 678 2.19
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 362 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO A 451 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO B 178 C - N - CA ANGL. DEV. = 10.3 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 SER A 64 -149.81 -165.97
REMARK 500 HIS A 66 2.79 -159.83
REMARK 500 ASN A 92 13.61 -64.98
REMARK 500 GLN A 123 -101.59 -108.45
REMARK 500 TRP A 124 -147.84 -90.49
REMARK 500 TYR A 128 -178.18 -174.73
REMARK 500 HIS A 162 31.79 -147.24
REMARK 500 PRO A 178 -52.06 -29.85
REMARK 500 ASP A 192 14.52 56.77
REMARK 500 ILE A 193 -57.53 -135.68
REMARK 500 SER A 242 -151.71 64.18
REMARK 500 SER A 275 60.34 -102.76
REMARK 500 ASN A 281 -160.74 -69.44
REMARK 500 THR A 307 -156.84 -137.31
REMARK 500 GLN A 320 38.08 -75.66
REMARK 500 ASP A 390 3.84 96.08
REMARK 500 ASP A 393 179.20 62.61
REMARK 500 TRP A 402 -176.21 -177.33
REMARK 500 LYS A 423 15.04 58.45
REMARK 500 ASP A 438 85.52 -160.91
REMARK 500 ASN A 450 68.87 -164.79
REMARK 500 GLU A 464 -23.50 82.46
REMARK 500 ALA A 465 38.18 76.42
REMARK 500 ASN A 487 48.98 -140.86
REMARK 500 TYR A 547 -75.26 -128.21
REMARK 500 ARG A 596 7.62 58.44
REMARK 500 THR A 600 -89.00 -115.42
REMARK 500 SER A 630 -130.20 55.67
REMARK 500 ASP A 678 -108.52 -118.74
REMARK 500 LYS A 696 7.18 -67.99
REMARK 500 ASP A 708 98.61 -59.47
REMARK 500 ASN A 710 -69.55 -101.25
REMARK 500 GLN A 714 -51.88 -21.98
REMARK 500 ILE A 742 58.43 38.90
REMARK 500 SER B 64 -168.14 -167.08
REMARK 500 HIS B 66 -2.27 -150.24
REMARK 500 GLN B 123 -105.42 -97.24
REMARK 500 TRP B 124 -140.76 -88.56
REMARK 500 LEU B 137 -72.14 -67.35
REMARK 500 ASN B 138 55.88 -64.28
REMARK 500 LYS B 139 -16.32 -175.50
REMARK 500 HIS B 162 36.97 -151.74
REMARK 500 PRO B 178 -27.47 -39.93
REMARK 500 ILE B 193 -64.47 -121.34
REMARK 500 SER B 242 -170.35 65.87
REMARK 500 GLU B 244 -33.59 -37.00
REMARK 500 THR B 307 -156.88 -119.29
REMARK 500 GLU B 309 12.06 -141.57
REMARK 500 CYS B 339 78.79 -105.09
REMARK 500 PHE B 371 165.74 179.64
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 2811
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 851
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KXA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 851
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 921
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2191
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KXA B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BJM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH (1S,3S,
REMARK 900 5S)-2-[(2S)-2-AMINO-2-(3-HYDROXYTRICYCLO[3.3.1.13,7]DEC-1-
REMARK 900 YL)ACETYL]-2-AZABICYCLO[3.1.0]HEXANE-3-CARBONITRILE (CAS),
REMARK 900 (1S,3S,5S)-2-((2S)-2-AMINO-2-(3-HYDROXYADAMANTAN-1- YL)
REMARK 900 ACETYL)-2-AZABICYCLO[3.1.0]HEXANE-3-CARBONITRILE (IUPAC),
REMARK 900 OR BMS-477118
REMARK 900 RELATED ID: 3NOX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH SA-(+)-
REMARK 900 (6-(AMINOMETHYL)-5-(2,4-DICHLOROPHENYL)-7-METHYLIMIDAZO[1,
REMARK 900 2-A]PYRIMIDIN-2-YL)(MORPHOLINO)METHANONE
REMARK 900 RELATED ID: 3SWW RELATED DB: PDB
REMARK 900 RELATED ID: 3Q0T RELATED DB: PDB
DBREF 3SX4 A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3SX4 B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3SX4 GLU A 37 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 PHE A 38 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 PRO A 767 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LEU A 768 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU A 769 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLN A 770 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LYS A 771 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LEU A 772 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ILE A 773 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 SER A 774 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU A 775 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU A 776 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ASP A 777 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LEU A 778 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ASN A 779 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 SER A 780 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ALA A 781 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 VAL A 782 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ASP A 783 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS A 784 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS A 785 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS A 786 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS A 787 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS A 788 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS A 789 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU B 37 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 PHE B 38 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 PRO B 767 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LEU B 768 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU B 769 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLN B 770 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LYS B 771 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LEU B 772 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ILE B 773 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 SER B 774 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU B 775 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 GLU B 776 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ASP B 777 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 LEU B 778 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ASN B 779 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 SER B 780 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ALA B 781 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 VAL B 782 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 ASP B 783 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS B 784 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS B 785 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS B 786 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS B 787 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS B 788 UNP P27487 EXPRESSION TAG
SEQADV 3SX4 HIS B 789 UNP P27487 EXPRESSION TAG
SEQRES 1 A 753 GLU PHE SER ARG LYS THR TYR THR LEU THR ASP TYR LEU
SEQRES 2 A 753 LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP
SEQRES 3 A 753 ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN
SEQRES 4 A 753 ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL
SEQRES 5 A 753 PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER
SEQRES 6 A 753 ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE
SEQRES 7 A 753 LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER
SEQRES 8 A 753 TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG
SEQRES 9 A 753 GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN
SEQRES 10 A 753 TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR
SEQRES 11 A 753 VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN
SEQRES 12 A 753 LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP
SEQRES 13 A 753 ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU
SEQRES 14 A 753 GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO
SEQRES 15 A 753 ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR
SEQRES 16 A 753 GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU
SEQRES 17 A 753 SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO
SEQRES 18 A 753 LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL
SEQRES 19 A 753 VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR
SEQRES 20 A 753 SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY
SEQRES 21 A 753 ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU
SEQRES 22 A 753 ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR
SEQRES 23 A 753 SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY
SEQRES 24 A 753 ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET
SEQRES 25 A 753 SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU
SEQRES 26 A 753 PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE
SEQRES 27 A 753 ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE
SEQRES 28 A 753 GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY
SEQRES 29 A 753 THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP
SEQRES 30 A 753 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO
SEQRES 31 A 753 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR
SEQRES 32 A 753 THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU
SEQRES 33 A 753 ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA
SEQRES 34 A 753 LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO
SEQRES 35 A 753 LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU
SEQRES 36 A 753 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 A 753 GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 A 753 ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU
SEQRES 39 A 753 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 A 753 LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 A 753 THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 A 753 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 A 753 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 A 753 ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 A 753 ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN
SEQRES 46 A 753 LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 A 753 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 A 753 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 A 753 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 A 753 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 A 753 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 A 753 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 A 753 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 A 753 VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 A 753 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 A 753 TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 57 A 753 LEU PRO PRO LEU GLU GLN LYS LEU ILE SER GLU GLU ASP
SEQRES 58 A 753 LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 753 GLU PHE SER ARG LYS THR TYR THR LEU THR ASP TYR LEU
SEQRES 2 B 753 LYS ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP
SEQRES 3 B 753 ILE SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN
SEQRES 4 B 753 ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL
SEQRES 5 B 753 PHE LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER
SEQRES 6 B 753 ILE ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE
SEQRES 7 B 753 LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER
SEQRES 8 B 753 TYR THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG
SEQRES 9 B 753 GLN LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN
SEQRES 10 B 753 TRP VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR
SEQRES 11 B 753 VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN
SEQRES 12 B 753 LEU PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP
SEQRES 13 B 753 ILE ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU
SEQRES 14 B 753 GLU VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO
SEQRES 15 B 753 ASN GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR
SEQRES 16 B 753 GLU VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU
SEQRES 17 B 753 SER LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO
SEQRES 18 B 753 LYS ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL
SEQRES 19 B 753 VAL ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR
SEQRES 20 B 753 SER ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY
SEQRES 21 B 753 ASP HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU
SEQRES 22 B 753 ARG ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR
SEQRES 23 B 753 SER VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY
SEQRES 24 B 753 ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET
SEQRES 25 B 753 SER THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU
SEQRES 26 B 753 PRO HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE
SEQRES 27 B 753 ILE SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE
SEQRES 28 B 753 GLN ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY
SEQRES 29 B 753 THR TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP
SEQRES 30 B 753 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO
SEQRES 31 B 753 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR
SEQRES 32 B 753 THR LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU
SEQRES 33 B 753 ARG CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA
SEQRES 34 B 753 LYS TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO
SEQRES 35 B 753 LEU TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU
SEQRES 36 B 753 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 B 753 GLN ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 B 753 ILE LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU
SEQRES 39 B 753 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 B 753 LEU ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 B 753 THR VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 B 753 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 B 753 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 B 753 ARG ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 B 753 ALA ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN
SEQRES 46 B 753 LYS ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 B 753 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 B 753 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 B 753 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 B 753 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 B 753 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 B 753 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 B 753 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 B 753 VAL GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 B 753 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 B 753 TYR THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 57 B 753 LEU PRO PRO LEU GLU GLN LYS LEU ILE SER GLU GLU ASP
SEQRES 58 B 753 LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
MODRES 3SX4 ASN B 520 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN B 281 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN B 92 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN A 520 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3SX4 ASN A 229 ASN GLYCOSYLATION SITE
HET NAG A 851 14
HET NAG A1501 14
HET NAG A2191 14
HET NAG A2291 14
HET NAG A2292 14
HET NAG A2811 14
HET NAG A5201 14
HET KXA A 1 58
HET NAG B 851 14
HET NAG B 921 14
HET NAG B1501 14
HET NAG B2191 14
HET NAG B2291 14
HET NAG B2292 14
HET NAG B2811 14
HET NAG B5201 14
HET KXA B 2 58
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM KXA 3-(AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-6-(2-
HETNAM 2 KXA METHOXYPHENYL)-2-METHYL-5,6-DIHYDRO-7H-PYRROLO[3,4-
HETNAM 3 KXA B]PYRIDIN-7-ONE
FORMUL 3 NAG 15(C8 H15 N O6)
FORMUL 9 KXA 2(C22 H19 CL2 N3 O2)
FORMUL 18 HOH *23(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 LYS A 463 ALA A 465 5 3
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 THR A 600 MET A 616 1 17
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 HIS A 712 GLY A 727 1 16
HELIX 17 17 SER A 744 PHE A 763 1 20
HELIX 18 18 THR B 44 ASN B 51 1 8
HELIX 19 19 GLU B 91 ASP B 96 5 6
HELIX 20 20 ASN B 138 ARG B 140 5 3
HELIX 21 21 ASP B 200 VAL B 207 1 8
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 LEU B 340 GLN B 344 5 5
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 LYS B 463 ALA B 465 5 3
HELIX 26 26 ASN B 497 LEU B 504 1 8
HELIX 27 27 GLN B 505 VAL B 507 5 3
HELIX 28 28 ASN B 562 THR B 570 1 9
HELIX 29 29 GLY B 587 ALA B 593 1 7
HELIX 30 30 THR B 600 LYS B 615 1 16
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 ARG B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 SER B 686 1 8
HELIX 35 35 VAL B 688 VAL B 698 5 11
HELIX 36 36 HIS B 712 ASP B 725 1 14
HELIX 37 37 SER B 744 PHE B 763 1 20
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 B 4 ILE A 102 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASN A 103
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 ILE A 143 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 TRP A 154 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 E 4 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 G 4 HIS A 298 TRP A 305 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 G 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 I 4 PRO A 362 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O ILE A 418 N ILE A 405
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 K 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 K 4 GLY A 490 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 L 8 VAL A 619 TRP A 629 1 O TRP A 627 N VAL A 546
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 4 ARG B 61 TRP B 62 0
SHEET 2 M 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 M 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 M 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 N 4 ILE B 102 ILE B 107 0
SHEET 2 N 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 N 4 TYR B 128 ASP B 136 -1 O ASP B 133 N LEU B 116
SHEET 4 N 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 TRP B 154 TRP B 157 0
SHEET 2 O 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 O 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 O 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 P 3 ILE B 194 ASN B 196 0
SHEET 2 P 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 P 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 Q 4 ILE B 194 ASN B 196 0
SHEET 2 Q 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 Q 4 ILE B 285 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 R 2 LEU B 235 PHE B 240 0
SHEET 2 R 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 S 4 HIS B 298 TRP B 305 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 S 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 S 4 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 1 T 4 HIS B 298 TRP B 305 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 T 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 U 4 PRO B 362 PHE B 364 0
SHEET 2 U 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 U 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 U 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 V 4 VAL B 404 LEU B 410 0
SHEET 2 V 4 TYR B 414 SER B 419 -1 O ILE B 418 N GLY B 406
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 V 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 W 4 TYR B 457 PHE B 461 0
SHEET 2 W 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 W 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 W 4 LYS B 489 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 X 8 SER B 511 ILE B 518 0
SHEET 2 X 8 LYS B 523 LEU B 530 -1 O MET B 528 N LYS B 513
SHEET 3 X 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 X 8 TYR B 540 ASP B 545 1 N ASP B 545 O ALA B 576
SHEET 5 X 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 544
SHEET 6 X 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 X 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 X 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.10
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.06
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.06
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
LINK ND2 ASN B 520 C1 NAG B5201 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B2291 1555 1555 1.43
LINK ND2 ASN A 85 C1 NAG A 851 1555 1555 1.43
LINK ND2 ASN A 150 C1 NAG A1501 1555 1555 1.43
LINK ND2 ASN B 281 C1 NAG B2811 1555 1555 1.43
LINK ND2 ASN B 92 C1 NAG B 921 1555 1555 1.43
LINK ND2 ASN A 520 C1 NAG A5201 1555 1555 1.44
LINK ND2 ASN B 150 C1 NAG B1501 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A2191 1555 1555 1.44
LINK ND2 ASN B 85 C1 NAG B 851 1555 1555 1.44
LINK ND2 ASN B 219 C1 NAG B2191 1555 1555 1.44
LINK O4 NAG A2291 C1 NAG A2292 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG A2291 1555 1555 1.44
LINK O4 NAG B2291 C1 NAG B2292 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 9.74
CISPEP 2 GLY B 474 PRO B 475 0 7.37
SITE 1 AC1 6 VAL A 78 ASN A 85 SER A 86 SER A 87
SITE 2 AC1 6 GLN A 388 THR A 395
SITE 1 AC2 2 ILE A 148 ASN A 150
SITE 1 AC3 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC4 4 ASN A 229 GLU A 232 LYS A 267 NAG A2292
SITE 1 AC5 2 GLU A 232 NAG A2291
SITE 1 AC6 3 TRP A 187 VAL A 279 ASN A 281
SITE 1 AC7 4 LEU A 519 ASN A 520 ARG A 581 ASP A 605
SITE 1 AC8 11 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC8 11 TRP A 629 SER A 630 TYR A 631 TYR A 662
SITE 3 AC8 11 TYR A 666 ASN A 710 HIS A 740
SITE 1 AC9 8 VAL B 78 ASN B 80 ASN B 85 SER B 86
SITE 2 AC9 8 SER B 87 TYR B 386 GLN B 388 THR B 395
SITE 1 BC1 3 GLU B 73 ASN B 75 ASN B 92
SITE 1 BC2 3 ARG B 147 ILE B 148 ASN B 150
SITE 1 BC3 4 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 1 BC4 5 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 BC4 5 NAG B2292
SITE 1 BC5 1 NAG B2291
SITE 1 BC6 1 ASN B 281
SITE 1 BC7 5 LEU B 519 ASN B 520 ARG B 581 GLU B 604
SITE 2 BC7 5 ASP B 605
SITE 1 BC8 12 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 BC8 12 TRP B 629 SER B 630 TYR B 631 TRP B 659
SITE 3 BC8 12 TYR B 662 TYR B 666 ASN B 710 HIS B 740
CRYST1 65.905 67.854 422.095 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014738 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002369 0.00000
TER 5884 PRO A 766
TER 11761 PRO B 766
MASTER 530 0 17 37 98 0 25 612042 2 358 116
END |