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HEADER HYDROLASE 25-JUN-10 3NOX
TITLE CRYSTAL STRUCTURE OF HUMAN DPP-IV IN COMPLEX WITH SA-(+)-(6-
TITLE 2 (AMINOMETHYL)-5-(2,4-DICHLOROPHENYL)-7-METHYLIMIDAZO[1,2-A]PYRIMIDIN-
TITLE 3 2-YL)(MORPHOLINO)METHANONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL-PEPTIDASE 4 (CD26, ADENOSINE DEAMINASE
COMPND 3 COMPLEXING PROTEIN 2);
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: UNP RESIDUES 39 TO 766;
COMPND 6 SYNONYM: DIPEPTIDYLPEPTIDASE IV;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP4, HCG_39008;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 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
EXPDTA X-RAY DIFFRACTION
AUTHOR H.E.KLEI
REVDAT 1 11-AUG-10 3NOX 0
JRNL AUTH W.MENG,R.P.BRIGANCE,H.J.CHAO,A.FURA,T.HARRITY,
JRNL AUTH 2 J.MARCINKEVICIENE,S.P.O'CONNOR,J.K.TAMURA,D.XIE,Y.ZHANG,
JRNL AUTH 3 H.E.KLEI,K.KISH,C.A.WEIGELT,H.TURDI,A.WANG,R.ZAHLER,M.KIRBY,
JRNL AUTH 4 L.G.HAMANN
JRNL TITL DISCOVERY OF
JRNL TITL 2 6-(AMINOMETHYL)-5-(2,4-DICHLOROPHENYL)-7-DIMETHYLIMIDAZO[1,
JRNL TITL 3 2-A]PYRIMIDINE-2-CARBOXAMIDES AS POTENT, SELECTIVE
JRNL TITL 4 DIPEPTIDYL PEPTIDASE-4 (DPP4) INHIBITORS
JRNL REF J.MED.CHEM. 2010
JRNL REFN ISSN 0022-2623
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_446)
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) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.440
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.1
REMARK 3 NUMBER OF REFLECTIONS : 68723
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.240
REMARK 3 FREE R VALUE TEST SET COUNT : 1540
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 35.6279 - 5.1946 1.00 7507 171 0.1918 0.2419
REMARK 3 2 5.1946 - 4.1251 1.00 7230 159 0.1475 0.1886
REMARK 3 3 4.1251 - 3.6042 1.00 7133 164 0.1684 0.2442
REMARK 3 4 3.6042 - 3.2749 1.00 7091 168 0.2072 0.2951
REMARK 3 5 3.2749 - 3.0403 1.00 7057 159 0.2191 0.2914
REMARK 3 6 3.0403 - 2.8612 1.00 7048 156 0.2235 0.2954
REMARK 3 7 2.8612 - 2.7179 0.96 6711 161 0.2396 0.3322
REMARK 3 8 2.7179 - 2.5997 0.81 5639 154 0.2370 0.3141
REMARK 3 9 2.5997 - 2.4996 0.66 4639 95 0.2537 0.3849
REMARK 3 10 2.4996 - 2.4134 0.56 3898 81 0.2523 0.3202
REMARK 3 11 2.4134 - 2.3379 0.46 3230 72 0.2550 0.3356
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 26.43
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.82820
REMARK 3 B22 (A**2) : 16.08820
REMARK 3 B33 (A**2) : -11.26000
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 12514
REMARK 3 ANGLE : 1.158 17028
REMARK 3 CHIRALITY : 0.078 1815
REMARK 3 PLANARITY : 0.005 2135
REMARK 3 DIHEDRAL : 17.594 4509
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 3NOX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB060097.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
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) : 1.1
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 : 68839
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
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 (%) : 86.5
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
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: PDB ENTRY 3BJM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GROWN FROM 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-PRESERVED IN LN2., VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.72550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 210.22150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.53600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 210.22150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.72550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.53600
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 300 REMARK: DIMERIC
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: 8440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 41.0 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 LYS A 139 CE NZ
REMARK 470 ARG A 140 NE CZ NH1 NH2
REMARK 470 ASN A 179 O
REMARK 470 LYS A 250 CE NZ
REMARK 470 LYS A 391 NZ
REMARK 470 LYS A 392 CG CD CE NZ
REMARK 470 GLN A 761 CD OE1 NE2
REMARK 470 ARG B 40 NH1 NH2
REMARK 470 LYS B 41 CD CE NZ
REMARK 470 GLU B 97 CD OE1 OE2
REMARK 470 LYS B 250 CE NZ
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 LYS B 391 CE NZ
REMARK 470 LYS B 392 CD CE NZ
REMARK 470 GLN B 761 CD OE1 NE2
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 B 92 C2 NAG B 921 1.97
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 TYR A 58 80.93 -159.03
REMARK 500 HIS A 66 5.76 -151.47
REMARK 500 PHE A 95 3.41 80.82
REMARK 500 GLN A 123 -97.66 -106.77
REMARK 500 ARG A 140 57.59 32.88
REMARK 500 GLU A 146 62.20 20.07
REMARK 500 ASP A 192 -2.48 69.38
REMARK 500 ILE A 193 -62.09 -120.60
REMARK 500 VAL A 207 -69.49 -108.05
REMARK 500 SER A 242 -151.72 73.98
REMARK 500 SER A 275 67.99 -107.76
REMARK 500 THR A 307 -159.35 -135.19
REMARK 500 GLU A 309 19.10 -144.96
REMARK 500 GLN A 320 39.00 -83.42
REMARK 500 LYS A 373 143.77 -170.58
REMARK 500 ILE A 389 -77.04 -34.87
REMARK 500 ASP A 390 32.72 -86.87
REMARK 500 ASP A 393 -161.03 62.12
REMARK 500 ASP A 438 87.02 -154.61
REMARK 500 GLU A 464 5.76 54.38
REMARK 500 ASP A 515 -156.78 -138.64
REMARK 500 LYS A 536 -7.28 -59.80
REMARK 500 TYR A 547 -71.76 -124.91
REMARK 500 ARG A 596 11.42 55.42
REMARK 500 THR A 600 -93.85 -131.94
REMARK 500 ASN A 621 5.71 -64.65
REMARK 500 SER A 630 -122.82 52.57
REMARK 500 ASP A 678 -106.71 -114.04
REMARK 500 ASP A 739 -158.67 -102.05
REMARK 500 ILE A 742 55.85 36.49
REMARK 500 SER A 764 35.86 75.30
REMARK 500 HIS B 66 -2.90 -141.72
REMARK 500 ASN B 74 13.00 52.80
REMARK 500 LEU B 90 112.84 -161.13
REMARK 500 GLN B 123 -104.94 -98.66
REMARK 500 TRP B 124 -142.90 -88.67
REMARK 500 TRP B 154 142.03 -170.57
REMARK 500 HIS B 162 24.08 -141.72
REMARK 500 ILE B 193 -61.57 -129.60
REMARK 500 SER B 242 -156.90 47.51
REMARK 500 ALA B 289 152.32 -49.31
REMARK 500 ALA B 291 -36.21 -37.98
REMARK 500 GLN B 320 42.93 -77.01
REMARK 500 SER B 333 -72.91 -71.24
REMARK 500 SER B 334 -38.31 -34.06
REMARK 500 ASP B 393 -157.11 57.58
REMARK 500 ASN B 420 41.22 -109.52
REMARK 500 ASN B 450 76.15 -155.09
REMARK 500 GLU B 464 7.06 57.25
REMARK 500 ASP B 515 -160.26 -128.53
REMARK 500
REMARK 500 THIS ENTRY HAS 61 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 6A5 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 5201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6A5 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BJM RELATED DB: PDB
DBREF 3NOX A 39 766 UNP Q53TN1 Q53TN1_HUMAN 39 766
DBREF 3NOX B 39 766 UNP Q53TN1 Q53TN1_HUMAN 39 766
SEQADV 3NOX GLU A 37 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX PHE A 38 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX PRO A 767 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LEU A 768 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU A 769 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLN A 770 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LYS A 771 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LEU A 772 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ILE A 773 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX SER A 774 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU A 775 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU A 776 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ASP A 777 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LEU A 778 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ASN A 779 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX SER A 780 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ALA A 781 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX VAL A 782 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ASP A 783 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS A 784 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS A 785 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS A 786 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS A 787 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS A 788 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS A 789 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU B 37 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX PHE B 38 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX PRO B 767 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LEU B 768 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU B 769 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLN B 770 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LYS B 771 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LEU B 772 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ILE B 773 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX SER B 774 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU B 775 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX GLU B 776 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ASP B 777 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX LEU B 778 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ASN B 779 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX SER B 780 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ALA B 781 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX VAL B 782 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX ASP B 783 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS B 784 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS B 785 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS B 786 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS B 787 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS B 788 UNP Q53TN1 EXPRESSION TAG
SEQADV 3NOX HIS B 789 UNP Q53TN1 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 3NOX ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN B 92 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN B 520 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3NOX ASN A 520 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 6A5 A 1 28
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 B5201 14
HET 6A5 B 2 28
HET GOL B 1 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 6A5 SA-(+)-(6-(AMINOMETHYL)-5-(2,4-DICHLOROPHENYL)-7-
HETNAM 2 6A5 METHYLIMIDAZO[1,2-A]PYRIMIDIN-2-YL)(MORPHOLINO)
HETNAM 3 6A5 METHANONE
HETNAM GOL GLYCEROL
HETSYN 6A5 1-[5-(2,4-DICHLOROPHENYL)-7-METHYL-2-(MORPHOLIN-4-
HETSYN 2 6A5 YLCARBONYL)IMIDAZO[1,2-A]PYRIMIDIN-6-YL]METHANAMINE;
HETSYN 3 6A5 6-(AMINOMETHYL)-5-(2,4-DICHLOROPHENYL)-7-METHYL-2-
HETSYN 4 6A5 (MORPHOLIN-4-YLCARBONYL)IMIDAZO[1,2-A]PYRIMIDIN-4-IUM-
HETSYN 5 6A5 1-IDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 9 6A5 2(C19 H19 CL2 N5 O2)
FORMUL 17 GOL C3 H8 O3
FORMUL 18 HOH *479(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 PRO A 290 ILE A 295 1 6
HELIX 4 4 LEU A 340 GLN A 344 5 5
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 LYS A 463 ALA A 465 5 3
HELIX 7 7 ASN A 497 GLN A 505 1 9
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
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 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 HIS A 712 VAL A 726 1 15
HELIX 18 18 SER A 744 SER A 764 1 21
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 PRO B 290 ILE B 295 1 6
HELIX 22 22 VAL B 341 GLN B 344 5 4
HELIX 23 23 GLU B 421 MET B 425 5 5
HELIX 24 24 LYS B 463 ALA B 465 5 3
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ASP B 663 GLY B 672 1 10
HELIX 32 32 ASN B 679 SER B 686 1 8
HELIX 33 33 THR B 687 VAL B 698 5 12
HELIX 34 34 HIS B 712 VAL B 726 1 15
HELIX 35 35 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 SER A 87 N VAL A 78
SHEET 1 B 4 ASP A 104 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
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 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 TRP A 154 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
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 ILE A 285 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 VAL A 252 N TYR A 238
SHEET 1 G 4 HIS A 298 TRP A 305 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 G 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 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 TYR A 416 N ALA A 409
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 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 ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
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 ASN B 75 N GLN B 72
SHEET 4 M 4 SER B 86 LEU B 90 -1 O PHE B 89 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 THR B 129 N VAL B 121
SHEET 4 N 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 TRP B 154 TRP B 157 0
SHEET 2 O 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 O 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
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 VAL B 271 N LEU B 223
SHEET 4 Q 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 R 2 LEU B 235 PHE B 240 0
SHEET 2 R 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 S 4 HIS B 298 THR B 307 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 S 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 S 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 T 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
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 TYR B 416 N ALA B 409
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 V 4 VAL B 442 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 LEU B 519 0
SHEET 2 X 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 X 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 X 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 X 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 544
SHEET 6 X 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 X 8 GLU B 699 GLY B 705 1 O GLU B 699 N GLY B 650
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 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.07
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.06
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.09
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
LINK ND2 ASN A 229 C1 NAG A2291 1555 1555 1.43
LINK ND2 ASN B 92 C1 NAG B 921 1555 1555 1.43
LINK ND2 ASN B 520 C1 NAG B5201 1555 1555 1.43
LINK ND2 ASN B 85 C1 NAG B 851 1555 1555 1.43
LINK ND2 ASN A 150 C1 NAG A1501 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG B1501 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B2291 1555 1555 1.44
LINK ND2 ASN B 219 C1 NAG B2191 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A2191 1555 1555 1.44
LINK ND2 ASN A 85 C1 NAG A 851 1555 1555 1.44
LINK O4 NAG B2291 C1 NAG B2292 1555 1555 1.44
LINK ND2 ASN A 520 C1 NAG A5201 1555 1555 1.44
LINK O4 NAG A2291 C1 NAG A2292 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 10.97
CISPEP 2 GLY B 474 PRO B 475 0 11.65
SITE 1 AC1 9 VAL A 78 ASN A 80 ASN A 85 SER A 86
SITE 2 AC1 9 SER A 87 GLN A 388 THR A 395 HOH A 892
SITE 3 AC1 9 HOH A 894
SITE 1 AC2 3 ARG A 147 ILE A 148 ASN A 150
SITE 1 AC3 6 ASN A 219 THR A 221 PHE A 222 ASP A 274
SITE 2 AC3 6 GLU A 309 GLU A 332
SITE 1 AC4 5 ASN A 229 THR A 231 GLU A 232 HOH A1000
SITE 2 AC4 5 NAG A2292
SITE 1 AC5 2 HOH A 976 NAG A2291
SITE 1 AC6 2 TRP A 187 ASN A 281
SITE 1 AC7 5 ASN A 520 ARG A 581 GLU A 604 ASP A 605
SITE 2 AC7 5 HOH A 968
SITE 1 AC8 12 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC8 12 SER A 630 VAL A 656 TYR A 662 TYR A 666
SITE 3 AC8 12 ASN A 710 HIS A 740 HOH A 904 HOH A 990
SITE 1 AC9 9 VAL B 78 ASN B 85 SER B 86 SER B 87
SITE 2 AC9 9 TYR B 386 GLN B 388 THR B 395 HOH B 910
SITE 3 AC9 9 HOH B1026
SITE 1 BC1 4 GLU B 73 ASN B 75 ASN B 92 HOH B 974
SITE 1 BC2 2 ASN B 150 ASP B 515
SITE 1 BC3 6 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC3 6 HOH B 991 HOH B1002
SITE 1 BC4 4 ASN B 229 THR B 231 GLU B 232 NAG B2292
SITE 1 BC5 2 GLU B 232 NAG B2291
SITE 1 BC6 6 LEU B 519 ASN B 520 PHE B 524 ARG B 581
SITE 2 BC6 6 GLU B 604 HOH B 968
SITE 1 BC7 15 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 BC7 15 TRP B 629 SER B 630 VAL B 656 TYR B 662
SITE 3 BC7 15 TYR B 666 ASN B 710 HIS B 740 HOH B 820
SITE 4 BC7 15 HOH B 967 HOH B1004 HOH B1018
SITE 1 BC8 4 GLU A 244 HOH A 960 ARG B 684 THR B 687
CRYST1 65.451 67.072 420.443 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 0.015279 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014909 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002378 0.00000
TER 5941 PRO A 766
TER 11885 PRO B 766
MASTER 448 0 17 35 98 0 31 612612 2 289 116
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