content |
HEADER HYDROLASE 02-AUG-05 2AJL
TITLE X-RAY STRUCTURE OF NOVEL BIARYL-BASED DIPEPTIDYL PEPTIDASE
TITLE 2 IV INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: I, J;
COMPND 4 FRAGMENT: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, RESIDUES 39-
COMPND 5 766;
COMPND 6 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL
COMPND 7 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE
COMPND 8 COMPLEXING PROTEIN 2, ADABP;
COMPND 9 EC: 3.4.14.5;
COMPND 10 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: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS AMINOPEPTIDASE, HYDROLASE, PROTEASE, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.QIAO,C.A.BAUMANN,C.S.CRYSLER,N.S.NINAN,M.C.ABAD,
AUTHOR 2 J.C.SPURLINO,R.L.DESJARLAIS,J.KERVINEN,M.P.NEEPER,
AUTHOR 3 S.S.BAYOUMY
REVDAT 3 24-FEB-09 2AJL 1 VERSN
REVDAT 2 22-NOV-05 2AJL 1 JRNL
REVDAT 1 08-NOV-05 2AJL 0
JRNL AUTH L.QIAO,C.A.BAUMANN,C.S.CRYSLER,N.S.NINAN,M.C.ABAD,
JRNL AUTH 2 J.C.SPURLINO,R.L.DESJARLAIS,J.KERVINEN,M.P.NEEPER,
JRNL AUTH 3 S.S.BAYOUMY,R.WILLIAMS,I.C.DECKMAN,M.DASGUPTA,
JRNL AUTH 4 R.L.REED,N.D.HUEBERT,B.E.TOMCZUK,K.J.MORIARTY
JRNL TITL DISCOVERY, SAR, AND X-RAY STRUCTURE OF NOVEL
JRNL TITL 2 BIARYL-BASED DIPEPTIDYL PEPTIDASE IV INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 123 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16236500
JRNL DOI 10.1016/J.BMCL.2005.09.037
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 55940
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5678
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11911
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 244
REMARK 3 SOLVENT ATOMS : 403
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.80
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.82
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AJL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-05.
REMARK 100 THE RCSB ID CODE IS RCSB033970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM
REMARK 200 DATA SCALING SOFTWARE : PROTEUM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55940
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 64.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.37400
REMARK 200 R SYM (I) : 0.12300
REMARK 200 FOR THE DATA SET : 5.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35800
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1N1M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.43850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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 I 39
REMARK 465 ARG I 40
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 OG SER J 630 C1 JNH J 1 2.09
REMARK 500 CB SER I 630 C20 JNH I 1 2.15
REMARK 500 O PHE I 98 N HIS I 100 2.18
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 GLN I 388 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 PRO I 766 CA - C - O ANGL. DEV. = 23.0 DEGREES
REMARK 500 PRO J 766 CA - C - O ANGL. DEV. = 22.1 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 GLU I 73 -117.74 75.09
REMARK 500 GLU I 82 -82.17 -72.68
REMARK 500 SER I 87 138.69 -177.34
REMARK 500 VAL I 88 96.31 -57.26
REMARK 500 THR I 94 -68.26 -10.72
REMARK 500 ASP I 96 -108.30 -96.41
REMARK 500 PHE I 98 89.42 158.25
REMARK 500 ASP I 104 126.00 63.48
REMARK 500 TYR I 105 -163.69 -100.54
REMARK 500 SER I 106 96.97 -174.66
REMARK 500 ASN I 119 19.60 88.04
REMARK 500 LYS I 122 129.19 -39.91
REMARK 500 GLN I 123 -112.43 -119.12
REMARK 500 TRP I 124 -155.50 -77.48
REMARK 500 HIS I 126 -32.08 -132.33
REMARK 500 TYR I 128 154.76 168.46
REMARK 500 ARG I 140 21.45 36.17
REMARK 500 THR I 144 -34.77 -136.24
REMARK 500 GLU I 146 3.10 58.61
REMARK 500 ARG I 147 142.94 -24.09
REMARK 500 PRO I 149 175.59 -50.27
REMARK 500 TRP I 154 140.74 176.54
REMARK 500 THR I 156 144.95 176.11
REMARK 500 PRO I 181 152.18 -46.05
REMARK 500 LYS I 190 95.60 -165.35
REMARK 500 GLU I 191 118.91 -14.07
REMARK 500 ILE I 193 -70.75 -146.37
REMARK 500 VAL I 207 -75.63 -115.23
REMARK 500 SER I 209 48.29 35.62
REMARK 500 SER I 242 -162.60 63.80
REMARK 500 GLU I 244 -33.37 -36.94
REMARK 500 ALA I 259 123.46 -29.21
REMARK 500 ASP I 274 -17.96 -167.85
REMARK 500 ALA I 282 107.02 9.63
REMARK 500 THR I 288 -153.84 -80.99
REMARK 500 ALA I 289 -160.05 39.37
REMARK 500 GLN I 320 44.50 -72.44
REMARK 500 GLU I 332 -88.16 -11.79
REMARK 500 SER I 334 -35.32 150.99
REMARK 500 PHE I 357 -10.56 -160.68
REMARK 500 SER I 360 161.28 -44.81
REMARK 500 THR I 401 64.54 -68.26
REMARK 500 TYR I 422 133.10 -19.32
REMARK 500 LYS I 423 8.68 49.17
REMARK 500 CYS I 447 -57.21 -18.67
REMARK 500 ASN I 450 67.29 -164.28
REMARK 500 LYS I 463 3.31 -51.09
REMARK 500 GLU I 464 37.88 -171.76
REMARK 500 PRO I 478 135.07 -37.52
REMARK 500 ARG I 492 -179.02 -179.57
REMARK 500 GLN I 508 51.11 -66.92
REMARK 500 MET I 509 150.47 -42.78
REMARK 500 ASP I 515 -159.94 -144.13
REMARK 500 GLU I 521 -67.09 80.05
REMARK 500 LYS I 536 0.52 -64.08
REMARK 500 TYR I 547 -50.26 -134.54
REMARK 500 CYS I 551 45.63 75.32
REMARK 500 ASN I 572 61.59 38.18
REMARK 500 GLN I 586 14.04 -142.90
REMARK 500 ARG I 597 42.57 -153.03
REMARK 500 THR I 600 -89.35 -127.44
REMARK 500 LYS I 615 13.95 -61.18
REMARK 500 ASN I 621 -37.62 -34.90
REMARK 500 SER I 630 -121.71 49.58
REMARK 500 SER I 657 -32.61 -130.13
REMARK 500 SER I 664 -75.23 -56.03
REMARK 500 VAL I 665 -57.79 -28.07
REMARK 500 PRO I 674 34.00 -70.89
REMARK 500 ASP I 678 -97.17 -110.01
REMARK 500 LEU I 680 -34.29 -35.63
REMARK 500 ASN I 710 -85.55 -85.65
REMARK 500 ASP I 737 14.44 54.92
REMARK 500 ASP I 739 -156.05 -94.42
REMARK 500 ILE I 742 48.13 37.67
REMARK 500 SER I 744 150.04 -48.22
REMARK 500 ASN J 51 54.31 30.46
REMARK 500 TYR J 58 77.17 -161.13
REMARK 500 ARG J 61 69.44 -168.71
REMARK 500 ASN J 74 -25.62 177.81
REMARK 500 VAL J 88 98.71 -67.39
REMARK 500 THR J 94 -55.36 -149.07
REMARK 500 PHE J 95 40.45 -98.12
REMARK 500 GLU J 97 10.11 59.44
REMARK 500 ASP J 104 119.46 -179.17
REMARK 500 GLN J 123 -97.44 -115.27
REMARK 500 TRP J 124 -153.36 -92.07
REMARK 500 ALA J 130 -174.09 -176.90
REMARK 500 PRO J 149 158.58 -46.59
REMARK 500 TRP J 157 -159.32 -79.61
REMARK 500 HIS J 162 48.53 -157.76
REMARK 500 LYS J 190 124.88 -172.91
REMARK 500 ASP J 192 -1.11 63.94
REMARK 500 ALA J 213 44.47 -147.33
REMARK 500 THR J 231 -37.68 -35.75
REMARK 500 SER J 242 -171.51 60.37
REMARK 500 THR J 273 8.66 -69.20
REMARK 500 LEU J 276 -74.46 -80.74
REMARK 500 SER J 277 91.98 -9.43
REMARK 500 SER J 278 -158.54 -167.52
REMARK 500 THR J 288 -144.85 -92.99
REMARK 500 ALA J 289 -156.20 30.00
REMARK 500 THR J 307 -159.79 -147.35
REMARK 500 GLN J 320 44.79 -60.21
REMARK 500 GLU J 378 -18.20 -49.27
REMARK 500 ILE J 389 -75.52 48.37
REMARK 500 ASP J 393 179.88 62.54
REMARK 500 ASP J 413 -72.16 -77.22
REMARK 500 TYR J 422 131.93 -37.32
REMARK 500 LYS J 423 21.71 42.87
REMARK 500 ASP J 438 101.44 -161.53
REMARK 500 LYS J 441 57.75 -91.84
REMARK 500 ASN J 450 77.18 -159.46
REMARK 500 PRO J 451 -72.30 -45.79
REMARK 500 PRO J 478 115.47 -38.14
REMARK 500 VAL J 486 -70.58 -37.36
REMARK 500 ASP J 488 26.28 48.34
REMARK 500 GLU J 495 128.22 -179.35
REMARK 500 ASN J 497 49.17 29.27
REMARK 500 ASN J 506 35.40 -169.98
REMARK 500 PHE J 534 88.84 -38.01
REMARK 500 LYS J 536 -7.19 -54.79
REMARK 500 TYR J 547 -57.43 -139.68
REMARK 500 GLN J 553 109.90 -160.84
REMARK 500 ASN J 562 -157.02 -135.66
REMARK 500 GLN J 586 24.60 -140.93
REMARK 500 ARG J 596 15.55 55.64
REMARK 500 ARG J 597 50.40 -140.61
REMARK 500 THR J 600 -98.67 -125.87
REMARK 500 SER J 630 -113.46 54.99
REMARK 500 ALA J 654 63.78 30.84
REMARK 500 PRO J 674 44.59 -84.96
REMARK 500 ASP J 678 -91.73 -127.98
REMARK 500 SER J 686 34.82 -93.07
REMARK 500 ASN J 710 -73.96 -85.04
REMARK 500 MET J 733 115.49 -165.87
REMARK 500 HIS J 740 -21.90 -38.34
REMARK 500 SER J 764 63.25 38.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR J 700 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH I 879 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH J 912 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH I 922 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH J 926 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH J 948 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH I 948 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH J 954 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH I 961 DISTANCE = 6.60 ANGSTROMS
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 I 767
REMARK 610 NAG I 768
REMARK 610 NAG I 769
REMARK 610 NAG I 770
REMARK 610 NAG I 771
REMARK 610 NAG J 767
REMARK 610 NAG J 768
REMARK 610 NAG J 769
REMARK 610 NAG J 770
REMARK 610 NAG J 771
REMARK 610 NAG J 772
REMARK 610 NAG J 773
REMARK 610 NAG J 774
REMARK 610 NAG J 775
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 767
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 768
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 769
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 770
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG I 771
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 767
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 768
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 769
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 770
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 771
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 772
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 773
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 774
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 775
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JNH I 1
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JNH J 1
DBREF 2AJL I 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2AJL J 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQRES 1 I 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 I 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 I 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 I 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 I 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 I 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 I 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 I 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 I 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 I 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 I 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 I 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 I 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 I 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 I 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 I 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 I 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 I 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 I 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 I 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 I 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 I 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 I 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 I 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 I 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 I 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 I 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 I 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 I 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 I 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 I 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 I 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 I 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 I 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 I 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 I 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 I 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 I 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 I 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 I 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 I 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 I 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 I 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 I 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 I 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 I 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 I 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 I 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 I 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 I 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 I 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 I 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 I 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 I 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 I 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 I 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 J 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 J 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 J 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 J 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 J 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 J 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 J 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 J 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 J 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 J 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 J 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 J 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 J 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 J 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 J 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 J 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 J 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 J 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 J 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 J 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 J 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 J 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 J 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 J 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 J 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 J 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 J 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 J 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 J 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 J 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 J 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 J 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 J 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 J 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 J 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 J 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 J 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 J 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 J 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 J 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 J 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 J 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 J 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 J 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 J 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 J 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 J 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 J 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 J 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 J 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 J 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 J 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 J 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 J 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 J 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 J 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET NAG I 767 14
HET NAG I 768 14
HET NAG I 769 14
HET NAG I 770 14
HET NAG I 771 14
HET NAG J 767 14
HET NAG J 768 14
HET NAG J 769 14
HET NAG J 770 14
HET NAG J 771 14
HET NAG J 772 14
HET NAG J 773 14
HET NAG J 774 14
HET NAG J 775 14
HET JNH I 1 24
HET JNH J 1 24
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM JNH 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-
HETNAM 2 JNH 2-(S)-CARBONITRILE
HETSYN NAG NAG
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 17 JNH 2(C20 H25 N3 O)
FORMUL 19 HOH *403(H2 O)
HELIX 1 1 THR I 44 ASN I 51 1 8
HELIX 2 2 ASP I 200 VAL I 207 1 8
HELIX 3 3 PRO I 290 ILE I 295 1 6
HELIX 4 4 LEU I 340 GLN I 344 5 5
HELIX 5 5 GLU I 421 MET I 425 5 5
HELIX 6 6 ASN I 497 GLN I 505 1 9
HELIX 7 7 ASN I 562 ASN I 572 1 11
HELIX 8 8 GLY I 587 HIS I 592 1 6
HELIX 9 9 THR I 600 LYS I 615 1 16
HELIX 10 10 SER I 630 GLY I 641 1 12
HELIX 11 11 ARG I 658 TYR I 662 5 5
HELIX 12 12 ASP I 663 GLY I 672 1 10
HELIX 13 13 ASN I 679 SER I 686 1 8
HELIX 14 14 THR I 687 VAL I 698 5 12
HELIX 15 15 HIS I 712 GLY I 727 1 16
HELIX 16 16 SER I 744 PHE I 763 1 20
HELIX 17 17 THR J 44 LYS J 50 1 7
HELIX 18 18 ASP J 200 GLU J 206 1 7
HELIX 19 19 PRO J 290 ILE J 295 1 6
HELIX 20 20 LEU J 340 GLN J 344 5 5
HELIX 21 21 GLU J 421 MET J 425 5 5
HELIX 22 22 ASN J 497 LEU J 504 1 8
HELIX 23 23 ASN J 562 THR J 570 1 9
HELIX 24 24 GLY J 587 HIS J 592 1 6
HELIX 25 25 ALA J 593 ASN J 595 5 3
HELIX 26 26 THR J 600 LYS J 615 1 16
HELIX 27 27 SER J 630 GLY J 641 1 12
HELIX 28 28 ARG J 658 TYR J 662 5 5
HELIX 29 29 ASP J 663 GLY J 672 1 10
HELIX 30 30 ASN J 679 SER J 686 1 8
HELIX 31 31 VAL J 688 VAL J 698 5 11
HELIX 32 32 PHE J 713 VAL J 726 1 14
HELIX 33 33 SER J 744 PHE J 763 1 20
SHEET 1 A 4 LEU I 60 TRP I 62 0
SHEET 2 A 4 GLU I 67 GLN I 72 -1 O LEU I 69 N ARG I 61
SHEET 3 A 4 ASN I 75 ASN I 80 -1 O ASN I 75 N GLN I 72
SHEET 4 A 4 SER I 86 VAL I 88 -1 O SER I 87 N VAL I 78
SHEET 1 B 3 ILE I 102 ILE I 107 0
SHEET 2 B 3 ILE I 114 LYS I 122 -1 O GLU I 117 N ASN I 103
SHEET 3 B 3 TYR I 128 ASP I 133 -1 O SER I 131 N TYR I 118
SHEET 1 C 4 TRP I 154 TRP I 157 0
SHEET 2 C 4 LEU I 164 TRP I 168 -1 O VAL I 167 N TRP I 154
SHEET 3 C 4 ASP I 171 LYS I 175 -1 O LYS I 175 N LEU I 164
SHEET 4 C 4 TYR I 183 ARG I 184 -1 O TYR I 183 N VAL I 174
SHEET 1 D 3 ILE I 194 ASN I 196 0
SHEET 2 D 3 PHE I 222 ASN I 229 -1 O PHE I 228 N TYR I 195
SHEET 3 D 3 LEU I 214 TRP I 216 -1 N TRP I 215 O ALA I 224
SHEET 1 E 4 ILE I 194 ASN I 196 0
SHEET 2 E 4 PHE I 222 ASN I 229 -1 O PHE I 228 N TYR I 195
SHEET 3 E 4 THR I 265 ASN I 272 -1 O VAL I 271 N LEU I 223
SHEET 4 E 4 ILE I 285 GLN I 286 -1 O ILE I 285 N VAL I 270
SHEET 1 F 2 LEU I 235 PHE I 240 0
SHEET 2 F 2 LYS I 250 PRO I 255 -1 O LYS I 250 N PHE I 240
SHEET 1 G 4 HIS I 298 THR I 307 0
SHEET 2 G 4 ARG I 310 ARG I 317 -1 O GLN I 314 N CYS I 301
SHEET 3 G 4 TYR I 322 TYR I 330 -1 O VAL I 324 N TRP I 315
SHEET 4 G 4 TRP I 337 ASN I 338 -1 O ASN I 338 N ASP I 329
SHEET 1 H 4 HIS I 298 THR I 307 0
SHEET 2 H 4 ARG I 310 ARG I 317 -1 O GLN I 314 N CYS I 301
SHEET 3 H 4 TYR I 322 TYR I 330 -1 O VAL I 324 N TRP I 315
SHEET 4 H 4 HIS I 345 MET I 348 -1 O GLU I 347 N SER I 323
SHEET 1 I 4 HIS I 363 PHE I 364 0
SHEET 2 I 4 SER I 370 SER I 376 -1 O TYR I 372 N HIS I 363
SHEET 3 I 4 ARG I 382 GLN I 388 -1 O PHE I 387 N PHE I 371
SHEET 4 I 4 LYS I 391 PHE I 396 -1 O LYS I 391 N GLN I 388
SHEET 1 J 4 VAL I 404 LEU I 410 0
SHEET 2 J 4 TYR I 414 SER I 419 -1 O TYR I 416 N ALA I 409
SHEET 3 J 4 ASN I 430 GLN I 435 -1 O TYR I 432 N TYR I 417
SHEET 4 J 4 ASP I 438 CYS I 444 -1 O THR I 443 N LYS I 433
SHEET 1 K 4 CYS I 454 PHE I 461 0
SHEET 2 K 4 TYR I 467 PRO I 475 -1 O GLY I 474 N GLN I 455
SHEET 3 K 4 LEU I 479 SER I 484 -1 O LEU I 479 N CYS I 472
SHEET 4 K 4 GLY I 490 GLU I 495 -1 O LEU I 491 N LEU I 482
SHEET 1 L 8 SER I 511 ILE I 518 0
SHEET 2 L 8 LYS I 523 LEU I 530 -1 O LEU I 530 N SER I 511
SHEET 3 L 8 ILE I 574 PHE I 578 -1 O SER I 577 N GLN I 527
SHEET 4 L 8 TYR I 540 VAL I 546 1 N ASP I 545 O ALA I 576
SHEET 5 L 8 VAL I 619 TRP I 629 1 O ALA I 625 N LEU I 544
SHEET 6 L 8 CYS I 649 VAL I 653 1 O VAL I 653 N GLY I 628
SHEET 7 L 8 GLU I 699 GLY I 705 1 O LEU I 701 N ALA I 652
SHEET 8 L 8 GLN I 731 TYR I 735 1 O GLN I 731 N TYR I 700
SHEET 1 M 2 LYS J 41 THR J 42 0
SHEET 2 M 2 VAL J 507 GLN J 508 1 O GLN J 508 N LYS J 41
SHEET 1 N 3 GLU J 67 LYS J 71 0
SHEET 2 N 3 ILE J 76 ASN J 80 -1 O LEU J 77 N TYR J 70
SHEET 3 N 3 SER J 86 SER J 87 -1 O SER J 87 N VAL J 78
SHEET 1 O 4 ILE J 102 ILE J 107 0
SHEET 2 O 4 PHE J 113 LYS J 122 -1 O LEU J 115 N SER J 106
SHEET 3 O 4 TYR J 128 ASP J 136 -1 O SER J 131 N TYR J 118
SHEET 4 O 4 GLN J 141 LEU J 142 -1 O GLN J 141 N ASP J 136
SHEET 1 P 4 TRP J 154 THR J 156 0
SHEET 2 P 4 LEU J 164 TRP J 168 -1 O VAL J 167 N TRP J 154
SHEET 3 P 4 ASP J 171 LYS J 175 -1 O TYR J 173 N TYR J 166
SHEET 4 P 4 TYR J 183 ARG J 184 -1 O TYR J 183 N VAL J 174
SHEET 1 Q 3 ILE J 194 ASN J 196 0
SHEET 2 Q 3 PHE J 222 ASN J 229 -1 O PHE J 228 N TYR J 195
SHEET 3 Q 3 LEU J 214 TRP J 216 -1 N TRP J 215 O ALA J 224
SHEET 1 R 4 ILE J 194 ASN J 196 0
SHEET 2 R 4 PHE J 222 ASN J 229 -1 O PHE J 228 N TYR J 195
SHEET 3 R 4 THR J 265 ASN J 272 -1 O PHE J 269 N TYR J 225
SHEET 4 R 4 ILE J 285 ILE J 287 -1 O ILE J 285 N VAL J 270
SHEET 1 S 2 LEU J 235 PHE J 240 0
SHEET 2 S 2 LYS J 250 PRO J 255 -1 O VAL J 252 N TYR J 238
SHEET 1 T 4 HIS J 298 TRP J 305 0
SHEET 2 T 4 ARG J 310 ARG J 317 -1 O LEU J 316 N TYR J 299
SHEET 3 T 4 TYR J 322 ASP J 331 -1 O ASP J 326 N LEU J 313
SHEET 4 T 4 ARG J 336 ASN J 338 -1 O ASN J 338 N ASP J 329
SHEET 1 U 4 HIS J 298 TRP J 305 0
SHEET 2 U 4 ARG J 310 ARG J 317 -1 O LEU J 316 N TYR J 299
SHEET 3 U 4 TYR J 322 ASP J 331 -1 O ASP J 326 N LEU J 313
SHEET 4 U 4 HIS J 345 MET J 348 -1 O GLU J 347 N SER J 323
SHEET 1 V 4 HIS J 363 PHE J 364 0
SHEET 2 V 4 PHE J 371 SER J 376 -1 O TYR J 372 N HIS J 363
SHEET 3 V 4 ARG J 382 PHE J 387 -1 O CYS J 385 N LYS J 373
SHEET 4 V 4 THR J 395 PHE J 396 -1 O THR J 395 N TYR J 386
SHEET 1 W 4 VAL J 404 LEU J 410 0
SHEET 2 W 4 TYR J 414 SER J 419 -1 O TYR J 416 N ALA J 409
SHEET 3 W 4 ASN J 430 GLN J 435 -1 O TYR J 432 N TYR J 417
SHEET 4 W 4 VAL J 442 CYS J 444 -1 O THR J 443 N LYS J 433
SHEET 1 X 4 CYS J 454 PHE J 461 0
SHEET 2 X 4 TYR J 467 PRO J 475 -1 O GLN J 469 N SER J 460
SHEET 3 X 4 LEU J 479 SER J 484 -1 O LEU J 479 N CYS J 472
SHEET 4 X 4 ARG J 492 GLU J 495 -1 O GLU J 495 N TYR J 480
SHEET 1 Y 8 SER J 511 LEU J 519 0
SHEET 2 Y 8 THR J 522 LEU J 530 -1 O THR J 522 N LEU J 519
SHEET 3 Y 8 ILE J 574 PHE J 578 -1 O VAL J 575 N ILE J 529
SHEET 4 Y 8 TYR J 540 VAL J 546 1 N ASP J 545 O ALA J 576
SHEET 5 Y 8 VAL J 619 TRP J 629 1 O ASP J 620 N TYR J 540
SHEET 6 Y 8 CYS J 649 VAL J 653 1 O VAL J 653 N GLY J 628
SHEET 7 Y 8 GLU J 699 GLY J 705 1 O LEU J 701 N ALA J 652
SHEET 8 Y 8 GLN J 731 TYR J 735 1 O GLN J 731 N LEU J 702
SSBOND 1 CYS I 328 CYS I 339 1555 1555 2.04
SSBOND 2 CYS I 385 CYS I 394 1555 1555 2.03
SSBOND 3 CYS I 444 CYS I 447 1555 1555 2.03
SSBOND 4 CYS I 454 CYS I 472 1555 1555 2.03
SSBOND 5 CYS I 649 CYS I 762 1555 1555 2.04
SSBOND 6 CYS J 328 CYS J 339 1555 1555 2.04
SSBOND 7 CYS J 385 CYS J 394 1555 1555 2.03
SSBOND 8 CYS J 444 CYS J 447 1555 1555 2.02
SSBOND 9 CYS J 454 CYS J 472 1555 1555 2.03
SSBOND 10 CYS J 649 CYS J 762 1555 1555 2.03
LINK C20 JNH I 1 OG SER I 630 1555 1555 1.31
LINK C20 JNH J 1 OG SER J 630 1555 1555 1.32
LINK C1 JNH I 1 OG SER I 630 1555 1555 1.91
CISPEP 1 ALA I 289 PRO I 290 0 -0.40
CISPEP 2 GLY I 474 PRO I 475 0 0.00
CISPEP 3 ALA J 289 PRO J 290 0 0.09
CISPEP 4 GLY J 474 PRO J 475 0 0.25
SITE 1 AC1 5 ASN I 80 ASN I 85 SER I 86 SER I 87
SITE 2 AC1 5 HOH I 884
SITE 1 AC2 5 ASN I 229 THR I 231 GLU I 232 NAG I 769
SITE 2 AC2 5 HOH I 914
SITE 1 AC3 1 NAG I 768
SITE 1 AC4 4 TRP I 187 ASN I 281 NAG I 771 HOH I 877
SITE 1 AC5 2 NAG I 770 HOH I 888
SITE 1 AC6 8 VAL J 78 ASN J 85 SER J 86 SER J 87
SITE 2 AC6 8 NAG J 768 HOH J 822 HOH J 859 HOH J 868
SITE 1 AC7 2 NAG J 767 HOH J 822
SITE 1 AC8 4 ASN J 219 GLN J 308 GLU J 309 NAG J 770
SITE 1 AC9 6 ASN J 272 ASP J 274 GLU J 309 TYR J 330
SITE 2 AC9 6 GLU J 332 NAG J 769
SITE 1 BC1 3 ASN J 229 THR J 231 NAG J 772
SITE 1 BC2 4 GLU J 232 NAG J 771 HOH J 814 HOH J 869
SITE 1 BC3 1 ASN J 281
SITE 1 BC4 3 ASN J 321 MET J 348 NAG J 775
SITE 1 BC5 3 ASP J 678 NAG J 774 HOH J 955
SITE 1 BC6 11 GLU I 205 GLU I 206 VAL I 207 SER I 209
SITE 2 BC6 11 PHE I 357 ARG I 358 TYR I 547 SER I 630
SITE 3 BC6 11 TYR I 631 TYR I 662 TYR I 666
SITE 1 BC7 13 ARG J 125 GLU J 205 GLU J 206 SER J 209
SITE 2 BC7 13 PHE J 357 ARG J 358 TYR J 547 SER J 630
SITE 3 BC7 13 TYR J 631 TYR J 662 TYR J 666 ASN J 710
SITE 4 BC7 13 HIS J 740
CRYST1 65.279 126.877 110.828 90.00 99.41 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015319 0.000000 0.002539 0.00000
SCALE2 0.000000 0.007882 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009146 0.00000
TER 5948 PRO I 766
TER 11913 PRO J 766
MASTER 508 0 16 33 98 0 25 612558 2 266 112
END |