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HEADER HYDROLASE/INHIBITOR 14-JUN-22 7Y4G
TITLE SIT-BOUND BTDPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BTDPP4;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: NCBI ACCESSION CODE: WP_022302284.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GUT MICROBIOTA, HYDROLASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HANG,C.JIANG,K.WANG,Z.ZHANG,F.GUO,J.LIU,G.WANG,X.LEI,F.GONZALEZ,
AUTHOR 2 J.QIAO
REVDAT 1 14-JUN-23 7Y4G 0
JRNL AUTH J.HANG,C.JIANG,K.WANG,Z.ZHANG,F.GUO,J.LIU,G.WANG,X.LEI,
JRNL AUTH 2 F.GONZALEZ,J.QIAO
JRNL TITL SIT-BOUND BTDPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20_4459
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.6
REMARK 3 NUMBER OF REFLECTIONS : 143666
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.380
REMARK 3 FREE R VALUE TEST SET COUNT : 1984
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 44.7900 - 4.7600 0.95 11572 165 0.2072 0.2443
REMARK 3 2 4.7600 - 3.7800 0.99 11893 166 0.1714 0.1935
REMARK 3 3 3.7800 - 3.3000 0.99 11926 164 0.1948 0.2233
REMARK 3 4 3.3000 - 3.0000 1.00 11903 174 0.2073 0.2676
REMARK 3 5 3.0000 - 2.7800 1.00 11948 168 0.2271 0.2735
REMARK 3 6 2.7800 - 2.6200 0.99 11806 170 0.2437 0.2765
REMARK 3 7 2.6200 - 2.4900 0.98 11740 160 0.2466 0.2937
REMARK 3 8 2.4900 - 2.3800 0.96 11488 154 0.2556 0.3020
REMARK 3 9 2.3800 - 2.2900 0.93 11074 164 0.2662 0.3094
REMARK 3 10 2.2900 - 2.2100 0.86 10274 132 0.2719 0.3444
REMARK 3 11 2.2100 - 2.1400 0.77 9130 134 0.2802 0.3527
REMARK 3 12 2.1400 - 2.0800 0.62 7427 92 0.2973 0.3108
REMARK 3 13 2.0800 - 2.0200 0.48 5722 87 0.3053 0.3574
REMARK 3 14 2.0200 - 1.9700 0.32 3779 54 0.3168 0.3658
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.70
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 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 : 0.030 17871
REMARK 3 ANGLE : 3.515 24195
REMARK 3 CHIRALITY : 0.189 2526
REMARK 3 PLANARITY : 0.027 3129
REMARK 3 DIHEDRAL : 12.215 2406
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 22 THROUGH 801)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0554 4.7200 6.7734
REMARK 3 T TENSOR
REMARK 3 T11: 0.1599 T22: 0.1995
REMARK 3 T33: 0.2052 T12: -0.0134
REMARK 3 T13: 0.0360 T23: -0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 1.1313 L22: 1.1869
REMARK 3 L33: 0.5372 L12: 0.1899
REMARK 3 L13: 0.0058 L23: -0.1880
REMARK 3 S TENSOR
REMARK 3 S11: 0.0904 S12: -0.1157 S13: 0.0971
REMARK 3 S21: 0.1459 S22: -0.0756 S23: 0.3934
REMARK 3 S31: -0.0237 S32: -0.1194 S33: 0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 22 THROUGH 801)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.0751 4.5849 -50.1064
REMARK 3 T TENSOR
REMARK 3 T11: 0.2251 T22: 0.2373
REMARK 3 T33: 0.2636 T12: 0.0304
REMARK 3 T13: 0.0479 T23: -0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 1.2328 L22: 1.4888
REMARK 3 L33: 0.7537 L12: -0.3242
REMARK 3 L13: 0.0344 L23: 0.1871
REMARK 3 S TENSOR
REMARK 3 S11: 0.0863 S12: 0.0577 S13: 0.2332
REMARK 3 S21: -0.1960 S22: 0.0489 S23: -0.4987
REMARK 3 S31: 0.0168 S32: 0.2398 S33: -0.0908
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 22 THROUGH 801)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6693 4.6928 -39.0230
REMARK 3 T TENSOR
REMARK 3 T11: 0.2274 T22: 0.3229
REMARK 3 T33: 0.3902 T12: -0.0109
REMARK 3 T13: 0.0609 T23: 0.1270
REMARK 3 L TENSOR
REMARK 3 L11: 1.2571 L22: 1.9205
REMARK 3 L33: 0.7402 L12: -0.5224
REMARK 3 L13: -0.0132 L23: -0.1829
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: -0.2422 S13: -0.2515
REMARK 3 S21: 0.2122 S22: 0.1799 S23: 0.7238
REMARK 3 S31: 0.0570 S32: -0.1660 S33: -0.0992
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 7Y4G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-22.
REMARK 100 THE DEPOSITION ID IS D_1300030240.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 143666
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 69.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1R9N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH6.0, 14% PEG 4,000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 82.64900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.49550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 82.64900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 55.49550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 5310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 165.29800
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 5280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 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 O HOH A 913 O HOH A 946 1.80
REMARK 500 O HOH B 1201 O HOH B 1207 1.83
REMARK 500 O HOH B 1103 O HOH B 1195 1.83
REMARK 500 O THR B 108 O HOH B 901 1.84
REMARK 500 O HOH A 1201 O HOH A 1315 1.84
REMARK 500 OH TYR B 588 O HOH B 902 1.90
REMARK 500 OG1 THR B 117 O HOH B 903 1.90
REMARK 500 OD2 ASP A 317 O HOH A 901 1.94
REMARK 500 O HOH A 1241 O HOH A 1336 1.95
REMARK 500 NZ LYS A 247 O HOH A 902 1.95
REMARK 500 O HOH B 1200 O HOH C 1191 1.95
REMARK 500 O HOH B 1017 O HOH B 1223 1.96
REMARK 500 O HOH C 1139 O HOH C 1160 1.96
REMARK 500 O HOH A 1215 O HOH A 1337 1.99
REMARK 500 O GLN A 494 O HOH A 903 1.99
REMARK 500 O HOH C 1200 O HOH C 1218 1.99
REMARK 500 OD2 ASP B 164 O HOH B 904 2.00
REMARK 500 OE2 GLU C 652 O HOH C 901 2.00
REMARK 500 O HOH A 1269 O HOH A 1349 2.02
REMARK 500 O GLN A 439 O HOH A 904 2.03
REMARK 500 O HOH C 905 O HOH C 954 2.04
REMARK 500 O ILE C 295 O HOH C 902 2.05
REMARK 500 OE1 GLU A 567 O HOH A 905 2.06
REMARK 500 N LEU A 25 O HOH A 906 2.06
REMARK 500 O HOH C 908 O HOH C 1189 2.06
REMARK 500 O HOH A 1301 O HOH A 1308 2.06
REMARK 500 OD2 ASP A 394 O HOH A 907 2.06
REMARK 500 NE2 GLN A 428 O HOH A 908 2.07
REMARK 500 O PRO B 285 O HOH B 905 2.07
REMARK 500 O GLY C 290 O HOH C 903 2.07
REMARK 500 N ALA A 82 O HOH A 909 2.07
REMARK 500 O HOH B 1193 O HOH B 1241 2.08
REMARK 500 OE2 GLU C 567 O HOH C 904 2.08
REMARK 500 OE2 GLU A 430 O HOH A 910 2.08
REMARK 500 OD1 ASP B 704 OD1 ASP C 704 2.09
REMARK 500 O HOH C 1034 O HOH C 1209 2.09
REMARK 500 NE2 GLN C 187 O HOH C 905 2.09
REMARK 500 O HOH C 1141 O HOH C 1180 2.10
REMARK 500 O HOH A 1239 O HOH A 1312 2.11
REMARK 500 OH TYR B 272 O HOH B 906 2.11
REMARK 500 O GLN A 81 O THR A 134 2.11
REMARK 500 OE1 GLU C 567 O HOH C 906 2.12
REMARK 500 NH1 ARG B 140 O HOH B 907 2.12
REMARK 500 O HOH C 1177 O HOH C 1186 2.12
REMARK 500 O HOH A 948 O HOH A 1117 2.13
REMARK 500 O PRO B 47 OE1 GLN B 439 2.13
REMARK 500 O HOH A 1249 O HOH A 1328 2.13
REMARK 500 OG1 THR C 326 O HOH C 907 2.13
REMARK 500 O GLY A 590 O HOH A 911 2.13
REMARK 500 OD1 ASN B 347 O HOH B 908 2.14
REMARK 500
REMARK 500 THIS ENTRY HAS 72 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 1106 O HOH C 1106 2554 1.63
REMARK 500 NZ LYS A 515 OD1 ASP C 129 3555 1.77
REMARK 500 NH1 ARG C 83 NH1 ARG C 83 2555 1.90
REMARK 500 O HOH B 958 O HOH C 1207 3545 1.98
REMARK 500 OD1 ASP A 704 OD1 ASP A 704 2655 1.99
REMARK 500 OE2 GLU B 353 CG PRO C 593 3545 2.07
REMARK 500 NZ LYS B 465 NZ LYS B 465 2654 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL A 79 CB VAL A 79 CG2 -0.133
REMARK 500 PHE A 161 CE1 PHE A 161 CZ 0.138
REMARK 500 GLU A 227 CG GLU A 227 CD 0.101
REMARK 500 GLU A 227 CD GLU A 227 OE1 0.084
REMARK 500 TYR A 249 CE1 TYR A 249 CZ 0.091
REMARK 500 TYR A 249 CE2 TYR A 249 CD2 0.119
REMARK 500 LYS A 266 CD LYS A 266 CE 0.196
REMARK 500 TYR A 401 CE2 TYR A 401 CD2 0.095
REMARK 500 TYR A 642 CG TYR A 642 CD2 0.091
REMARK 500 GLU A 652 CD GLU A 652 OE1 0.070
REMARK 500 ASP A 667 CB ASP A 667 CG 0.146
REMARK 500 TYR A 716 CD1 TYR A 716 CE1 0.095
REMARK 500 ILE B 44 CB ILE B 44 CG2 0.366
REMARK 500 GLU B 210 CD GLU B 210 OE1 0.067
REMARK 500 ASP B 214 CB ASP B 214 CG -0.140
REMARK 500 VAL B 269 CB VAL B 269 CG1 0.132
REMARK 500 GLU B 342 CG GLU B 342 CD 0.090
REMARK 500 LYS B 465 CB LYS B 465 CG -0.280
REMARK 500 LYS B 477 CG LYS B 477 CD -0.269
REMARK 500 LYS B 477 CD LYS B 477 CE 0.168
REMARK 500 LYS C 23 CB LYS C 23 CG -0.356
REMARK 500 LYS C 23 CG LYS C 23 CD -0.254
REMARK 500 GLU C 50 CB GLU C 50 CG -0.116
REMARK 500 GLU C 183 CD GLU C 183 OE2 0.101
REMARK 500 GLN C 187 CB GLN C 187 CG -0.314
REMARK 500 GLN C 187 CD GLN C 187 NE2 0.163
REMARK 500 ARG C 315 CZ ARG C 315 NH1 0.083
REMARK 500 PHE C 491 CE1 PHE C 491 CZ 0.117
REMARK 500 TYR C 607 CB TYR C 607 CG 0.097
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 MET A 46 CA - CB - CG ANGL. DEV. = -13.3 DEGREES
REMARK 500 LYS A 64 CB - CA - C ANGL. DEV. = -23.6 DEGREES
REMARK 500 LYS A 64 N - CA - CB ANGL. DEV. = 25.2 DEGREES
REMARK 500 LYS A 64 CG - CD - CE ANGL. DEV. = -42.8 DEGREES
REMARK 500 LYS A 64 CD - CE - NZ ANGL. DEV. = 36.9 DEGREES
REMARK 500 GLU A 252 OE1 - CD - OE2 ANGL. DEV. = -43.1 DEGREES
REMARK 500 GLU A 252 CG - CD - OE1 ANGL. DEV. = 44.5 DEGREES
REMARK 500 GLU A 252 CG - CD - OE2 ANGL. DEV. = -35.5 DEGREES
REMARK 500 ASP A 362 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 MET A 372 CB - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 MET A 372 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASN A 375 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 ASN A 375 N - CA - CB ANGL. DEV. = -22.4 DEGREES
REMARK 500 ASN A 375 CB - CG - OD1 ANGL. DEV. = 13.5 DEGREES
REMARK 500 ASN A 375 CB - CG - ND2 ANGL. DEV. = -24.9 DEGREES
REMARK 500 GLN A 428 C - N - CA ANGL. DEV. = 19.3 DEGREES
REMARK 500 GLN A 428 CB - CA - C ANGL. DEV. = 16.1 DEGREES
REMARK 500 GLN A 428 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 GLN A 428 CA - CB - CG ANGL. DEV. = -32.7 DEGREES
REMARK 500 GLN A 428 CG - CD - OE1 ANGL. DEV. = 32.4 DEGREES
REMARK 500 GLN A 428 CG - CD - NE2 ANGL. DEV. = -35.3 DEGREES
REMARK 500 LYS A 447 CA - CB - CG ANGL. DEV. = 21.9 DEGREES
REMARK 500 LYS A 447 CB - CG - CD ANGL. DEV. = -22.6 DEGREES
REMARK 500 SER A 449 N - CA - CB ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU A 456 CD1 - CG - CD2 ANGL. DEV. = -28.6 DEGREES
REMARK 500 LEU A 456 CB - CG - CD2 ANGL. DEV. = -26.6 DEGREES
REMARK 500 GLU A 489 OE1 - CD - OE2 ANGL. DEV. = -36.8 DEGREES
REMARK 500 GLU A 489 CG - CD - OE1 ANGL. DEV. = 43.3 DEGREES
REMARK 500 GLU A 489 CG - CD - OE2 ANGL. DEV. = -35.1 DEGREES
REMARK 500 ASP A 555 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 667 CB - CG - OD1 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ILE B 44 C - N - CA ANGL. DEV. = -17.4 DEGREES
REMARK 500 ILE B 44 CB - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 ILE B 44 CA - CB - CG1 ANGL. DEV. = -14.3 DEGREES
REMARK 500 ILE B 44 CB - CG1 - CD1 ANGL. DEV. = 26.6 DEGREES
REMARK 500 ILE B 44 CA - CB - CG2 ANGL. DEV. = -15.9 DEGREES
REMARK 500 ILE B 44 N - CA - C ANGL. DEV. = -27.5 DEGREES
REMARK 500 MET B 55 CA - CB - CG ANGL. DEV. = 10.9 DEGREES
REMARK 500 LYS B 126 CB - CG - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 GLU B 210 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP B 214 CB - CG - OD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP B 273 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ILE B 274 CG1 - CB - CG2 ANGL. DEV. = -18.7 DEGREES
REMARK 500 MET B 445 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 LYS B 465 CG - CD - CE ANGL. DEV. = 20.7 DEGREES
REMARK 500 LYS B 465 CD - CE - NZ ANGL. DEV. = 28.3 DEGREES
REMARK 500 GLN B 475 C - N - CA ANGL. DEV. = -17.7 DEGREES
REMARK 500 GLN B 475 CB - CA - C ANGL. DEV. = -26.0 DEGREES
REMARK 500 GLN B 475 N - CA - CB ANGL. DEV. = 34.5 DEGREES
REMARK 500 GLN B 475 CA - CB - CG ANGL. DEV. = 39.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 79 ANGLE DEVIATIONS.
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 ILE A 111 -73.16 -114.62
REMARK 500 TYR A 112 -149.65 -112.49
REMARK 500 LEU A 125 55.42 -96.39
REMARK 500 SER A 189 -58.37 -136.35
REMARK 500 THR A 326 -1.20 72.89
REMARK 500 TYR A 338 -85.91 -116.95
REMARK 500 SER A 525 -2.09 78.48
REMARK 500 CYS A 569 -8.82 -59.85
REMARK 500 LEU A 572 -5.58 73.40
REMARK 500 LYS A 573 65.53 -154.14
REMARK 500 SER A 606 -122.75 68.60
REMARK 500 ARG A 648 -158.77 56.84
REMARK 500 ASN A 653 49.49 -140.96
REMARK 500 ALA A 680 30.42 -99.34
REMARK 500 ASN A 683 -68.90 -105.93
REMARK 500 ILE A 715 77.75 36.36
REMARK 500 ILE B 111 -74.33 -114.40
REMARK 500 TYR B 112 -150.48 -111.73
REMARK 500 LEU B 125 51.80 -97.41
REMARK 500 SER B 189 -62.19 -139.38
REMARK 500 TYR B 338 -88.33 -110.54
REMARK 500 SER B 525 -4.39 77.16
REMARK 500 LEU B 572 -0.65 76.64
REMARK 500 LYS B 573 59.51 -157.10
REMARK 500 SER B 606 -122.28 67.31
REMARK 500 ARG B 648 -161.82 64.83
REMARK 500 ASN B 683 -67.87 -105.94
REMARK 500 ASN B 712 -155.74 -102.87
REMARK 500 ILE B 715 74.52 36.70
REMARK 500 VAL C 73 -61.91 -93.60
REMARK 500 ILE C 111 -73.53 -114.79
REMARK 500 TYR C 112 -146.73 -115.61
REMARK 500 VAL C 149 49.79 37.71
REMARK 500 TYR C 174 54.68 -93.33
REMARK 500 GLU C 183 10.38 -143.14
REMARK 500 SER C 189 -60.44 -138.08
REMARK 500 TYR C 338 -87.65 -112.08
REMARK 500 LEU C 357 116.40 -160.22
REMARK 500 LYS C 384 59.83 -97.92
REMARK 500 SER C 525 -3.77 76.09
REMARK 500 CYS C 569 -7.57 -59.34
REMARK 500 LEU C 572 -4.57 75.77
REMARK 500 LYS C 573 63.63 -156.23
REMARK 500 SER C 606 -123.15 67.55
REMARK 500 ARG C 648 -160.14 50.40
REMARK 500 ASN C 683 -69.23 -106.35
REMARK 500 GLN C 687 -39.76 -38.69
REMARK 500 ASN C 712 -159.49 -101.23
REMARK 500 ILE C 715 79.38 31.08
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 ASN A 375 0.13 SIDE CHAIN
REMARK 500 GLN A 428 0.10 SIDE CHAIN
REMARK 500 GLU A 489 0.08 SIDE CHAIN
REMARK 500 ARG B 36 0.25 SIDE CHAIN
REMARK 500 ARG B 361 0.10 SIDE CHAIN
REMARK 500 ARG B 411 0.21 SIDE CHAIN
REMARK 500 GLU B 489 0.08 SIDE CHAIN
REMARK 500 GLN C 187 0.10 SIDE CHAIN
REMARK 500 ARG C 315 0.32 SIDE CHAIN
REMARK 500 ARG C 361 0.17 SIDE CHAIN
REMARK 500 ASN C 375 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7Y4F RELATED DB: PDB
REMARK 900 RELATED ID: 8HAY RELATED DB: PDB
DBREF 7Y4G A 22 736 PDB 7Y4G 7Y4G 22 736
DBREF 7Y4G B 22 736 PDB 7Y4G 7Y4G 22 736
DBREF 7Y4G C 22 736 PDB 7Y4G 7Y4G 22 736
SEQRES 1 A 715 GLN LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG
SEQRES 2 A 715 PHE ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO
SEQRES 3 A 715 ASP GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR
SEQRES 4 A 715 GLN ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL
SEQRES 5 A 715 GLU VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP
SEQRES 6 A 715 PHE LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY
SEQRES 7 A 715 ASP LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR
SEQRES 8 A 715 ARG HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU
SEQRES 9 A 715 LYS ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE
SEQRES 10 A 715 GLU ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL
SEQRES 11 A 715 PHE SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP
SEQRES 12 A 715 ASN ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER
SEQRES 13 A 715 GLU SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL
SEQRES 14 A 715 LEU ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE
SEQRES 15 A 715 GLY PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR
SEQRES 16 A 715 MET ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO
SEQRES 17 A 715 SER TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN
SEQRES 18 A 715 ILE THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR
SEQRES 19 A 715 LYS TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU
SEQRES 20 A 715 VAL ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR
SEQRES 21 A 715 MET LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG
SEQRES 22 A 715 ILE ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET
SEQRES 23 A 715 THR LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE
SEQRES 24 A 715 ALA ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG
SEQRES 25 A 715 ASP GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP
SEQRES 26 A 715 ASN ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER
SEQRES 27 A 715 GLU ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET
SEQRES 28 A 715 GLY GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR
SEQRES 29 A 715 GLU VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY
SEQRES 30 A 715 SER PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG
SEQRES 31 A 715 LYS ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU
SEQRES 32 A 715 LYS LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE
SEQRES 33 A 715 SER GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN
SEQRES 34 A 715 LEU ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR
SEQRES 35 A 715 GLY LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU
SEQRES 36 A 715 LYS GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU
SEQRES 37 A 715 PHE PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN
SEQRES 38 A 715 GLY TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS
SEQRES 39 A 715 LYS TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY
SEQRES 40 A 715 SER GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU
SEQRES 41 A 715 THR TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL
SEQRES 42 A 715 ASP GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU
SEQRES 43 A 715 LYS CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS
SEQRES 44 A 715 ASP GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO
SEQRES 45 A 715 TYR VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER
SEQRES 46 A 715 TYR GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY
SEQRES 47 A 715 THR PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO
SEQRES 48 A 715 THR ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG
SEQRES 49 A 715 PHE MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS
SEQRES 50 A 715 GLU SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY
SEQRES 51 A 715 ASN LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL
SEQRES 52 A 715 HIS PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL
SEQRES 53 A 715 GLN LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN
SEQRES 54 A 715 ARG ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS
SEQRES 55 A 715 LEU TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 B 715 GLN LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG
SEQRES 2 B 715 PHE ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO
SEQRES 3 B 715 ASP GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR
SEQRES 4 B 715 GLN ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL
SEQRES 5 B 715 GLU VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP
SEQRES 6 B 715 PHE LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY
SEQRES 7 B 715 ASP LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR
SEQRES 8 B 715 ARG HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU
SEQRES 9 B 715 LYS ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE
SEQRES 10 B 715 GLU ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL
SEQRES 11 B 715 PHE SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP
SEQRES 12 B 715 ASN ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER
SEQRES 13 B 715 GLU SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL
SEQRES 14 B 715 LEU ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE
SEQRES 15 B 715 GLY PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR
SEQRES 16 B 715 MET ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO
SEQRES 17 B 715 SER TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN
SEQRES 18 B 715 ILE THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR
SEQRES 19 B 715 LYS TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU
SEQRES 20 B 715 VAL ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR
SEQRES 21 B 715 MET LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG
SEQRES 22 B 715 ILE ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET
SEQRES 23 B 715 THR LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE
SEQRES 24 B 715 ALA ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG
SEQRES 25 B 715 ASP GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP
SEQRES 26 B 715 ASN ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER
SEQRES 27 B 715 GLU ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET
SEQRES 28 B 715 GLY GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR
SEQRES 29 B 715 GLU VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY
SEQRES 30 B 715 SER PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG
SEQRES 31 B 715 LYS ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU
SEQRES 32 B 715 LYS LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE
SEQRES 33 B 715 SER GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN
SEQRES 34 B 715 LEU ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR
SEQRES 35 B 715 GLY LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU
SEQRES 36 B 715 LYS GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU
SEQRES 37 B 715 PHE PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN
SEQRES 38 B 715 GLY TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS
SEQRES 39 B 715 LYS TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY
SEQRES 40 B 715 SER GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU
SEQRES 41 B 715 THR TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL
SEQRES 42 B 715 ASP GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU
SEQRES 43 B 715 LYS CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS
SEQRES 44 B 715 ASP GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO
SEQRES 45 B 715 TYR VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER
SEQRES 46 B 715 TYR GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY
SEQRES 47 B 715 THR PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO
SEQRES 48 B 715 THR ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG
SEQRES 49 B 715 PHE MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS
SEQRES 50 B 715 GLU SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY
SEQRES 51 B 715 ASN LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL
SEQRES 52 B 715 HIS PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL
SEQRES 53 B 715 GLN LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN
SEQRES 54 B 715 ARG ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS
SEQRES 55 B 715 LEU TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 C 715 GLN LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG
SEQRES 2 C 715 PHE ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO
SEQRES 3 C 715 ASP GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR
SEQRES 4 C 715 GLN ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL
SEQRES 5 C 715 GLU VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP
SEQRES 6 C 715 PHE LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY
SEQRES 7 C 715 ASP LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR
SEQRES 8 C 715 ARG HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU
SEQRES 9 C 715 LYS ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE
SEQRES 10 C 715 GLU ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL
SEQRES 11 C 715 PHE SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP
SEQRES 12 C 715 ASN ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER
SEQRES 13 C 715 GLU SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL
SEQRES 14 C 715 LEU ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE
SEQRES 15 C 715 GLY PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR
SEQRES 16 C 715 MET ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO
SEQRES 17 C 715 SER TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN
SEQRES 18 C 715 ILE THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR
SEQRES 19 C 715 LYS TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU
SEQRES 20 C 715 VAL ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR
SEQRES 21 C 715 MET LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG
SEQRES 22 C 715 ILE ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET
SEQRES 23 C 715 THR LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE
SEQRES 24 C 715 ALA ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG
SEQRES 25 C 715 ASP GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP
SEQRES 26 C 715 ASN ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER
SEQRES 27 C 715 GLU ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET
SEQRES 28 C 715 GLY GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR
SEQRES 29 C 715 GLU VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY
SEQRES 30 C 715 SER PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG
SEQRES 31 C 715 LYS ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU
SEQRES 32 C 715 LYS LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE
SEQRES 33 C 715 SER GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN
SEQRES 34 C 715 LEU ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR
SEQRES 35 C 715 GLY LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU
SEQRES 36 C 715 LYS GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU
SEQRES 37 C 715 PHE PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN
SEQRES 38 C 715 GLY TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS
SEQRES 39 C 715 LYS TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY
SEQRES 40 C 715 SER GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU
SEQRES 41 C 715 THR TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL
SEQRES 42 C 715 ASP GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU
SEQRES 43 C 715 LYS CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS
SEQRES 44 C 715 ASP GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO
SEQRES 45 C 715 TYR VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER
SEQRES 46 C 715 TYR GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY
SEQRES 47 C 715 THR PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO
SEQRES 48 C 715 THR ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG
SEQRES 49 C 715 PHE MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS
SEQRES 50 C 715 GLU SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY
SEQRES 51 C 715 ASN LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL
SEQRES 52 C 715 HIS PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL
SEQRES 53 C 715 GLN LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN
SEQRES 54 C 715 ARG ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS
SEQRES 55 C 715 LEU TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
HET 715 A 801 28
HET 715 B 801 28
HET 715 C 801 28
HETNAM 715 (2R)-4-OXO-4-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,
HETNAM 2 715 4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-1-(2,4,5-
HETNAM 3 715 TRIFLUOROPHENYL)BUTAN-2-A MINE
HETSYN 715 SITAGLIPTIN
FORMUL 4 715 3(C16 H15 F6 N5 O)
FORMUL 7 HOH *1201(H2 O)
HELIX 1 AA1 ASP A 26 SER A 32 1 7
HELIX 2 AA2 ASN A 80 ALA A 82 5 3
HELIX 3 AA3 ASP A 196 PHE A 203 1 8
HELIX 4 AA4 ILE A 243 LYS A 247 5 5
HELIX 5 AA5 LYS A 341 ILE A 348 5 8
HELIX 6 AA6 ASN A 473 GLY A 482 1 10
HELIX 7 AA7 SER A 539 LEU A 547 1 9
HELIX 8 AA8 GLY A 563 CYS A 569 1 7
HELIX 9 AA9 GLY A 575 LYS A 591 1 17
HELIX 10 AB1 SER A 606 SER A 617 1 12
HELIX 11 AB2 ASP A 634 TYR A 638 5 5
HELIX 12 AB3 ASP A 639 ARG A 648 1 10
HELIX 13 AB4 ASN A 653 SER A 661 1 9
HELIX 14 AB5 ARG A 665 LEU A 669 5 5
HELIX 15 AB6 PHE A 686 LEU A 699 1 14
HELIX 16 AB7 ASN A 719 LEU A 736 1 18
HELIX 17 AB8 ASP B 26 SER B 32 1 7
HELIX 18 AB9 ASN B 80 ALA B 82 5 3
HELIX 19 AC1 ASP B 196 PHE B 203 1 8
HELIX 20 AC2 ILE B 243 LYS B 247 5 5
HELIX 21 AC3 LYS B 341 ILE B 348 5 8
HELIX 22 AC4 ASN B 473 GLY B 482 1 10
HELIX 23 AC5 SER B 539 LEU B 547 1 9
HELIX 24 AC6 GLY B 563 CYS B 569 1 7
HELIX 25 AC7 GLY B 575 LYS B 591 1 17
HELIX 26 AC8 SER B 606 SER B 617 1 12
HELIX 27 AC9 ASP B 634 TYR B 638 5 5
HELIX 28 AD1 ASP B 639 ARG B 648 1 10
HELIX 29 AD2 ASN B 653 SER B 661 1 9
HELIX 30 AD3 SER B 661 ALA B 666 1 6
HELIX 31 AD4 ASP B 667 LEU B 669 5 3
HELIX 32 AD5 HIS B 685 LEU B 699 1 15
HELIX 33 AD6 ASN B 719 LEU B 736 1 18
HELIX 34 AD7 ASP C 26 SER C 32 1 7
HELIX 35 AD8 VAL C 132 ASN C 136 5 5
HELIX 36 AD9 ASP C 196 GLY C 204 1 9
HELIX 37 AE1 ILE C 243 LYS C 247 5 5
HELIX 38 AE2 LYS C 341 ILE C 348 5 8
HELIX 39 AE3 ASN C 473 GLY C 482 1 10
HELIX 40 AE4 SER C 539 LEU C 547 1 9
HELIX 41 AE5 GLY C 563 CYS C 569 1 7
HELIX 42 AE6 GLY C 575 LYS C 591 1 17
HELIX 43 AE7 SER C 606 SER C 617 1 12
HELIX 44 AE8 ASP C 634 TYR C 638 5 5
HELIX 45 AE9 ASP C 639 ARG C 648 1 10
HELIX 46 AF1 ASN C 653 SER C 661 1 9
HELIX 47 AF2 ARG C 665 LEU C 669 5 5
HELIX 48 AF3 PHE C 686 GLY C 700 1 15
HELIX 49 AF4 ASN C 719 LEU C 736 1 18
SHEET 1 AA1 4 ILE A 44 PRO A 45 0
SHEET 2 AA1 4 HIS A 51 MET A 55 -1 O THR A 53 N ILE A 44
SHEET 3 AA1 4 GLN A 61 SER A 66 -1 O TYR A 65 N TYR A 52
SHEET 4 AA1 4 LYS A 72 ASP A 78 -1 O GLU A 74 N LYS A 64
SHEET 1 AA2 4 SER A 92 PHE A 95 0
SHEET 2 AA2 4 LYS A 101 PRO A 110 -1 O LEU A 103 N GLN A 94
SHEET 3 AA2 4 TYR A 116 PRO A 124 -1 O THR A 117 N THR A 109
SHEET 4 AA2 4 GLU A 139 ARG A 140 -1 O GLU A 139 N ILE A 122
SHEET 1 AA3 4 GLN A 148 PHE A 152 0
SHEET 2 AA3 4 MET A 158 ARG A 163 -1 O VAL A 162 N GLN A 148
SHEET 3 AA3 4 ASN A 166 LYS A 171 -1 O VAL A 170 N ILE A 159
SHEET 4 AA3 4 SER A 177 GLN A 180 -1 O SER A 179 N LEU A 169
SHEET 1 AA4 3 VAL A 190 ASN A 192 0
SHEET 2 AA4 3 MET A 217 ASP A 224 -1 O PHE A 223 N LEU A 191
SHEET 3 AA4 3 LEU A 209 PHE A 211 -1 N GLU A 210 O ALA A 219
SHEET 1 AA5 4 VAL A 190 ASN A 192 0
SHEET 2 AA5 4 MET A 217 ASP A 224 -1 O PHE A 223 N LEU A 191
SHEET 3 AA5 4 LYS A 266 ASP A 273 -1 O LYS A 266 N ASP A 224
SHEET 4 AA5 4 THR A 279 THR A 281 -1 O ARG A 280 N THR A 271
SHEET 1 AA6 2 SER A 230 MET A 235 0
SHEET 2 AA6 2 GLY A 251 LYS A 256 -1 O GLY A 251 N MET A 235
SHEET 1 AA7 4 TYR A 291 PHE A 297 0
SHEET 2 AA7 4 LEU A 304 LEU A 309 -1 O ALA A 305 N ARG A 296
SHEET 3 AA7 4 ARG A 315 ALA A 321 -1 O TYR A 319 N VAL A 306
SHEET 4 AA7 4 CYS A 328 GLU A 335 -1 O VAL A 331 N LEU A 318
SHEET 1 AA8 3 THR A 354 SER A 359 0
SHEET 2 AA8 3 HIS A 366 SER A 371 -1 O TYR A 368 N LEU A 357
SHEET 3 AA8 3 LEU A 376 LYS A 379 -1 O LYS A 378 N TRP A 369
SHEET 1 AA9 4 VAL A 387 ASP A 394 0
SHEET 2 AA9 4 SER A 399 SER A 404 -1 O TYR A 401 N GLY A 392
SHEET 3 AA9 4 ALA A 413 ILE A 417 -1 O TYR A 415 N TYR A 402
SHEET 4 AA9 4 LYS A 423 LYS A 425 -1 O LEU A 424 N LYS A 416
SHEET 1 AB1 4 THR A 432 PHE A 437 0
SHEET 2 AB1 4 TYR A 443 ASN A 450 -1 O SER A 449 N THR A 432
SHEET 3 AB1 4 THR A 453 ASP A 461 -1 O ASN A 460 N TYR A 444
SHEET 4 AB1 4 THR A 466 ILE A 471 -1 O LEU A 467 N LEU A 459
SHEET 1 AB2 8 LYS A 488 GLN A 494 0
SHEET 2 AB2 8 THR A 500 MET A 506 -1 O GLY A 503 N PHE A 491
SHEET 3 AB2 8 ILE A 550 ASP A 555 -1 O VAL A 551 N MET A 506
SHEET 4 AB2 8 TYR A 517 TYR A 522 1 N TYR A 522 O VAL A 552
SHEET 5 AB2 8 VAL A 595 TRP A 605 1 O GLY A 601 N VAL A 519
SHEET 6 AB2 8 ALA A 625 VAL A 629 1 O VAL A 629 N GLY A 604
SHEET 7 AB2 8 ASN A 672 GLY A 678 1 O VAL A 676 N ALA A 628
SHEET 8 AB2 8 ASP A 704 TYR A 708 1 O TYR A 708 N HIS A 677
SHEET 1 AB3 4 ILE B 44 PRO B 45 0
SHEET 2 AB3 4 HIS B 51 MET B 55 -1 O THR B 53 N ILE B 44
SHEET 3 AB3 4 GLN B 61 SER B 66 -1 O ILE B 63 N GLN B 54
SHEET 4 AB3 4 LYS B 72 ASP B 78 -1 O GLU B 74 N LYS B 64
SHEET 1 AB4 4 SER B 92 PHE B 95 0
SHEET 2 AB4 4 LYS B 101 PRO B 110 -1 O ALA B 105 N SER B 92
SHEET 3 AB4 4 TYR B 116 PRO B 124 -1 O THR B 117 N THR B 109
SHEET 4 AB4 4 GLU B 139 ARG B 140 -1 O GLU B 139 N ILE B 122
SHEET 1 AB5 4 GLN B 148 PHE B 152 0
SHEET 2 AB5 4 MET B 158 ARG B 163 -1 O VAL B 162 N GLN B 148
SHEET 3 AB5 4 ASN B 166 LYS B 171 -1 O PHE B 168 N PHE B 161
SHEET 4 AB5 4 SER B 177 GLN B 180 -1 O SER B 179 N LEU B 169
SHEET 1 AB6 3 VAL B 190 ASN B 192 0
SHEET 2 AB6 3 MET B 217 ASP B 224 -1 O PHE B 223 N LEU B 191
SHEET 3 AB6 3 LEU B 209 PHE B 211 -1 N GLU B 210 O ALA B 219
SHEET 1 AB7 4 VAL B 190 ASN B 192 0
SHEET 2 AB7 4 MET B 217 ASP B 224 -1 O PHE B 223 N LEU B 191
SHEET 3 AB7 4 LYS B 266 ASP B 273 -1 O GLU B 268 N ARG B 222
SHEET 4 AB7 4 THR B 279 THR B 281 -1 O ARG B 280 N THR B 271
SHEET 1 AB8 2 SER B 230 MET B 235 0
SHEET 2 AB8 2 GLY B 251 LYS B 256 -1 O TYR B 255 N TYR B 231
SHEET 1 AB9 4 TYR B 291 PHE B 297 0
SHEET 2 AB9 4 LEU B 304 LEU B 309 -1 O MET B 307 N ARG B 294
SHEET 3 AB9 4 ARG B 315 ASP B 322 -1 O TYR B 319 N VAL B 306
SHEET 4 AB9 4 LEU B 327 GLU B 335 -1 O VAL B 331 N LEU B 318
SHEET 1 AC1 3 THR B 354 SER B 359 0
SHEET 2 AC1 3 HIS B 366 SER B 371 -1 O TYR B 368 N LEU B 357
SHEET 3 AC1 3 LEU B 376 LYS B 379 -1 O LYS B 378 N TRP B 369
SHEET 1 AC2 4 VAL B 387 ASP B 394 0
SHEET 2 AC2 4 SER B 399 SER B 404 -1 O TYR B 401 N GLY B 392
SHEET 3 AC2 4 ALA B 413 ILE B 417 -1 O ILE B 417 N PHE B 400
SHEET 4 AC2 4 LYS B 423 LYS B 425 -1 O LEU B 424 N LYS B 416
SHEET 1 AC3 4 THR B 432 PHE B 437 0
SHEET 2 AC3 4 TYR B 443 ASN B 450 -1 O LYS B 447 N THR B 434
SHEET 3 AC3 4 THR B 453 ASP B 461 -1 O THR B 458 N ASN B 446
SHEET 4 AC3 4 THR B 466 ILE B 471 -1 O LEU B 467 N LEU B 459
SHEET 1 AC4 8 LYS B 488 GLN B 494 0
SHEET 2 AC4 8 THR B 500 MET B 506 -1 O MET B 505 N GLU B 489
SHEET 3 AC4 8 ILE B 550 ASP B 555 -1 O CYS B 553 N TRP B 504
SHEET 4 AC4 8 TYR B 517 TYR B 522 1 N TYR B 522 O VAL B 552
SHEET 5 AC4 8 VAL B 595 TRP B 605 1 O GLY B 601 N MET B 521
SHEET 6 AC4 8 ALA B 625 VAL B 629 1 O VAL B 629 N GLY B 604
SHEET 7 AC4 8 ASN B 672 GLY B 678 1 O VAL B 676 N ALA B 628
SHEET 8 AC4 8 ASP B 704 TYR B 708 1 O ASP B 704 N LEU B 675
SHEET 1 AC5 4 ILE C 44 PRO C 45 0
SHEET 2 AC5 4 HIS C 51 MET C 55 -1 O THR C 53 N ILE C 44
SHEET 3 AC5 4 GLN C 61 SER C 66 -1 O ILE C 63 N GLN C 54
SHEET 4 AC5 4 LYS C 72 ASP C 78 -1 O GLU C 74 N LYS C 64
SHEET 1 AC6 4 SER C 92 PHE C 95 0
SHEET 2 AC6 4 LYS C 101 PRO C 110 -1 O ALA C 105 N SER C 92
SHEET 3 AC6 4 TYR C 116 PRO C 124 -1 O THR C 117 N THR C 109
SHEET 4 AC6 4 GLU C 139 ARG C 140 -1 O GLU C 139 N ILE C 122
SHEET 1 AC7 4 GLN C 148 PHE C 152 0
SHEET 2 AC7 4 MET C 158 ARG C 163 -1 O VAL C 162 N GLN C 148
SHEET 3 AC7 4 ASN C 166 LYS C 171 -1 O VAL C 170 N ILE C 159
SHEET 4 AC7 4 SER C 177 GLN C 180 -1 O SER C 179 N LEU C 169
SHEET 1 AC8 3 VAL C 190 ASN C 192 0
SHEET 2 AC8 3 MET C 217 ASP C 224 -1 O PHE C 223 N LEU C 191
SHEET 3 AC8 3 LEU C 209 PHE C 211 -1 N GLU C 210 O ALA C 219
SHEET 1 AC9 4 VAL C 190 ASN C 192 0
SHEET 2 AC9 4 MET C 217 ASP C 224 -1 O PHE C 223 N LEU C 191
SHEET 3 AC9 4 LYS C 266 ASP C 273 -1 O LYS C 266 N ASP C 224
SHEET 4 AC9 4 THR C 279 THR C 281 -1 O ARG C 280 N THR C 271
SHEET 1 AD1 2 SER C 230 MET C 235 0
SHEET 2 AD1 2 GLY C 251 LYS C 256 -1 O TYR C 255 N TYR C 231
SHEET 1 AD2 4 TYR C 291 PHE C 297 0
SHEET 2 AD2 4 LEU C 304 LEU C 309 -1 O MET C 307 N ARG C 294
SHEET 3 AD2 4 ARG C 315 ALA C 321 -1 O TYR C 319 N VAL C 306
SHEET 4 AD2 4 CYS C 328 GLU C 335 -1 O VAL C 331 N LEU C 318
SHEET 1 AD3 3 THR C 354 SER C 359 0
SHEET 2 AD3 3 HIS C 366 SER C 371 -1 O HIS C 366 N SER C 359
SHEET 3 AD3 3 LEU C 376 LYS C 379 -1 O LYS C 378 N TRP C 369
SHEET 1 AD4 4 VAL C 387 ASP C 394 0
SHEET 2 AD4 4 SER C 399 SER C 404 -1 O THR C 403 N ASP C 389
SHEET 3 AD4 4 ALA C 413 ILE C 417 -1 O TYR C 415 N TYR C 402
SHEET 4 AD4 4 LYS C 423 LYS C 425 -1 O LEU C 424 N LYS C 416
SHEET 1 AD5 4 THR C 432 PHE C 437 0
SHEET 2 AD5 4 TYR C 443 ASN C 450 -1 O LYS C 447 N THR C 434
SHEET 3 AD5 4 THR C 453 ASP C 461 -1 O ASN C 460 N TYR C 444
SHEET 4 AD5 4 THR C 466 ILE C 471 -1 O LEU C 467 N LEU C 459
SHEET 1 AD6 8 GLN C 487 GLN C 494 0
SHEET 2 AD6 8 THR C 500 LYS C 507 -1 O MET C 505 N GLU C 489
SHEET 3 AD6 8 ILE C 550 VAL C 554 -1 O VAL C 551 N MET C 506
SHEET 4 AD6 8 TYR C 517 TYR C 522 1 N TYR C 522 O VAL C 552
SHEET 5 AD6 8 VAL C 595 TRP C 605 1 O ASP C 596 N TYR C 517
SHEET 6 AD6 8 ALA C 625 VAL C 629 1 O VAL C 629 N GLY C 604
SHEET 7 AD6 8 ASN C 672 GLY C 678 1 O VAL C 676 N ALA C 628
SHEET 8 AD6 8 ASP C 704 TYR C 708 1 O ASP C 704 N LEU C 673
CISPEP 1 ALA A 240 PRO A 241 0 2.26
CISPEP 2 ALA B 240 PRO B 241 0 2.36
CISPEP 3 ALA C 240 PRO C 241 0 2.65
CRYST1 165.298 110.991 134.392 90.00 91.17 90.00 C 1 2 1 12
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 0.006050 0.000000 0.000124 0.00000
SCALE2 0.000000 0.009010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007442 0.00000
TER 5780 LEU A 736
TER 11560 LEU B 736
TER 17340 LEU C 736
MASTER 564 0 3 49 132 0 0 618622 3 84 165
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