| content |
HEADER PEPTIDE BINDING PROTEIN 03-JAN-25 9LBT
TITLE DPPIV-VAMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: VAL-ALA-MET-PRO;
COMPND 8 CHAIN: C, D;
COMPND 9 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: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: CANNABIS SATIVA;
SOURCE 11 ORGANISM_TAXID: 3483
KEYWDS DPP-IV, VAMP, PEPTIDE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.H.CHEN,X.H.XING
REVDAT 1 23-JUL-25 9LBT 0
JRNL AUTH H.H.CHEN,X.H.XING
JRNL TITL DISCOVERY OF AN ORAL-ADMISTRATED BIOPEPTIDE VAMP: A NOVEL
JRNL TITL 2 GLUCOSE HOMEOSTASIS MODULATOR WITH BIFUNCTIONALITIES OF
JRNL TITL 3 TARGETING INTESTINAL DPP-IV AND MICROBIOTA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 138313
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.450
REMARK 3 FREE R VALUE TEST SET COUNT : 2003
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 3.8000 - 3.3200 1.00 9934 140 0.1560 0.1777
REMARK 3 2 3.3200 - 3.0200 1.00 9861 147 0.1639 0.2005
REMARK 3 3 3.0200 - 2.8000 1.00 9851 145 0.1717 0.1954
REMARK 3 4 2.8000 - 2.6400 0.99 9792 139 0.1697 0.2251
REMARK 3 5 2.6400 - 2.5100 0.99 9735 143 0.1698 0.2258
REMARK 3 6 2.5100 - 2.4000 0.99 9713 150 0.1644 0.1962
REMARK 3 7 2.4000 - 2.3100 0.99 9710 140 0.1665 0.2025
REMARK 3 8 2.3100 - 2.2300 0.99 9663 147 0.1764 0.2025
REMARK 3 9 2.2300 - 2.1600 0.98 9648 133 0.1789 0.2278
REMARK 3 10 2.1600 - 2.0900 0.98 9608 146 0.1885 0.2435
REMARK 3 11 2.0900 - 2.0400 0.98 9582 156 0.2127 0.2492
REMARK 3 12 2.0400 - 1.9900 0.91 8920 120 0.2530 0.3453
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.030
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) : 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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : 0.083 1756
REMARK 3 PLANARITY : 0.013 2110
REMARK 3 DIHEDRAL : 6.862 1618
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0528 -6.2919 -55.0338
REMARK 3 T TENSOR
REMARK 3 T11: 0.3441 T22: 0.2614
REMARK 3 T33: 0.2985 T12: -0.0153
REMARK 3 T13: -0.0051 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.6127 L22: 0.2841
REMARK 3 L33: 0.3936 L12: -0.2388
REMARK 3 L13: 0.0305 L23: 0.2390
REMARK 3 S TENSOR
REMARK 3 S11: 0.1636 S12: 0.1535 S13: -0.2890
REMARK 3 S21: -0.0462 S22: -0.0839 S23: 0.0845
REMARK 3 S31: 0.3106 S32: 0.0079 S33: -0.0293
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3526 -8.1162 -28.4658
REMARK 3 T TENSOR
REMARK 3 T11: 0.2331 T22: 0.1747
REMARK 3 T33: 0.2833 T12: -0.0059
REMARK 3 T13: -0.0413 T23: 0.0844
REMARK 3 L TENSOR
REMARK 3 L11: 1.1272 L22: 0.3026
REMARK 3 L33: 0.5154 L12: -0.0199
REMARK 3 L13: 0.0971 L23: 0.0327
REMARK 3 S TENSOR
REMARK 3 S11: 0.0873 S12: -0.2077 S13: -0.3582
REMARK 3 S21: 0.0448 S22: -0.0386 S23: -0.0741
REMARK 3 S31: 0.1487 S32: 0.0198 S33: -0.0095
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 387 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1993 13.4422 -28.6936
REMARK 3 T TENSOR
REMARK 3 T11: 0.1794 T22: 0.1912
REMARK 3 T33: 0.1806 T12: -0.0069
REMARK 3 T13: -0.0312 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.4764 L22: 0.5627
REMARK 3 L33: 0.6712 L12: 0.1910
REMARK 3 L13: 0.1510 L23: 0.1012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: -0.2627 S13: -0.0046
REMARK 3 S21: 0.1277 S22: -0.0435 S23: -0.0619
REMARK 3 S31: -0.0557 S32: 0.1242 S33: -0.0069
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 388 THROUGH 499 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0985 15.7446 -55.4596
REMARK 3 T TENSOR
REMARK 3 T11: 0.2088 T22: 0.1993
REMARK 3 T33: 0.1669 T12: -0.0348
REMARK 3 T13: 0.0040 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 1.4660 L22: 0.4443
REMARK 3 L33: 0.8581 L12: -0.2372
REMARK 3 L13: 0.2411 L23: -0.1282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0164 S12: 0.2307 S13: 0.1721
REMARK 3 S21: -0.0269 S22: -0.0383 S23: -0.0627
REMARK 3 S31: -0.1047 S32: 0.0982 S33: 0.0146
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 500 THROUGH 616 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7815 24.4714 -46.7476
REMARK 3 T TENSOR
REMARK 3 T11: 0.2044 T22: 0.1507
REMARK 3 T33: 0.2072 T12: 0.0139
REMARK 3 T13: -0.0023 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 0.9865 L22: 0.3910
REMARK 3 L33: 0.5635 L12: 0.0974
REMARK 3 L13: 0.0672 L23: 0.1000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0305 S12: 0.0944 S13: 0.2200
REMARK 3 S21: -0.0138 S22: 0.0306 S23: 0.0112
REMARK 3 S31: -0.1730 S32: -0.0426 S33: 0.0117
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 617 THROUGH 723 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7352 16.4834 -38.8160
REMARK 3 T TENSOR
REMARK 3 T11: 0.1422 T22: 0.1163
REMARK 3 T33: 0.1478 T12: 0.0180
REMARK 3 T13: 0.0103 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 1.1673 L22: 0.6824
REMARK 3 L33: 0.6912 L12: 0.1705
REMARK 3 L13: 0.0403 L23: 0.0548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: -0.0091 S13: 0.1255
REMARK 3 S21: 0.0131 S22: 0.0016 S23: 0.0712
REMARK 3 S31: -0.0825 S32: -0.0781 S33: 0.0053
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): -75.9412 22.9238 -24.3147
REMARK 3 T TENSOR
REMARK 3 T11: 0.3172 T22: 0.2425
REMARK 3 T33: 0.3603 T12: -0.0340
REMARK 3 T13: -0.0468 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.7972 L22: 0.4161
REMARK 3 L33: 0.4461 L12: -0.0322
REMARK 3 L13: -0.0860 L23: -0.1910
REMARK 3 S TENSOR
REMARK 3 S11: 0.2022 S12: -0.2786 S13: 0.3298
REMARK 3 S21: 0.2939 S22: -0.1200 S23: -0.2167
REMARK 3 S31: -0.3841 S32: 0.2154 S33: 0.0266
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.7160 1.0759 -13.3780
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.1689
REMARK 3 T33: 0.1610 T12: 0.0011
REMARK 3 T13: -0.0231 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.9539 L22: 0.3951
REMARK 3 L33: 0.9401 L12: 0.3496
REMARK 3 L13: -0.4626 L23: -0.3353
REMARK 3 S TENSOR
REMARK 3 S11: 0.0738 S12: -0.0834 S13: 0.0944
REMARK 3 S21: 0.1050 S22: -0.0423 S23: -0.0230
REMARK 3 S31: -0.1420 S32: -0.0608 S33: 0.0407
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 723 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.1664 0.7886 -40.6957
REMARK 3 T TENSOR
REMARK 3 T11: 0.1345 T22: 0.1720
REMARK 3 T33: 0.1341 T12: -0.0038
REMARK 3 T13: -0.0267 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 1.0145 L22: 0.3148
REMARK 3 L33: 0.2932 L12: 0.1173
REMARK 3 L13: -0.1973 L23: -0.0399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: 0.1877 S13: 0.0149
REMARK 3 S21: -0.0576 S22: 0.0139 S23: 0.0283
REMARK 3 S31: 0.0355 S32: -0.0776 S33: -0.0087
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 4 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8455 11.9388 -39.5546
REMARK 3 T TENSOR
REMARK 3 T11: 0.4421 T22: 0.9406
REMARK 3 T33: 0.5561 T12: -0.0119
REMARK 3 T13: 0.0878 T23: -0.0767
REMARK 3 L TENSOR
REMARK 3 L11: 0.1420 L22: 0.3136
REMARK 3 L33: 0.1363 L12: -0.0761
REMARK 3 L13: 0.1320 L23: -0.0094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0496 S12: 0.0126 S13: -0.1394
REMARK 3 S21: -0.0873 S22: 0.0546 S23: 0.0141
REMARK 3 S31: 0.0899 S32: 0.0035 S33: -0.0616
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 4 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4434 2.4361 -37.0719
REMARK 3 T TENSOR
REMARK 3 T11: 0.3086 T22: 0.3696
REMARK 3 T33: 0.5491 T12: 0.0398
REMARK 3 T13: 0.1036 T23: 0.0865
REMARK 3 L TENSOR
REMARK 3 L11: 1.1715 L22: 4.3888
REMARK 3 L33: 0.6255 L12: 1.2511
REMARK 3 L13: -0.6880 L23: 0.0877
REMARK 3 S TENSOR
REMARK 3 S11: 0.0717 S12: 0.1249 S13: 0.1001
REMARK 3 S21: -0.0926 S22: 0.0075 S23: 0.2216
REMARK 3 S31: -0.0694 S32: -0.1322 S33: -0.0614
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 9LBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 11-JAN-25.
REMARK 100 THE DEPOSITION ID IS D_1300055307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-24
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 : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138319
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 32.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 11.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M AMMONIUM ACETATE, 0.1 M TRIS PH
REMARK 280 8.5, 21% W/V POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 296K
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 58.91350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.43350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.43350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.91350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.18500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLN A 32A
REMARK 465 GLU A 32B
REMARK 465 ASN A 32C
REMARK 465 GLN B 32A
REMARK 465 GLU B 32B
REMARK 465 ASN B 32C
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 ASN A 33 N
REMARK 470 ASN B 33 N
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 1305 O HOH A 1437 2.05
REMARK 500 OE2 GLU B 104 O HOH B 801 2.14
REMARK 500 O SER B 233 N SER B 235 2.16
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 CG1 VAL B 237 O HOH A 840 2455 1.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO C 4 C - N - CA ANGL. DEV. = -13.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 25 -169.22 -165.22
REMARK 500 GLN A 81 -90.06 -105.56
REMARK 500 TRP A 82 -151.34 -99.77
REMARK 500 HIS A 120 32.63 -150.61
REMARK 500 GLU A 149 127.19 -39.84
REMARK 500 ILE A 151 -62.33 -125.79
REMARK 500 SER A 200 -164.71 66.88
REMARK 500 GLN A 278 31.89 -86.31
REMARK 500 ASN A 408 67.99 -163.94
REMARK 500 GLU A 479 16.69 57.77
REMARK 500 ARG A 555 42.96 -143.91
REMARK 500 THR A 558 -76.87 -119.71
REMARK 500 SER A 588 -116.87 67.44
REMARK 500 ALA A 612 55.86 39.14
REMARK 500 ASP A 636 -81.35 -113.41
REMARK 500 ASN A 637 22.59 -140.39
REMARK 500 ASN A 668 -67.48 -99.82
REMARK 500 ILE A 700 57.60 36.73
REMARK 500 SER B 64 116.14 -160.91
REMARK 500 GLN B 81 -90.16 -108.03
REMARK 500 TRP B 82 -150.67 -102.38
REMARK 500 HIS B 120 28.50 -148.56
REMARK 500 ILE B 151 -56.35 -128.02
REMARK 500 SER B 200 -166.19 67.62
REMARK 500 LEU B 234 55.93 -51.21
REMARK 500 SER B 235 19.39 -147.00
REMARK 500 VAL B 237 44.41 -1.08
REMARK 500 THR B 238 2.19 46.59
REMARK 500 GLN B 278 43.34 -85.85
REMARK 500 LYS B 381 19.71 55.51
REMARK 500 ASP B 396 96.86 -160.29
REMARK 500 ASN B 408 81.27 -153.76
REMARK 500 ASN B 445 24.17 -144.89
REMARK 500 TYR B 505 -65.08 -120.39
REMARK 500 ARG B 555 44.97 -142.13
REMARK 500 THR B 558 -81.52 -120.57
REMARK 500 SER B 588 -117.32 67.18
REMARK 500 ALA B 612 56.50 36.03
REMARK 500 ASP B 636 -85.13 -111.90
REMARK 500 ASN B 668 -66.56 -101.60
REMARK 500 ASP B 697 -161.37 -100.82
REMARK 500 ILE B 700 56.33 34.37
REMARK 500 ALA C 2 55.02 72.42
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 ARG A 294 0.13 SIDE CHAIN
REMARK 500 ARG A 340 0.10 SIDE CHAIN
REMARK 500 ARG B 340 0.09 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 A1564 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1565 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A1566 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A1567 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A1568 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A1569 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A1570 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A1571 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH A1572 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH A1573 DISTANCE = 9.06 ANGSTROMS
REMARK 525 HOH B1563 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1564 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B1565 DISTANCE = 8.70 ANGSTROMS
REMARK 525 HOH B1566 DISTANCE = 8.77 ANGSTROMS
DBREF 9LBT A 2 723 UNP P27487 DPP4_HUMAN 41 765
DBREF 9LBT B 2 723 UNP P27487 DPP4_HUMAN 41 765
DBREF 9LBT C 1 4 PDB 9LBT 9LBT 1 4
DBREF 9LBT D 1 4 PDB 9LBT 9LBT 1 4
SEQADV 9LBT ALA A 1 UNP P27487 EXPRESSION TAG
SEQADV 9LBT ALA B 1 UNP P27487 EXPRESSION TAG
SEQRES 1 A 726 ALA LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 A 726 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 A 726 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 A 726 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 A 726 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 A 726 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 A 726 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 A 726 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 A 726 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 A 726 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 A 726 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 A 726 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 A 726 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 A 726 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 A 726 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 A 726 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 A 726 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 A 726 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 A 726 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 A 726 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 A 726 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 A 726 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 A 726 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 A 726 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 A 726 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 A 726 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 A 726 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 A 726 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 A 726 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 A 726 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 A 726 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 A 726 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 A 726 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 A 726 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 A 726 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 A 726 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 A 726 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 A 726 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 A 726 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 A 726 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 A 726 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 A 726 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 A 726 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 A 726 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 A 726 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 A 726 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 A 726 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 A 726 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 A 726 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 A 726 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 A 726 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 A 726 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 A 726 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 A 726 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 A 726 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 A 726 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU
SEQRES 1 B 726 ALA LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 B 726 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 B 726 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 B 726 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 B 726 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 B 726 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 B 726 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 B 726 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 B 726 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 B 726 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 B 726 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 B 726 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 B 726 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 B 726 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 B 726 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 B 726 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 B 726 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 B 726 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 B 726 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 B 726 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 B 726 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 B 726 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 B 726 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 B 726 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 B 726 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 B 726 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 B 726 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 B 726 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 B 726 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 B 726 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 B 726 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 B 726 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 B 726 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 B 726 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 B 726 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 B 726 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 B 726 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 B 726 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 B 726 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 B 726 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 B 726 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 B 726 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 B 726 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 B 726 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 B 726 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 B 726 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 B 726 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 B 726 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 B 726 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 B 726 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 B 726 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 B 726 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 B 726 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 B 726 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 B 726 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 B 726 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU
SEQRES 1 C 4 VAL ALA MET PRO
SEQRES 1 D 4 VAL ALA MET PRO
FORMUL 5 HOH *1543(H2 O)
HELIX 1 AA1 THR A 5 ASN A 12 1 8
HELIX 2 AA2 ASP A 158 VAL A 165 1 8
HELIX 3 AA3 PRO A 248 ILE A 253 1 6
HELIX 4 AA4 VAL A 299 GLN A 302 5 4
HELIX 5 AA5 GLU A 379 MET A 383 5 5
HELIX 6 AA6 ASN A 455 ASN A 464 1 10
HELIX 7 AA7 ASN A 520 THR A 528 1 9
HELIX 8 AA8 GLY A 545 HIS A 550 1 6
HELIX 9 AA9 ALA A 551 ASN A 553 5 3
HELIX 10 AB1 THR A 558 SER A 572 1 15
HELIX 11 AB2 SER A 588 GLY A 599 1 12
HELIX 12 AB3 ARG A 616 TYR A 620 5 5
HELIX 13 AB4 ASP A 621 GLY A 630 1 10
HELIX 14 AB5 ASN A 637 SER A 644 1 8
HELIX 15 AB6 VAL A 646 VAL A 656 5 11
HELIX 16 AB7 HIS A 670 GLY A 685 1 16
HELIX 17 AB8 SER A 702 PHE A 721 1 20
HELIX 18 AB9 THR B 5 ASN B 12 1 8
HELIX 19 AC1 PHE B 53 GLY B 57 5 5
HELIX 20 AC2 ASP B 158 VAL B 165 1 8
HELIX 21 AC3 ASP B 232 LEU B 234 5 3
HELIX 22 AC4 PRO B 248 ILE B 253 1 6
HELIX 23 AC5 VAL B 299 GLN B 302 5 4
HELIX 24 AC6 GLU B 379 MET B 383 5 5
HELIX 25 AC7 ASN B 455 ASN B 464 1 10
HELIX 26 AC8 ASN B 520 THR B 528 1 9
HELIX 27 AC9 GLY B 545 HIS B 550 1 6
HELIX 28 AD1 ALA B 551 ASN B 553 5 3
HELIX 29 AD2 THR B 558 MET B 574 1 17
HELIX 30 AD3 SER B 588 GLY B 599 1 12
HELIX 31 AD4 ARG B 616 TYR B 620 5 5
HELIX 32 AD5 ASP B 621 GLY B 630 1 10
HELIX 33 AD6 ASN B 637 SER B 644 1 8
HELIX 34 AD7 VAL B 646 VAL B 656 5 11
HELIX 35 AD8 HIS B 670 VAL B 684 1 15
HELIX 36 AD9 SER B 702 PHE B 721 1 20
SHEET 1 AA1 2 LYS A 2 THR A 3 0
SHEET 2 AA1 2 VAL A 465 GLN A 466 1 O GLN A 466 N LYS A 2
SHEET 1 AA2 4 ARG A 22 TRP A 23 0
SHEET 2 AA2 4 GLU A 28 TYR A 31 -1 O LEU A 30 N ARG A 22
SHEET 3 AA2 4 ILE A 34 ASN A 38 -1 O LEU A 35 N TYR A 31
SHEET 4 AA2 4 SER A 44 LEU A 48 -1 O PHE A 47 N ILE A 34
SHEET 1 AA3 4 ILE A 60 ILE A 65 0
SHEET 2 AA3 4 PHE A 71 LYS A 80 -1 O LEU A 73 N SER A 64
SHEET 3 AA3 4 TYR A 86 ASP A 94 -1 O ASP A 91 N LEU A 74
SHEET 4 AA3 4 GLN A 99 LEU A 100 -1 O GLN A 99 N ASP A 94
SHEET 1 AA4 4 TRP A 112 TRP A 115 0
SHEET 2 AA4 4 LEU A 122 TRP A 126 -1 O VAL A 125 N TRP A 112
SHEET 3 AA4 4 ASP A 129 LYS A 133 -1 O TYR A 131 N TYR A 124
SHEET 4 AA4 4 TYR A 141 ARG A 142 -1 O TYR A 141 N VAL A 132
SHEET 1 AA5 3 ILE A 152 ASN A 154 0
SHEET 2 AA5 3 PHE A 180 ASN A 187 -1 O PHE A 186 N TYR A 153
SHEET 3 AA5 3 LEU A 172 TRP A 174 -1 N TRP A 173 O ALA A 182
SHEET 1 AA6 4 ILE A 152 ASN A 154 0
SHEET 2 AA6 4 PHE A 180 ASN A 187 -1 O PHE A 186 N TYR A 153
SHEET 3 AA6 4 THR A 223 ASN A 230 -1 O PHE A 227 N TYR A 183
SHEET 4 AA6 4 ILE A 243 ILE A 245 -1 O ILE A 243 N VAL A 228
SHEET 1 AA7 2 LEU A 193 PHE A 198 0
SHEET 2 AA7 2 LYS A 208 PRO A 213 -1 O VAL A 210 N TYR A 196
SHEET 1 AA8 4 HIS A 256 THR A 265 0
SHEET 2 AA8 4 ARG A 268 ARG A 275 -1 O ARG A 268 N ALA A 264
SHEET 3 AA8 4 TYR A 280 ASP A 289 -1 O CYS A 286 N ILE A 269
SHEET 4 AA8 4 ARG A 294 CYS A 297 -1 O ARG A 294 N ASP A 289
SHEET 1 AA9 4 HIS A 256 THR A 265 0
SHEET 2 AA9 4 ARG A 268 ARG A 275 -1 O ARG A 268 N ALA A 264
SHEET 3 AA9 4 TYR A 280 ASP A 289 -1 O CYS A 286 N ILE A 269
SHEET 4 AA9 4 HIS A 303 MET A 306 -1 O HIS A 303 N MET A 283
SHEET 1 AB1 4 HIS A 321 PHE A 322 0
SHEET 2 AB1 4 SER A 328 SER A 334 -1 O TYR A 330 N HIS A 321
SHEET 3 AB1 4 ARG A 340 GLN A 346 -1 O PHE A 345 N PHE A 329
SHEET 4 AB1 4 THR A 353 PHE A 354 -1 O THR A 353 N TYR A 344
SHEET 1 AB2 4 VAL A 362 LEU A 368 0
SHEET 2 AB2 4 TYR A 372 SER A 377 -1 O TYR A 374 N ALA A 367
SHEET 3 AB2 4 ASN A 388 GLN A 393 -1 O TYR A 390 N TYR A 375
SHEET 4 AB2 4 VAL A 400 CYS A 402 -1 O THR A 401 N LYS A 391
SHEET 1 AB3 4 CYS A 412 PHE A 419 0
SHEET 2 AB3 4 TYR A 425 PRO A 433 -1 O GLY A 432 N GLN A 413
SHEET 3 AB3 4 LEU A 437 SER A 442 -1 O HIS A 441 N TYR A 426
SHEET 4 AB3 4 LYS A 447 GLU A 453 -1 O GLU A 453 N TYR A 438
SHEET 1 AB4 8 SER A 469 LEU A 477 0
SHEET 2 AB4 8 THR A 480 LEU A 488 -1 O PHE A 482 N ILE A 475
SHEET 3 AB4 8 ILE A 532 PHE A 536 -1 O SER A 535 N GLN A 485
SHEET 4 AB4 8 TYR A 498 VAL A 504 1 N LEU A 501 O ILE A 532
SHEET 5 AB4 8 VAL A 577 TRP A 587 1 O ASP A 578 N TYR A 498
SHEET 6 AB4 8 CYS A 607 VAL A 611 1 O VAL A 611 N GLY A 586
SHEET 7 AB4 8 GLU A 657 GLY A 663 1 O ILE A 661 N ALA A 610
SHEET 8 AB4 8 GLN A 689 TYR A 693 1 O GLN A 689 N TYR A 658
SHEET 1 AB5 2 LYS B 2 THR B 3 0
SHEET 2 AB5 2 VAL B 465 GLN B 466 1 O GLN B 466 N LYS B 2
SHEET 1 AB6 4 ARG B 22 TRP B 23 0
SHEET 2 AB6 4 GLU B 28 TYR B 31 -1 O LEU B 30 N ARG B 22
SHEET 3 AB6 4 ILE B 34 ASN B 38 -1 O PHE B 37 N TYR B 29
SHEET 4 AB6 4 SER B 44 LEU B 48 -1 O LEU B 48 N ILE B 34
SHEET 1 AB7 4 ILE B 60 ILE B 65 0
SHEET 2 AB7 4 PHE B 71 LYS B 80 -1 O LEU B 73 N SER B 64
SHEET 3 AB7 4 TYR B 86 ASP B 94 -1 O SER B 89 N TYR B 76
SHEET 4 AB7 4 GLN B 99 LEU B 100 -1 O GLN B 99 N ASP B 94
SHEET 1 AB8 4 THR B 110 TRP B 115 0
SHEET 2 AB8 4 LEU B 122 TRP B 126 -1 O VAL B 125 N GLN B 111
SHEET 3 AB8 4 ASP B 129 LYS B 133 -1 O LYS B 133 N LEU B 122
SHEET 4 AB8 4 TYR B 141 ARG B 142 -1 O TYR B 141 N VAL B 132
SHEET 1 AB9 3 ILE B 152 ASN B 154 0
SHEET 2 AB9 3 PHE B 180 ASN B 187 -1 O PHE B 186 N TYR B 153
SHEET 3 AB9 3 LEU B 172 TRP B 174 -1 N TRP B 173 O ALA B 182
SHEET 1 AC1 4 ILE B 152 ASN B 154 0
SHEET 2 AC1 4 PHE B 180 ASN B 187 -1 O PHE B 186 N TYR B 153
SHEET 3 AC1 4 THR B 223 ASN B 230 -1 O PHE B 227 N TYR B 183
SHEET 4 AC1 4 SER B 242 GLN B 244 -1 O ILE B 243 N VAL B 228
SHEET 1 AC2 2 LEU B 193 PHE B 198 0
SHEET 2 AC2 2 LYS B 208 PRO B 213 -1 O LYS B 208 N PHE B 198
SHEET 1 AC3 4 HIS B 256 THR B 265 0
SHEET 2 AC3 4 ARG B 268 ARG B 275 -1 O ARG B 268 N ALA B 264
SHEET 3 AC3 4 TYR B 280 ASP B 289 -1 O CYS B 286 N ILE B 269
SHEET 4 AC3 4 ARG B 294 CYS B 297 -1 O ARG B 294 N ASP B 289
SHEET 1 AC4 4 HIS B 256 THR B 265 0
SHEET 2 AC4 4 ARG B 268 ARG B 275 -1 O ARG B 268 N ALA B 264
SHEET 3 AC4 4 TYR B 280 ASP B 289 -1 O CYS B 286 N ILE B 269
SHEET 4 AC4 4 HIS B 303 MET B 306 -1 O HIS B 303 N MET B 283
SHEET 1 AC5 4 HIS B 321 PHE B 322 0
SHEET 2 AC5 4 SER B 328 SER B 334 -1 O TYR B 330 N HIS B 321
SHEET 3 AC5 4 ARG B 340 GLN B 346 -1 O PHE B 345 N PHE B 329
SHEET 4 AC5 4 THR B 353 PHE B 354 -1 O THR B 353 N TYR B 344
SHEET 1 AC6 4 VAL B 362 LEU B 368 0
SHEET 2 AC6 4 TYR B 372 SER B 377 -1 O TYR B 374 N ALA B 367
SHEET 3 AC6 4 ASN B 388 GLN B 393 -1 O TYR B 390 N TYR B 375
SHEET 4 AC6 4 ASP B 396 CYS B 402 -1 O THR B 401 N LYS B 391
SHEET 1 AC7 4 TYR B 415 PHE B 419 0
SHEET 2 AC7 4 TYR B 425 CYS B 430 -1 O GLN B 427 N SER B 418
SHEET 3 AC7 4 LEU B 437 SER B 442 -1 O LEU B 437 N CYS B 430
SHEET 4 AC7 4 GLY B 448 GLU B 453 -1 O LEU B 449 N LEU B 440
SHEET 1 AC8 8 SER B 469 LEU B 477 0
SHEET 2 AC8 8 THR B 480 LEU B 488 -1 O THR B 480 N LEU B 477
SHEET 3 AC8 8 ILE B 532 PHE B 536 -1 O VAL B 533 N ILE B 487
SHEET 4 AC8 8 TYR B 498 VAL B 504 1 N ASP B 503 O ALA B 534
SHEET 5 AC8 8 VAL B 577 TRP B 587 1 O TRP B 585 N VAL B 504
SHEET 6 AC8 8 CYS B 607 VAL B 611 1 O VAL B 611 N GLY B 586
SHEET 7 AC8 8 GLU B 657 GLY B 663 1 O LEU B 659 N ALA B 610
SHEET 8 AC8 8 GLN B 689 TYR B 693 1 O GLN B 689 N TYR B 658
SSBOND 1 CYS A 286 CYS A 297 1555 1555 2.08
SSBOND 2 CYS A 343 CYS A 352 1555 1555 2.09
SSBOND 3 CYS A 402 CYS A 405 1555 1555 2.03
SSBOND 4 CYS A 412 CYS A 430 1555 1555 2.09
SSBOND 5 CYS A 607 CYS A 720 1555 1555 2.11
SSBOND 6 CYS B 286 CYS B 297 1555 1555 2.09
SSBOND 7 CYS B 343 CYS B 352 1555 1555 2.06
SSBOND 8 CYS B 402 CYS B 405 1555 1555 2.06
SSBOND 9 CYS B 412 CYS B 430 1555 1555 2.11
SSBOND 10 CYS B 607 CYS B 720 1555 1555 2.08
CISPEP 1 GLY A 432 PRO A 433 0 8.38
CISPEP 2 GLY B 432 PRO B 433 0 6.16
CRYST1 117.827 126.370 136.867 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 0.008487 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007913 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007306 0.00000
TER 5918 LEU A 723
TER 11836 LEU B 723
TER 11864 PRO C 4
TER 11892 PRO D 4
MASTER 544 0 0 36 102 0 0 613431 4 20 114
END |