HEADER IMMUNE SYSTEM/INHIBITOR 11-JAN-16 5HI5
TITLE BINDING SITE ELUCIDATION AND STRUCTURE GUIDED DESIGN OF MACROCYCLIC
TITLE 2 IL-17A ANTAGONISTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-17A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 24-155;
COMPND 5 SYNONYM: IL-17A,CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8,CTLA-8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAT-2000 FAB HEAVY CHAIN;
COMPND 9 CHAIN: C, H;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: CAT-2000 LIGHT CHAIN;
COMPND 13 CHAIN: D, L;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: SYNTHETIC IL-17A INHIBITOR;
COMPND 17 CHAIN: I;
COMPND 18 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: IL17A, CTLA8, IL17;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPPARG4;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 22 MOL_ID: 4;
SOURCE 23 SYNTHETIC: YES;
SOURCE 24 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 25 ORGANISM_TAXID: 32630
KEYWDS IL-17A, PSORIASIS, MD SIMULATION, SULFONYL FLUORIDE, INHIBITOR,
KEYWDS 2 MACROCYCLE, IMMUNE SYSTEM-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LIU
REVDAT 3 06-MAR-24 5HI5 1 REMARK
REVDAT 2 22-NOV-17 5HI5 1 REMARK
REVDAT 1 31-AUG-16 5HI5 0
JRNL AUTH S.LIU,L.A.DAKIN,L.XING,J.M.WITHKA,P.V.SAHASRABUDHE,W.LI,
JRNL AUTH 2 M.E.BANKER,P.BALBO,S.SHANKER,B.A.CHRUNYK,Z.GUO,J.M.CHEN,
JRNL AUTH 3 J.A.YOUNG,G.BAI,J.T.STARR,S.W.WRIGHT,J.BUSSENIUS,S.TAN,
JRNL AUTH 4 A.GOPALSAMY,B.A.LEFKER,F.VINCENT,L.H.JONES,H.XU,L.R.HOTH,
JRNL AUTH 5 K.F.GEOGHEGAN,X.QIU,M.E.BUNNAGE,A.THORARENSEN
JRNL TITL BINDING SITE ELUCIDATION AND STRUCTURE GUIDED DESIGN OF
JRNL TITL 2 MACROCYCLIC IL-17A ANTAGONISTS.
JRNL REF SCI REP V. 6 30859 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27527709
JRNL DOI 10.1038/SREP30859
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 110571
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5555
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.85
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.63
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 7637
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2694
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7239
REMARK 3 BIN R VALUE (WORKING SET) : 0.2676
REMARK 3 BIN FREE R VALUE : 0.3028
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.21
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 398
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 : 8028
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 319
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.09230
REMARK 3 B22 (A**2) : -2.33260
REMARK 3 B33 (A**2) : 3.42480
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.90180
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.259
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.118
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.108
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.121
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.110
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8328 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11394 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2711 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 163 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1258 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8328 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1105 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8988 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.10
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 74.3911 -30.8624 -42.3863
REMARK 3 T TENSOR
REMARK 3 T11: 0.0594 T22: -0.0401
REMARK 3 T33: -0.0787 T12: 0.0053
REMARK 3 T13: 0.0803 T23: -0.0884
REMARK 3 L TENSOR
REMARK 3 L11: 0.6130 L22: 0.8434
REMARK 3 L33: 4.4690 L12: 0.3765
REMARK 3 L13: -0.3250 L23: -0.3272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: 0.0360 S13: -0.1959
REMARK 3 S21: 0.1366 S22: 0.0172 S23: -0.2139
REMARK 3 S31: 0.4074 S32: 0.5821 S33: -0.0328
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5804 -39.0838 -49.2691
REMARK 3 T TENSOR
REMARK 3 T11: 0.1188 T22: -0.1043
REMARK 3 T33: -0.1105 T12: -0.0187
REMARK 3 T13: 0.0948 T23: -0.1636
REMARK 3 L TENSOR
REMARK 3 L11: 1.3869 L22: 1.5031
REMARK 3 L33: 3.6372 L12: 0.3469
REMARK 3 L13: -0.3727 L23: 0.3156
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: 0.3946 S13: -0.4962
REMARK 3 S21: -0.2097 S22: 0.0719 S23: -0.2621
REMARK 3 S31: 0.9610 S32: 0.0629 S33: 0.0026
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 81.8338 -23.4446 -84.9169
REMARK 3 T TENSOR
REMARK 3 T11: -0.0549 T22: -0.0482
REMARK 3 T33: -0.0091 T12: -0.0297
REMARK 3 T13: 0.0095 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 0.8427 L22: 0.7297
REMARK 3 L33: 0.6967 L12: 0.2789
REMARK 3 L13: -0.5129 L23: -0.5150
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.1794 S13: 0.0696
REMARK 3 S21: 0.1331 S22: -0.0661 S23: -0.0131
REMARK 3 S31: -0.0585 S32: -0.0329 S33: 0.0582
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 75.7568 -7.1456 -87.9848
REMARK 3 T TENSOR
REMARK 3 T11: -0.0838 T22: -0.1916
REMARK 3 T33: -0.0154 T12: 0.0172
REMARK 3 T13: 0.0956 T23: -0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 0.9450 L22: 1.1705
REMARK 3 L33: 1.9188 L12: 0.9678
REMARK 3 L13: -0.6780 L23: -1.5922
REMARK 3 S TENSOR
REMARK 3 S11: 0.2834 S12: -0.1183 S13: 0.3135
REMARK 3 S21: 0.3340 S22: 0.0462 S23: 0.3672
REMARK 3 S31: -0.3584 S32: -0.1553 S33: -0.3296
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { H|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5398 -30.0499 -8.1449
REMARK 3 T TENSOR
REMARK 3 T11: -0.0981 T22: -0.0555
REMARK 3 T33: -0.0004 T12: -0.0146
REMARK 3 T13: -0.0110 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.9510 L22: 0.5683
REMARK 3 L33: 0.7979 L12: 0.0289
REMARK 3 L13: -0.8246 L23: -0.1865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: -0.0073 S13: -0.0858
REMARK 3 S21: -0.1578 S22: -0.0103 S23: 0.0709
REMARK 3 S31: 0.0403 S32: 0.0524 S33: 0.0461
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { I|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 76.8378 -60.7559 -40.1141
REMARK 3 T TENSOR
REMARK 3 T11: 0.1330 T22: -0.2317
REMARK 3 T33: 0.0359 T12: 0.1708
REMARK 3 T13: 0.0008 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: -0.0258 L22: 1.2275
REMARK 3 L33: 0.0349 L12: -1.4821
REMARK 3 L13: 1.1390 L23: 0.9790
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.1141 S13: -0.0817
REMARK 3 S21: -0.0265 S22: -0.0255 S23: -0.0362
REMARK 3 S31: 0.0354 S32: 0.0735 S33: 0.0274
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { L|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8842 -15.5391 -9.6956
REMARK 3 T TENSOR
REMARK 3 T11: -0.0740 T22: -0.0589
REMARK 3 T33: -0.0236 T12: 0.0104
REMARK 3 T13: 0.0082 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.5433 L22: 0.4127
REMARK 3 L33: 1.3204 L12: -0.0006
REMARK 3 L13: -0.5335 L23: -0.0892
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: 0.0602 S13: 0.0001
REMARK 3 S21: -0.0119 S22: 0.0209 S23: -0.0275
REMARK 3 S31: -0.1337 S32: -0.1069 S33: -0.0505
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5HI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217070.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113034
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 91.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.40800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% 2-PROPANOL, 20-24% PEG 6K, 0.1 M
REMARK 280 SODIUM ACETATE PH=4.0-5.0, PH 4.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 34.34000
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: HEPTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, I, L
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 GLY A 1
REMARK 465 ILE A 2
REMARK 465 THR A 3
REMARK 465 ILE A 4
REMARK 465 PRO A 5
REMARK 465 ARG A 6
REMARK 465 ASN A 7
REMARK 465 PRO A 8
REMARK 465 GLY A 9
REMARK 465 CYS A 10
REMARK 465 PRO A 11
REMARK 465 ASN A 12
REMARK 465 SER A 13
REMARK 465 GLU A 14
REMARK 465 ASP A 15
REMARK 465 LYS A 16
REMARK 465 ASN A 17
REMARK 465 PHE A 18
REMARK 465 PRO A 19
REMARK 465 ARG A 20
REMARK 465 THR A 21
REMARK 465 ARG A 31
REMARK 465 ASN A 32
REMARK 465 THR A 33
REMARK 465 ASN A 34
REMARK 465 THR A 35
REMARK 465 ARG A 101
REMARK 465 GLU A 102
REMARK 465 PRO A 103
REMARK 465 PRO A 104
REMARK 465 HIS A 105
REMARK 465 CYS A 106
REMARK 465 PRO A 107
REMARK 465 ASN A 108
REMARK 465 SER A 109
REMARK 465 HIS A 130
REMARK 465 VAL A 131
REMARK 465 ALA A 132
REMARK 465 GLY B 1
REMARK 465 ILE B 2
REMARK 465 THR B 3
REMARK 465 ILE B 4
REMARK 465 PRO B 5
REMARK 465 ARG B 6
REMARK 465 ASN B 7
REMARK 465 PRO B 8
REMARK 465 GLY B 9
REMARK 465 CYS B 10
REMARK 465 PRO B 11
REMARK 465 ASN B 12
REMARK 465 SER B 13
REMARK 465 GLU B 14
REMARK 465 ASP B 15
REMARK 465 LYS B 16
REMARK 465 ASN B 17
REMARK 465 PHE B 18
REMARK 465 PRO B 19
REMARK 465 ARG B 20
REMARK 465 THR B 21
REMARK 465 VAL B 22
REMARK 465 MET B 23
REMARK 465 VAL B 24
REMARK 465 ASN B 25
REMARK 465 LEU B 26
REMARK 465 ASN B 27
REMARK 465 ILE B 28
REMARK 465 HIS B 29
REMARK 465 ASN B 30
REMARK 465 ARG B 31
REMARK 465 ASN B 32
REMARK 465 THR B 33
REMARK 465 ASN B 34
REMARK 465 THR B 35
REMARK 465 ARG B 101
REMARK 465 GLU B 102
REMARK 465 PRO B 103
REMARK 465 PRO B 104
REMARK 465 HIS B 105
REMARK 465 CYS B 106
REMARK 465 PRO B 107
REMARK 465 HIS B 130
REMARK 465 VAL B 131
REMARK 465 ALA B 132
REMARK 465 GLY C -16
REMARK 465 SER C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 GLY C -8
REMARK 465 SER C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLN C -1
REMARK 465 GLY C 0
REMARK 465 GLU D 211
REMARK 465 GLY H -16
REMARK 465 SER H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 HIS H -10
REMARK 465 HIS H -9
REMARK 465 GLY H -8
REMARK 465 SER H -7
REMARK 465 GLU H -6
REMARK 465 ASN H -5
REMARK 465 LEU H -4
REMARK 465 TYR H -3
REMARK 465 PHE H -2
REMARK 465 GLN H -1
REMARK 465 GLY H 0
REMARK 465 ACE I 0
REMARK 465 LYS I 15
REMARK 465 GLU L 211
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 111 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 ARG B 111 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 113 CG CD OE1 OE2
REMARK 470 ASN D 1 CG OD1 ND2
REMARK 470 ASN L 1 CG OD1 ND2
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 MET A 23 97.46 -69.81
REMARK 500 ASN A 25 62.20 -108.80
REMARK 500 THR C 191 -50.76 -128.18
REMARK 500 ASN D 51 -48.40 72.36
REMARK 500 ASN D 52 11.10 -145.09
REMARK 500 ALA D 84 -179.60 176.52
REMARK 500 PRO D 142 -177.21 -68.97
REMARK 500 ASP D 152 -110.86 61.67
REMARK 500 ASN D 171 -8.67 77.05
REMARK 500 ASN L 51 -48.48 72.09
REMARK 500 ASN L 52 11.30 -145.58
REMARK 500 ALA L 84 -179.19 177.49
REMARK 500 ASP L 152 -109.86 60.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 63Q B 4000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HHV RELATED DB: PDB
REMARK 900 RELATED ID: 5HHX RELATED DB: PDB
REMARK 900 RELATED ID: 5HI3 RELATED DB: PDB
REMARK 900 RELATED ID: 5HI4 RELATED DB: PDB
DBREF 5HI5 A 1 132 UNP Q16552 IL17_HUMAN 24 155
DBREF 5HI5 B 1 132 UNP Q16552 IL17_HUMAN 24 155
DBREF 5HI5 C -16 215 PDB 5HI5 5HI5 -16 215
DBREF 5HI5 D 1 211 PDB 5HI5 5HI5 1 211
DBREF 5HI5 H -16 215 PDB 5HI5 5HI5 -16 215
DBREF 5HI5 I 0 15 PDB 5HI5 5HI5 0 15
DBREF 5HI5 L 1 211 PDB 5HI5 5HI5 1 211
SEQRES 1 A 132 GLY ILE THR ILE PRO ARG ASN PRO GLY CYS PRO ASN SER
SEQRES 2 A 132 GLU ASP LYS ASN PHE PRO ARG THR VAL MET VAL ASN LEU
SEQRES 3 A 132 ASN ILE HIS ASN ARG ASN THR ASN THR ASN PRO LYS ARG
SEQRES 4 A 132 SER SER ASP TYR TYR ASN ARG SER THR SER PRO TRP ASN
SEQRES 5 A 132 LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR PRO SER VAL
SEQRES 6 A 132 ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN
SEQRES 7 A 132 ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SER VAL PRO
SEQRES 8 A 132 ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO
SEQRES 9 A 132 HIS CYS PRO ASN SER PHE ARG LEU GLU LYS ILE LEU VAL
SEQRES 10 A 132 SER VAL GLY CYS THR CYS VAL THR PRO ILE VAL HIS HIS
SEQRES 11 A 132 VAL ALA
SEQRES 1 B 132 GLY ILE THR ILE PRO ARG ASN PRO GLY CYS PRO ASN SER
SEQRES 2 B 132 GLU ASP LYS ASN PHE PRO ARG THR VAL MET VAL ASN LEU
SEQRES 3 B 132 ASN ILE HIS ASN ARG ASN THR ASN THR ASN PRO LYS ARG
SEQRES 4 B 132 SER SER ASP TYR TYR ASN ARG SER THR SER PRO TRP ASN
SEQRES 5 B 132 LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR PRO SER VAL
SEQRES 6 B 132 ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN
SEQRES 7 B 132 ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SER VAL PRO
SEQRES 8 B 132 ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO
SEQRES 9 B 132 HIS CYS PRO ASN SER PHE ARG LEU GLU LYS ILE LEU VAL
SEQRES 10 B 132 SER VAL GLY CYS THR CYS VAL THR PRO ILE VAL HIS HIS
SEQRES 11 B 132 VAL ALA
SEQRES 1 C 237 GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU
SEQRES 2 C 237 TYR PHE GLN GLY GLU VAL GLN LEU LEU GLU SER GLY GLY
SEQRES 3 C 237 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS
SEQRES 4 C 237 ALA ALA SER GLY PHE THR PHE SER SER TYR ALA MET SER
SEQRES 5 C 237 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL
SEQRES 6 C 237 SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA
SEQRES 7 C 237 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN
SEQRES 8 C 237 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG
SEQRES 9 C 237 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ASP LEU
SEQRES 10 C 237 ILE HIS GLY VAL THR ARG ASN TRP GLY GLN GLY THR LEU
SEQRES 11 C 237 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL
SEQRES 12 C 237 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY
SEQRES 13 C 237 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO
SEQRES 14 C 237 GLN PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR
SEQRES 15 C 237 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER
SEQRES 16 C 237 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER
SEQRES 17 C 237 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN
SEQRES 18 C 237 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU
SEQRES 19 C 237 PRO LYS SER
SEQRES 1 D 214 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER
SEQRES 2 D 214 PRO GLY LYS THR VAL THR ILE SER CYS THR ARG SER SER
SEQRES 3 D 214 GLY SER LEU ALA ASN TYR TYR VAL GLN TRP TYR GLN GLN
SEQRES 4 D 214 ARG PRO GLY SER SER PRO THR ILE VAL ILE PHE ALA ASN
SEQRES 5 D 214 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY
SEQRES 6 D 214 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE
SEQRES 7 D 214 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS
SEQRES 8 D 214 GLN THR TYR ASP PRO TYR SER VAL VAL PHE GLY GLY GLY
SEQRES 9 D 214 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO
SEQRES 10 D 214 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 D 214 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 D 214 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 D 214 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 D 214 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 D 214 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 D 214 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 D 214 THR VAL ALA PRO THR GLU
SEQRES 1 H 237 GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU
SEQRES 2 H 237 TYR PHE GLN GLY GLU VAL GLN LEU LEU GLU SER GLY GLY
SEQRES 3 H 237 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS
SEQRES 4 H 237 ALA ALA SER GLY PHE THR PHE SER SER TYR ALA MET SER
SEQRES 5 H 237 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL
SEQRES 6 H 237 SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA
SEQRES 7 H 237 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN
SEQRES 8 H 237 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG
SEQRES 9 H 237 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ASP LEU
SEQRES 10 H 237 ILE HIS GLY VAL THR ARG ASN TRP GLY GLN GLY THR LEU
SEQRES 11 H 237 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL
SEQRES 12 H 237 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY
SEQRES 13 H 237 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO
SEQRES 14 H 237 GLN PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR
SEQRES 15 H 237 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER
SEQRES 16 H 237 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER
SEQRES 17 H 237 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN
SEQRES 18 H 237 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU
SEQRES 19 H 237 PRO LYS SER
SEQRES 1 I 16 ACE ILE HIS VAL THR ILE PRO ALA ASP LEU TRP ASP TRP
SEQRES 2 I 16 ILE ASN LYS
SEQRES 1 L 214 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER
SEQRES 2 L 214 PRO GLY LYS THR VAL THR ILE SER CYS THR ARG SER SER
SEQRES 3 L 214 GLY SER LEU ALA ASN TYR TYR VAL GLN TRP TYR GLN GLN
SEQRES 4 L 214 ARG PRO GLY SER SER PRO THR ILE VAL ILE PHE ALA ASN
SEQRES 5 L 214 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY
SEQRES 6 L 214 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE
SEQRES 7 L 214 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS
SEQRES 8 L 214 GLN THR TYR ASP PRO TYR SER VAL VAL PHE GLY GLY GLY
SEQRES 9 L 214 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO
SEQRES 10 L 214 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 L 214 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 L 214 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 L 214 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 L 214 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 L 214 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 L 214 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 L 214 THR VAL ALA PRO THR GLU
HET 63Q B4000 77
HETNAM 63Q (4S,20R)-7-CHLORO-N-METHYL-4-{[(1-METHYL-1H-PYRAZOL-5-
HETNAM 2 63Q YL)CARBONYL]AMINO}-3,18-DIOXO-2,19-
HETNAM 3 63Q DIAZATETRACYCLO[20.2.2.1~6,10~.1~11,15~]OCTACOSA-
HETNAM 4 63Q 1(24),6(28),7,9,11(27),12,14,22,25-NONAENE-20-
HETNAM 5 63Q CARBOXAMIDE
FORMUL 8 63Q C33 H33 CL N6 O4
FORMUL 9 HOH *319(H2 O)
HELIX 1 AA1 ASN A 36 SER A 40 5 5
HELIX 2 AA2 ASP A 42 SER A 47 1 6
HELIX 3 AA3 ASN B 36 SER B 40 5 5
HELIX 4 AA4 ASP B 42 SER B 47 1 6
HELIX 5 AA5 THR C 28 TYR C 32 5 5
HELIX 6 AA6 ASP C 61 LYS C 64 5 4
HELIX 7 AA7 ARG C 83 THR C 87 5 5
HELIX 8 AA8 SER C 156 ALA C 158 5 3
HELIX 9 AA9 SER C 187 LEU C 189 5 3
HELIX 10 AB1 LYS C 201 ASN C 204 5 4
HELIX 11 AB2 SER D 27B TYR D 31 5 5
HELIX 12 AB3 LYS D 79 GLU D 83 5 5
HELIX 13 AB4 SER D 122 ALA D 128 1 7
HELIX 14 AB5 THR D 182 HIS D 189 1 8
HELIX 15 AB6 THR H 28 TYR H 32 5 5
HELIX 16 AB7 ASP H 61 LYS H 64 5 4
HELIX 17 AB8 ARG H 83 THR H 87 5 5
HELIX 18 AB9 SER H 127 LYS H 129 5 3
HELIX 19 AC1 SER H 156 ALA H 158 5 3
HELIX 20 AC2 SER H 187 LEU H 189 5 3
HELIX 21 AC3 LYS H 201 ASN H 204 5 4
HELIX 22 AC4 ALA I 7 ASN I 14 1 8
HELIX 23 AC5 SER L 27B TYR L 31 5 5
HELIX 24 AC6 LYS L 79 GLU L 83 5 5
HELIX 25 AC7 SER L 122 ALA L 128 1 7
HELIX 26 AC8 THR L 182 HIS L 189 1 8
SHEET 1 AA1 4 ASN A 27 HIS A 29 0
SHEET 2 AA1 4 HIS I 2 PRO I 6 1 O ILE I 5 N ASN A 27
SHEET 3 AA1 4 SER B 109 VAL B 124 1 N PHE B 110 O THR I 4
SHEET 4 AA1 4 ASN B 88 ARG B 100 -1 N ILE B 96 O ILE B 115
SHEET 1 AA2 2 TRP A 51 GLU A 57 0
SHEET 2 AA2 2 VAL A 65 CYS A 71 -1 O GLU A 68 N HIS A 54
SHEET 1 AA3 2 CYS A 76 ILE A 77 0
SHEET 2 AA3 2 VAL A 83 ASP A 84 -1 O ASP A 84 N CYS A 76
SHEET 1 AA4 2 ASN A 88 LEU A 99 0
SHEET 2 AA4 2 LEU A 112 VAL A 124 -1 O GLY A 120 N ILE A 92
SHEET 1 AA5 2 TRP B 51 GLU B 57 0
SHEET 2 AA5 2 VAL B 65 CYS B 71 -1 O GLU B 68 N HIS B 54
SHEET 1 AA6 2 CYS B 76 ILE B 77 0
SHEET 2 AA6 2 VAL B 83 ASP B 84 -1 O ASP B 84 N CYS B 76
SHEET 1 AA7 4 GLN C 3 SER C 7 0
SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O ALA C 23 N LEU C 5
SHEET 3 AA7 4 THR C 77 MET C 82 -1 O LEU C 80 N LEU C 20
SHEET 4 AA7 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79
SHEET 1 AA8 6 GLY C 10 VAL C 12 0
SHEET 2 AA8 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12
SHEET 3 AA8 6 ALA C 88 ASP C 95 -1 N TYR C 90 O THR C 107
SHEET 4 AA8 6 ALA C 33 GLN C 39 -1 N VAL C 37 O TYR C 91
SHEET 5 AA8 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38
SHEET 6 AA8 6 THR C 57 TYR C 59 -1 O TYR C 58 N ALA C 50
SHEET 1 AA9 4 GLY C 10 VAL C 12 0
SHEET 2 AA9 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12
SHEET 3 AA9 4 ALA C 88 ASP C 95 -1 N TYR C 90 O THR C 107
SHEET 4 AA9 4 THR C 100A TRP C 103 -1 O ARG C 101 N ARG C 94
SHEET 1 AB1 4 SER C 120 LEU C 124 0
SHEET 2 AB1 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124
SHEET 3 AB1 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142
SHEET 4 AB1 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181
SHEET 1 AB2 4 THR C 131 SER C 132 0
SHEET 2 AB2 4 THR C 135 TYR C 145 -1 O THR C 135 N SER C 132
SHEET 3 AB2 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142
SHEET 4 AB2 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177
SHEET 1 AB3 3 THR C 151 TRP C 154 0
SHEET 2 AB3 3 TYR C 194 HIS C 200 -1 O ASN C 197 N SER C 153
SHEET 3 AB3 3 THR C 205 VAL C 211 -1 O VAL C 207 N VAL C 198
SHEET 1 AB4 4 LEU D 4 THR D 5 0
SHEET 2 AB4 4 VAL D 19 ARG D 25 -1 O THR D 24 N THR D 5
SHEET 3 AB4 4 SER D 70 ILE D 75 -1 O ILE D 75 N VAL D 19
SHEET 4 AB4 4 PHE D 62 ASP D 67 -1 N ASP D 67 O SER D 70
SHEET 1 AB5 5 SER D 9 GLU D 13 0
SHEET 2 AB5 5 THR D 102 VAL D 106 1 O THR D 105 N VAL D 11
SHEET 3 AB5 5 ALA D 84 TYR D 91 -1 N ALA D 84 O LEU D 104
SHEET 4 AB5 5 GLN D 34 GLN D 38 -1 N GLN D 34 O GLN D 89
SHEET 5 AB5 5 THR D 45 ILE D 48 -1 O ILE D 48 N TRP D 35
SHEET 1 AB6 4 SER D 9 GLU D 13 0
SHEET 2 AB6 4 THR D 102 VAL D 106 1 O THR D 105 N VAL D 11
SHEET 3 AB6 4 ALA D 84 TYR D 91 -1 N ALA D 84 O LEU D 104
SHEET 4 AB6 4 VAL D 96 PHE D 98 -1 O VAL D 97 N THR D 90
SHEET 1 AB7 4 SER D 115 PHE D 119 0
SHEET 2 AB7 4 ALA D 131 PHE D 140 -1 O LEU D 136 N THR D 117
SHEET 3 AB7 4 TYR D 173 LEU D 181 -1 O SER D 177 N CYS D 135
SHEET 4 AB7 4 VAL D 160 THR D 162 -1 N GLU D 161 O TYR D 178
SHEET 1 AB8 4 SER D 115 PHE D 119 0
SHEET 2 AB8 4 ALA D 131 PHE D 140 -1 O LEU D 136 N THR D 117
SHEET 3 AB8 4 TYR D 173 LEU D 181 -1 O SER D 177 N CYS D 135
SHEET 4 AB8 4 SER D 166 LYS D 167 -1 N SER D 166 O ALA D 174
SHEET 1 AB9 4 SER D 154 VAL D 156 0
SHEET 2 AB9 4 THR D 146 ALA D 151 -1 N ALA D 151 O SER D 154
SHEET 3 AB9 4 TYR D 192 HIS D 198 -1 O GLN D 195 N ALA D 148
SHEET 4 AB9 4 SER D 201 VAL D 207 -1 O VAL D 203 N VAL D 196
SHEET 1 AC1 4 GLN H 3 SER H 7 0
SHEET 2 AC1 4 LEU H 18 SER H 25 -1 O ALA H 23 N LEU H 5
SHEET 3 AC1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18
SHEET 4 AC1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 AC2 6 LEU H 11 VAL H 12 0
SHEET 2 AC2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 AC2 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AC2 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 AC2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AC2 6 THR H 57 TYR H 59 -1 O TYR H 58 N ALA H 50
SHEET 1 AC3 4 LEU H 11 VAL H 12 0
SHEET 2 AC3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 AC3 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AC3 4 THR H 100A TRP H 103 -1 O ARG H 101 N ARG H 94
SHEET 1 AC4 4 SER H 120 LEU H 124 0
SHEET 2 AC4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AC4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 AC4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AC5 4 THR H 131 SER H 132 0
SHEET 2 AC5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132
SHEET 3 AC5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 AC5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AC6 3 THR H 151 TRP H 154 0
SHEET 2 AC6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 AC6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198
SHEET 1 AC7 4 LEU L 4 THR L 5 0
SHEET 2 AC7 4 VAL L 19 ARG L 25 -1 O THR L 24 N THR L 5
SHEET 3 AC7 4 SER L 70 ILE L 75 -1 O ILE L 75 N VAL L 19
SHEET 4 AC7 4 PHE L 62 ASP L 67 -1 N ASP L 67 O SER L 70
SHEET 1 AC8 5 SER L 9 GLU L 13 0
SHEET 2 AC8 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AC8 5 ALA L 84 TYR L 91 -1 N ALA L 84 O LEU L 104
SHEET 4 AC8 5 GLN L 34 GLN L 38 -1 N GLN L 34 O GLN L 89
SHEET 5 AC8 5 THR L 45 ILE L 48 -1 O ILE L 48 N TRP L 35
SHEET 1 AC9 4 SER L 9 GLU L 13 0
SHEET 2 AC9 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AC9 4 ALA L 84 TYR L 91 -1 N ALA L 84 O LEU L 104
SHEET 4 AC9 4 VAL L 96 PHE L 98 -1 O VAL L 97 N THR L 90
SHEET 1 AD1 4 SER L 115 PHE L 119 0
SHEET 2 AD1 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AD1 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 140
SHEET 4 AD1 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178
SHEET 1 AD2 4 SER L 115 PHE L 119 0
SHEET 2 AD2 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AD2 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 140
SHEET 4 AD2 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174
SHEET 1 AD3 4 SER L 154 VAL L 156 0
SHEET 2 AD3 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154
SHEET 3 AD3 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148
SHEET 4 AD3 4 SER L 201 VAL L 207 -1 O VAL L 203 N VAL L 196
SSBOND 1 CYS A 71 CYS A 121 1555 1555 2.07
SSBOND 2 CYS A 76 CYS A 123 1555 1555 2.05
SSBOND 3 CYS B 71 CYS B 121 1555 1555 2.08
SSBOND 4 CYS B 76 CYS B 123 1555 1555 2.05
SSBOND 5 CYS C 22 CYS C 92 1555 1555 2.03
SSBOND 6 CYS C 140 CYS C 196 1555 1555 2.04
SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.05
SSBOND 8 CYS D 135 CYS D 194 1555 1555 2.05
SSBOND 9 CYS H 22 CYS H 92 1555 1555 2.05
SSBOND 10 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.06
SSBOND 12 CYS L 135 CYS L 194 1555 1555 2.04
CISPEP 1 TYR A 62 PRO A 63 0 1.55
CISPEP 2 TYR B 62 PRO B 63 0 1.94
CISPEP 3 PHE C 146 PRO C 147 0 -4.41
CISPEP 4 GLN C 148 PRO C 149 0 0.08
CISPEP 5 TYR D 141 PRO D 142 0 -2.38
CISPEP 6 PHE H 146 PRO H 147 0 -8.32
CISPEP 7 GLN H 148 PRO H 149 0 4.76
CISPEP 8 TYR L 141 PRO L 142 0 -2.77
SITE 1 AC1 13 PRO A 63 GLU A 95 ILE A 96 LEU A 97
SITE 2 AC1 13 TYR B 62 PRO B 63 VAL B 65 ILE B 66
SITE 3 AC1 13 TRP B 67 GLU B 95 ILE B 96 LEU B 97
SITE 4 AC1 13 LEU B 112
CRYST1 91.320 68.680 100.530 90.00 90.65 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 0.010951 0.000000 0.000124 0.00000
SCALE2 0.000000 0.014560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009948 0.00000
(ATOM LINES ARE NOT SHOWN.)
END