HEADER IMMUNE SYSTEM/PROTEIN BINDING 29-OCT-12 4HSA
TITLE STRUCTURE OF INTERLEUKIN 17A IN COMPLEX WITH IL17RA RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-17A;
COMPND 3 CHAIN: A, B, D, E;
COMPND 4 SYNONYM: IL-17, IL-17A, CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8,
COMPND 5 CTLA-8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERLEUKIN-17 RECEPTOR A;
COMPND 10 CHAIN: C, F;
COMPND 11 SYNONYM: IL-17 RECEPTOR A, IL-17RA, CDW217;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: 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: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: IL17RA, IL17R;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS CYTOKINE RECEPTOR, GLYCOSYLATION, IMMUNE SYSTEM-PROTEIN BINDING
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LIU
REVDAT 4 29-JUL-20 4HSA 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 19-JUN-13 4HSA 1 JRNL
REVDAT 2 05-JUN-13 4HSA 1 JRNL
REVDAT 1 22-MAY-13 4HSA 0
JRNL AUTH S.LIU,X.SONG,B.A.CHRUNYK,S.SHANKER,L.R.HOTH,E.S.MARR,
JRNL AUTH 2 M.C.GRIFFOR
JRNL TITL CRYSTAL STRUCTURES OF INTERLEUKIN 17A AND ITS COMPLEX WITH
JRNL TITL 2 IL-17 RECEPTOR A.
JRNL REF NAT COMMUN V. 4 1888 2013
JRNL REFN ESSN 2041-1723
JRNL PMID 23695682
JRNL DOI 10.1038/NCOMMS2880
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
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) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 32406
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1774
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 : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2816
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2366
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2662
REMARK 3 BIN R VALUE (WORKING SET) : 0.2323
REMARK 3 BIN FREE R VALUE : 0.3115
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.47
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 154
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 : 7830
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 196
REMARK 3 SOLVENT ATOMS : 5
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 97.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 106.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.27640
REMARK 3 B22 (A**2) : -11.27640
REMARK 3 B33 (A**2) : 22.55270
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.674
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8289 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11345 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2842 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 201 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1186 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8289 ; 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 : 1125 ; 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 : 8885 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.31
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 24.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A 17 A 131
REMARK 3 ORIGIN FOR THE GROUP (A): -58.3734 42.9358 -33.2586
REMARK 3 T TENSOR
REMARK 3 T11: -0.3285 T22: -0.0678
REMARK 3 T33: -0.3920 T12: -0.1260
REMARK 3 T13: -0.0210 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.8096 L22: 2.6276
REMARK 3 L33: 4.0812 L12: 0.1365
REMARK 3 L13: -0.5991 L23: 1.1713
REMARK 3 S TENSOR
REMARK 3 S11: 0.2538 S12: -0.0419 S13: -0.3603
REMARK 3 S21: 0.3029 S22: -0.1844 S23: 0.2801
REMARK 3 S31: 0.5105 S32: -0.3158 S33: -0.0694
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: B 19 B 127
REMARK 3 ORIGIN FOR THE GROUP (A): -52.9465 52.3940 -35.6823
REMARK 3 T TENSOR
REMARK 3 T11: -0.4174 T22: -0.0732
REMARK 3 T33: -0.4290 T12: 0.0068
REMARK 3 T13: 0.0675 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.5627 L22: 3.4587
REMARK 3 L33: 5.1166 L12: 1.0102
REMARK 3 L13: 1.0226 L23: 2.0587
REMARK 3 S TENSOR
REMARK 3 S11: 0.3121 S12: 0.1821 S13: -0.0394
REMARK 3 S21: -0.1338 S22: -0.1596 S23: 0.1450
REMARK 3 S31: -0.1462 S32: -0.3417 S33: -0.1525
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: C 2 C 273
REMARK 3 ORIGIN FOR THE GROUP (A): -36.2146 42.0479 -34.7152
REMARK 3 T TENSOR
REMARK 3 T11: -0.5408 T22: -0.2621
REMARK 3 T33: -0.5712 T12: 0.1002
REMARK 3 T13: -0.1562 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 1.1056 L22: 3.1603
REMARK 3 L33: 2.6969 L12: 0.7928
REMARK 3 L13: 0.6193 L23: 1.5409
REMARK 3 S TENSOR
REMARK 3 S11: 0.3565 S12: 0.0243 S13: -0.4265
REMARK 3 S21: 0.4523 S22: 0.0003 S23: -0.4526
REMARK 3 S31: 0.5770 S32: 0.3635 S33: -0.3568
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: D 20 D 131
REMARK 3 ORIGIN FOR THE GROUP (A): -80.7792 58.7090 -64.8682
REMARK 3 T TENSOR
REMARK 3 T11: -0.3121 T22: 0.1584
REMARK 3 T33: 0.1288 T12: 0.0504
REMARK 3 T13: 0.0528 T23: 0.1652
REMARK 3 L TENSOR
REMARK 3 L11: 3.0365 L22: 3.2158
REMARK 3 L33: 7.4173 L12: 0.4268
REMARK 3 L13: -0.0829 L23: 0.2785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0946 S12: -0.3019 S13: 0.0430
REMARK 3 S21: 0.1284 S22: 0.1583 S23: 0.7358
REMARK 3 S31: 0.0695 S32: -1.1046 S33: -0.0637
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: E 19 E 127
REMARK 3 ORIGIN FOR THE GROUP (A): -70.4000 58.3355 -68.9809
REMARK 3 T TENSOR
REMARK 3 T11: -0.3554 T22: -0.1332
REMARK 3 T33: -0.0691 T12: 0.0102
REMARK 3 T13: -0.0124 T23: 0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 2.7884 L22: 2.3805
REMARK 3 L33: 7.3898 L12: -0.1431
REMARK 3 L13: -0.5004 L23: -0.5475
REMARK 3 S TENSOR
REMARK 3 S11: 0.1568 S12: -0.1552 S13: 0.1213
REMARK 3 S21: 0.0139 S22: 0.3376 S23: 0.2509
REMARK 3 S31: 0.1031 S32: -0.1988 S33: -0.4944
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: F 2 F 272
REMARK 3 ORIGIN FOR THE GROUP (A): -70.2374 78.0096 -68.0738
REMARK 3 T TENSOR
REMARK 3 T11: -0.4365 T22: -0.7139
REMARK 3 T33: -0.3677 T12: 0.1540
REMARK 3 T13: 0.1656 T23: 0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 2.5155 L22: 1.6543
REMARK 3 L33: 5.1270 L12: 0.1594
REMARK 3 L13: -1.4875 L23: -0.6678
REMARK 3 S TENSOR
REMARK 3 S11: 0.3642 S12: -0.1461 S13: 0.9642
REMARK 3 S21: 0.3903 S22: 0.2907 S23: 0.4405
REMARK 3 S31: -1.2441 S32: -0.3766 S33: -0.6549
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4HSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000075857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34990
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> 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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.69667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 119.39333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 119.39333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.69667
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H, I
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 30
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 ASN A 36
REMARK 465 PRO A 37
REMARK 465 LYS A 38
REMARK 465 ARG A 39
REMARK 465 SER A 40
REMARK 465 ALA A 132
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 VAL B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 VAL B 131
REMARK 465 ALA B 132
REMARK 465 SER C 1
REMARK 465 GLU C 274
REMARK 465 MET C 275
REMARK 465 PRO C 276
REMARK 465 ASP C 277
REMARK 465 THR C 278
REMARK 465 PRO C 279
REMARK 465 GLU C 280
REMARK 465 PRO C 281
REMARK 465 ILE C 282
REMARK 465 PRO C 283
REMARK 465 ASP C 284
REMARK 465 TYR C 285
REMARK 465 MET C 286
REMARK 465 LEU C 287
REMARK 465 VAL C 288
REMARK 465 PRO C 289
REMARK 465 ARG C 290
REMARK 465 GLY C 291
REMARK 465 SER C 292
REMARK 465 ASP C 293
REMARK 465 TYR C 294
REMARK 465 LYS C 295
REMARK 465 ASP C 296
REMARK 465 ASP C 297
REMARK 465 ASP C 298
REMARK 465 ASP C 299
REMARK 465 LYS C 300
REMARK 465 GLY C 301
REMARK 465 PRO D 11
REMARK 465 ASN D 12
REMARK 465 SER D 13
REMARK 465 GLU D 14
REMARK 465 ASP D 15
REMARK 465 LYS D 16
REMARK 465 ASN D 17
REMARK 465 PHE D 18
REMARK 465 PRO D 19
REMARK 465 ASN D 30
REMARK 465 ARG D 31
REMARK 465 ASN D 32
REMARK 465 THR D 33
REMARK 465 ASN D 34
REMARK 465 THR D 35
REMARK 465 ASN D 36
REMARK 465 PRO D 37
REMARK 465 LYS D 38
REMARK 465 ARG D 39
REMARK 465 SER D 40
REMARK 465 SER D 41
REMARK 465 ALA D 132
REMARK 465 PRO E 11
REMARK 465 ASN E 12
REMARK 465 SER E 13
REMARK 465 GLU E 14
REMARK 465 ASP E 15
REMARK 465 LYS E 16
REMARK 465 ASN E 17
REMARK 465 PHE E 18
REMARK 465 VAL E 128
REMARK 465 HIS E 129
REMARK 465 HIS E 130
REMARK 465 VAL E 131
REMARK 465 ALA E 132
REMARK 465 SER F 1
REMARK 465 PRO F 273
REMARK 465 GLU F 274
REMARK 465 MET F 275
REMARK 465 PRO F 276
REMARK 465 ASP F 277
REMARK 465 THR F 278
REMARK 465 PRO F 279
REMARK 465 GLU F 280
REMARK 465 PRO F 281
REMARK 465 ILE F 282
REMARK 465 PRO F 283
REMARK 465 ASP F 284
REMARK 465 TYR F 285
REMARK 465 MET F 286
REMARK 465 LEU F 287
REMARK 465 VAL F 288
REMARK 465 PRO F 289
REMARK 465 ARG F 290
REMARK 465 GLY F 291
REMARK 465 SER F 292
REMARK 465 ASP F 293
REMARK 465 TYR F 294
REMARK 465 LYS F 295
REMARK 465 ASP F 296
REMARK 465 ASP F 297
REMARK 465 ASP F 298
REMARK 465 ASP F 299
REMARK 465 LYS F 300
REMARK 465 GLY F 301
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 ASP C 29 CG OD1 OD2
REMARK 470 VAL C 178 CG1 CG2
REMARK 470 SER C 189 OG
REMARK 470 GLN C 231 CG CD OE1 NE2
REMARK 470 LYS C 243 CG CD CE NZ
REMARK 470 SER C 267 OG
REMARK 470 ASP F 29 CG OD1 OD2
REMARK 470 LEU F 101 CG CD1 CD2
REMARK 470 VAL F 178 CG1 CG2
REMARK 470 SER F 189 OG
REMARK 470 GLN F 231 CG CD OE1 NE2
REMARK 470 LYS F 243 CG CD CE NZ
REMARK 470 SER F 267 OG
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 E 103 CA - C - N ANGL. DEV. = 16.8 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 ASP A 42 -152.90 -171.14
REMARK 500 TYR A 43 -45.16 70.55
REMARK 500 SER A 49 73.60 -111.44
REMARK 500 HIS A 105 -6.00 77.22
REMARK 500 SER B 40 140.14 56.73
REMARK 500 SER B 49 69.31 -111.77
REMARK 500 PRO B 103 -102.63 7.10
REMARK 500 HIS B 105 147.42 141.39
REMARK 500 SER B 106 78.33 60.75
REMARK 500 ASN C 91 47.31 -95.48
REMARK 500 ALA C 183 86.29 51.25
REMARK 500 HIS C 184 46.20 36.62
REMARK 500 SER C 196 49.84 -86.04
REMARK 500 ASN C 211 40.45 -91.94
REMARK 500 HIS C 230 -3.27 64.98
REMARK 500 LEU C 242 103.21 -164.25
REMARK 500 LEU C 260 -115.24 57.03
REMARK 500 ASP C 262 34.03 -86.46
REMARK 500 SER C 271 -151.00 -86.20
REMARK 500 CYS C 272 -77.32 -133.59
REMARK 500 SER D 49 70.30 -115.01
REMARK 500 SER E 40 128.13 42.82
REMARK 500 PRO E 103 -99.48 10.43
REMARK 500 HIS E 105 129.16 160.40
REMARK 500 SER E 106 154.34 71.16
REMARK 500 ASN E 108 -157.89 -99.72
REMARK 500 ASN F 91 47.11 -95.88
REMARK 500 ALA F 183 86.09 51.67
REMARK 500 HIS F 184 46.14 36.43
REMARK 500 ASN F 211 36.13 -89.12
REMARK 500 HIS F 230 -3.16 65.50
REMARK 500 LEU F 260 -116.79 63.03
REMARK 500 ASP F 262 34.00 -84.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HR9 RELATED DB: PDB
REMARK 900 UNBOUND IL17A
DBREF 4HSA A 11 132 UNP Q16552 IL17_HUMAN 34 155
DBREF 4HSA B 11 132 UNP Q16552 IL17_HUMAN 34 155
DBREF 4HSA C 1 286 UNP Q96F46 I17RA_HUMAN 32 317
DBREF 4HSA D 11 132 UNP Q16552 IL17_HUMAN 34 155
DBREF 4HSA E 11 132 UNP Q16552 IL17_HUMAN 34 155
DBREF 4HSA F 1 286 UNP Q96F46 I17RA_HUMAN 32 317
SEQADV 4HSA ASP A 45 UNP Q16552 ASN 68 ENGINEERED MUTATION
SEQADV 4HSA SER A 106 UNP Q16552 CYS 129 ENGINEERED MUTATION
SEQADV 4HSA ASP B 45 UNP Q16552 ASN 68 ENGINEERED MUTATION
SEQADV 4HSA SER B 106 UNP Q16552 CYS 129 ENGINEERED MUTATION
SEQADV 4HSA ASP C 175 UNP Q96F46 ASN 206 ENGINEERED MUTATION
SEQADV 4HSA ASP C 234 UNP Q96F46 ASN 265 ENGINEERED MUTATION
SEQADV 4HSA LEU C 287 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA VAL C 288 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA PRO C 289 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ARG C 290 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA GLY C 291 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA SER C 292 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP C 293 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA TYR C 294 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA LYS C 295 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP C 296 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP C 297 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP C 298 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP C 299 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA LYS C 300 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA GLY C 301 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP D 45 UNP Q16552 ASN 68 ENGINEERED MUTATION
SEQADV 4HSA SER D 106 UNP Q16552 CYS 129 ENGINEERED MUTATION
SEQADV 4HSA ASP E 45 UNP Q16552 ASN 68 ENGINEERED MUTATION
SEQADV 4HSA SER E 106 UNP Q16552 CYS 129 ENGINEERED MUTATION
SEQADV 4HSA ASP F 175 UNP Q96F46 ASN 206 ENGINEERED MUTATION
SEQADV 4HSA ASP F 234 UNP Q96F46 ASN 265 ENGINEERED MUTATION
SEQADV 4HSA LEU F 287 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA VAL F 288 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA PRO F 289 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ARG F 290 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA GLY F 291 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA SER F 292 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP F 293 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA TYR F 294 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA LYS F 295 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP F 296 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP F 297 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP F 298 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA ASP F 299 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA LYS F 300 UNP Q96F46 EXPRESSION TAG
SEQADV 4HSA GLY F 301 UNP Q96F46 EXPRESSION TAG
SEQRES 1 A 122 PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET
SEQRES 2 A 122 VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN
SEQRES 3 A 122 PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER
SEQRES 4 A 122 PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR
SEQRES 5 A 122 PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY
SEQRES 6 A 122 CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN
SEQRES 7 A 122 SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG
SEQRES 8 A 122 GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS
SEQRES 9 A 122 ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE
SEQRES 10 A 122 VAL HIS HIS VAL ALA
SEQRES 1 B 122 PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET
SEQRES 2 B 122 VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN
SEQRES 3 B 122 PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER
SEQRES 4 B 122 PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR
SEQRES 5 B 122 PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY
SEQRES 6 B 122 CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN
SEQRES 7 B 122 SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG
SEQRES 8 B 122 GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS
SEQRES 9 B 122 ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE
SEQRES 10 B 122 VAL HIS HIS VAL ALA
SEQRES 1 C 301 SER LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER
SEQRES 2 C 301 GLN PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS
SEQRES 3 C 301 LEU ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO
SEQRES 4 C 301 SER SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA
SEQRES 5 C 301 HIS THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE
SEQRES 6 C 301 GLU TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU
SEQRES 7 C 301 GLU GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN
SEQRES 8 C 301 GLU ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU
SEQRES 9 C 301 ARG HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS
SEQRES 10 C 301 PHE VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL
SEQRES 11 C 301 HIS HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN
SEQRES 12 C 301 HIS GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS
SEQRES 13 C 301 ALA ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY
SEQRES 14 C 301 SER LEU TRP ASP PRO ASP ILE THR VAL GLU THR LEU GLU
SEQRES 15 C 301 ALA HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU
SEQRES 16 C 301 SER THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS
SEQRES 17 C 301 MET GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE
SEQRES 18 C 301 PRO ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASP
SEQRES 19 C 301 VAL THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG
SEQRES 20 C 301 HIS GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU
SEQRES 21 C 301 ASN ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO
SEQRES 22 C 301 GLU MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET
SEQRES 23 C 301 LEU VAL PRO ARG GLY SER ASP TYR LYS ASP ASP ASP ASP
SEQRES 24 C 301 LYS GLY
SEQRES 1 D 122 PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET
SEQRES 2 D 122 VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN
SEQRES 3 D 122 PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER
SEQRES 4 D 122 PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR
SEQRES 5 D 122 PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY
SEQRES 6 D 122 CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN
SEQRES 7 D 122 SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG
SEQRES 8 D 122 GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS
SEQRES 9 D 122 ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE
SEQRES 10 D 122 VAL HIS HIS VAL ALA
SEQRES 1 E 122 PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET
SEQRES 2 E 122 VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN
SEQRES 3 E 122 PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER
SEQRES 4 E 122 PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR
SEQRES 5 E 122 PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY
SEQRES 6 E 122 CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN
SEQRES 7 E 122 SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG
SEQRES 8 E 122 GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS
SEQRES 9 E 122 ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE
SEQRES 10 E 122 VAL HIS HIS VAL ALA
SEQRES 1 F 301 SER LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER
SEQRES 2 F 301 GLN PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS
SEQRES 3 F 301 LEU ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO
SEQRES 4 F 301 SER SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA
SEQRES 5 F 301 HIS THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE
SEQRES 6 F 301 GLU TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU
SEQRES 7 F 301 GLU GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN
SEQRES 8 F 301 GLU ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU
SEQRES 9 F 301 ARG HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS
SEQRES 10 F 301 PHE VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL
SEQRES 11 F 301 HIS HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN
SEQRES 12 F 301 HIS GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS
SEQRES 13 F 301 ALA ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY
SEQRES 14 F 301 SER LEU TRP ASP PRO ASP ILE THR VAL GLU THR LEU GLU
SEQRES 15 F 301 ALA HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU
SEQRES 16 F 301 SER THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS
SEQRES 17 F 301 MET GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE
SEQRES 18 F 301 PRO ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASP
SEQRES 19 F 301 VAL THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG
SEQRES 20 F 301 HIS GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU
SEQRES 21 F 301 ASN ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO
SEQRES 22 F 301 GLU MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET
SEQRES 23 F 301 LEU VAL PRO ARG GLY SER ASP TYR LYS ASP ASP ASP ASP
SEQRES 24 F 301 LYS GLY
MODRES 4HSA ASN F 23 ASN GLYCOSYLATION SITE
MODRES 4HSA ASN C 194 ASN GLYCOSYLATION SITE
MODRES 4HSA ASN F 194 ASN GLYCOSYLATION SITE
MODRES 4HSA ASN C 23 ASN GLYCOSYLATION SITE
MODRES 4HSA ASN C 18 ASN GLYCOSYLATION SITE
HET NAG G 1 14
HET NAG G 2 14
HET MAN G 3 11
HET MAN G 4 11
HET FUC G 5 10
HET NAG H 1 14
HET NAG H 2 14
HET FUC H 3 10
HET NAG I 1 14
HET FUC I 2 10
HET NAG J 1 14
HET NAG J 2 14
HET MAN J 3 11
HET MAN J 4 11
HET FUC J 5 10
HET NAG F 606 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
FORMUL 7 NAG 8(C8 H15 N O6)
FORMUL 7 MAN 4(C6 H12 O6)
FORMUL 7 FUC 4(C6 H12 O5)
FORMUL 12 HOH *5(H2 O)
HELIX 1 1 ASP C 28 HIS C 33 1 6
HELIX 2 2 ASP C 72 LEU C 78 5 7
HELIX 3 3 ARG C 158 VAL C 161 5 4
HELIX 4 4 THR C 162 SER C 168 1 7
HELIX 5 5 ARG C 225 PHE C 229 5 5
HELIX 6 6 CYS C 259 CYS C 263 5 5
HELIX 7 7 TYR D 43 SER D 47 1 5
HELIX 8 8 ASP F 28 HIS F 33 1 6
HELIX 9 9 ASP F 72 LEU F 78 5 7
HELIX 10 10 ARG F 158 VAL F 161 5 4
HELIX 11 11 THR F 162 SER F 167 1 6
HELIX 12 12 ARG F 225 PHE F 229 5 5
HELIX 13 13 CYS F 259 CYS F 263 5 5
SHEET 1 A 8 ARG A 61 TYR A 62 0
SHEET 2 A 8 ASN A 88 ARG A 101 -1 O LEU A 99 N TYR A 62
SHEET 3 A 8 SER A 109 VAL A 124 -1 O GLY A 120 N ILE A 92
SHEET 4 A 8 THR B 21 ASN B 30 1 O HIS B 29 N LEU A 112
SHEET 5 A 8 THR A 21 LEU A 26 -1 N VAL A 24 O VAL B 22
SHEET 6 A 8 PHE B 110 VAL B 124 1 O PHE B 110 N ASN A 25
SHEET 7 A 8 ASN B 88 ARG B 101 -1 N ILE B 96 O ILE B 115
SHEET 8 A 8 ARG B 61 TYR B 62 -1 N TYR B 62 O LEU B 99
SHEET 1 B 2 TRP A 51 GLU A 57 0
SHEET 2 B 2 VAL A 65 CYS A 71 -1 O GLU A 68 N HIS A 54
SHEET 1 C 2 CYS A 76 ILE A 77 0
SHEET 2 C 2 VAL A 83 ASP A 84 -1 O ASP A 84 N CYS A 76
SHEET 1 D 5 VAL A 128 HIS A 130 0
SHEET 2 D 5 ARG C 265 VAL C 270 1 O SER C 267 N HIS A 129
SHEET 3 D 5 CYS C 245 PRO C 254 -1 N VAL C 250 O ALA C 268
SHEET 4 D 5 TYR C 199 PRO C 207 -1 N LEU C 202 O GLN C 251
SHEET 5 D 5 PHE C 215 ILE C 221 -1 O PHE C 215 N SER C 205
SHEET 1 E 2 TRP B 51 GLU B 57 0
SHEET 2 E 2 VAL B 65 CYS B 71 -1 O GLU B 68 N HIS B 54
SHEET 1 F 2 CYS B 76 ILE B 77 0
SHEET 2 F 2 VAL B 83 ASP B 84 -1 O ASP B 84 N CYS B 76
SHEET 1 G 4 ARG C 3 LEU C 4 0
SHEET 2 G 4 ARG C 112 VAL C 119 -1 O VAL C 119 N ARG C 3
SHEET 3 G 4 LEU C 59 LEU C 69 -1 N TRP C 67 O PHE C 113
SHEET 4 G 4 PRO C 42 HIS C 53 -1 N LYS C 43 O THR C 68
SHEET 1 H 5 CYS C 19 SER C 24 0
SHEET 2 H 5 ARG C 93 PHE C 100 -1 O ARG C 97 N LYS C 22
SHEET 3 H 5 GLY C 80 GLN C 87 -1 N ALA C 81 O PHE C 98
SHEET 4 H 5 GLN C 124 LEU C 133 -1 O THR C 129 N SER C 84
SHEET 5 H 5 HIS C 144 VAL C 151 -1 O PHE C 149 N TYR C 126
SHEET 1 I 3 THR C 177 LEU C 181 0
SHEET 2 I 3 GLN C 185 SER C 189 -1 O ARG C 187 N GLU C 179
SHEET 3 I 3 VAL C 235 THR C 238 -1 O LEU C 237 N LEU C 186
SHEET 1 J 8 ARG D 61 TYR D 62 0
SHEET 2 J 8 ASN D 88 ARG D 101 -1 O LEU D 99 N TYR D 62
SHEET 3 J 8 SER D 109 VAL D 124 -1 O THR D 122 N VAL D 90
SHEET 4 J 8 THR E 21 ASN E 30 1 O MET E 23 N PHE D 110
SHEET 5 J 8 THR D 21 ASN D 25 -1 N VAL D 24 O VAL E 22
SHEET 6 J 8 PHE E 110 VAL E 124 1 O LEU E 112 N ASN D 25
SHEET 7 J 8 ASN E 88 ARG E 101 -1 N VAL E 90 O THR E 122
SHEET 8 J 8 ARG E 61 TYR E 62 -1 N TYR E 62 O LEU E 99
SHEET 1 K 2 TRP D 51 GLU D 57 0
SHEET 2 K 2 VAL D 65 CYS D 71 -1 O GLU D 68 N HIS D 54
SHEET 1 L 2 CYS D 76 ILE D 77 0
SHEET 2 L 2 VAL D 83 ASP D 84 -1 O ASP D 84 N CYS D 76
SHEET 1 M 5 VAL D 128 HIS D 130 0
SHEET 2 M 5 ARG F 265 VAL F 270 1 O SER F 267 N HIS D 129
SHEET 3 M 5 CYS F 245 PRO F 254 -1 N VAL F 250 O ALA F 268
SHEET 4 M 5 TYR F 199 PRO F 207 -1 N THR F 204 O GLN F 249
SHEET 5 M 5 PHE F 215 ILE F 221 -1 O PHE F 215 N SER F 205
SHEET 1 N 2 TRP E 51 GLU E 57 0
SHEET 2 N 2 VAL E 65 CYS E 71 -1 O GLU E 68 N HIS E 54
SHEET 1 O 2 CYS E 76 ILE E 77 0
SHEET 2 O 2 VAL E 83 ASP E 84 -1 O ASP E 84 N CYS E 76
SHEET 1 P 4 ARG F 3 LEU F 4 0
SHEET 2 P 4 ARG F 112 VAL F 119 -1 O VAL F 119 N ARG F 3
SHEET 3 P 4 LEU F 59 LEU F 69 -1 N TRP F 67 O PHE F 113
SHEET 4 P 4 PRO F 42 HIS F 53 -1 N ALA F 52 O PHE F 60
SHEET 1 Q 5 CYS F 19 SER F 24 0
SHEET 2 Q 5 ARG F 93 PHE F 100 -1 O ARG F 97 N LYS F 22
SHEET 3 Q 5 GLY F 80 GLN F 87 -1 N ALA F 81 O PHE F 98
SHEET 4 Q 5 GLN F 124 LEU F 133 -1 O THR F 129 N SER F 84
SHEET 5 Q 5 HIS F 144 VAL F 151 -1 O VAL F 151 N GLN F 124
SHEET 1 R 3 THR F 177 LEU F 181 0
SHEET 2 R 3 GLN F 185 SER F 189 -1 O ARG F 187 N GLU F 179
SHEET 3 R 3 VAL F 235 THR F 238 -1 O LEU F 237 N LEU F 186
SSBOND 1 CYS A 71 CYS A 121 1555 1555 2.06
SSBOND 2 CYS A 76 CYS A 123 1555 1555 2.04
SSBOND 3 CYS B 71 CYS B 121 1555 1555 2.07
SSBOND 4 CYS B 76 CYS B 123 1555 1555 2.04
SSBOND 5 CYS C 12 CYS C 19 1555 1555 2.04
SSBOND 6 CYS C 26 CYS C 95 1555 1555 2.05
SSBOND 7 CYS C 154 CYS C 165 1555 1555 2.04
SSBOND 8 CYS C 214 CYS C 245 1555 1555 2.04
SSBOND 9 CYS C 246 CYS C 272 1555 1555 2.05
SSBOND 10 CYS C 259 CYS C 263 1555 1555 2.05
SSBOND 11 CYS D 71 CYS D 121 1555 1555 2.06
SSBOND 12 CYS D 76 CYS D 123 1555 1555 2.04
SSBOND 13 CYS E 71 CYS E 121 1555 1555 2.05
SSBOND 14 CYS E 76 CYS E 123 1555 1555 2.05
SSBOND 15 CYS F 12 CYS F 19 1555 1555 2.05
SSBOND 16 CYS F 26 CYS F 95 1555 1555 2.06
SSBOND 17 CYS F 154 CYS F 165 1555 1555 2.04
SSBOND 18 CYS F 214 CYS F 245 1555 1555 2.04
SSBOND 19 CYS F 246 CYS F 272 1555 1555 2.04
SSBOND 20 CYS F 259 CYS F 263 1555 1555 2.03
LINK ND2 ASN C 18 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN C 23 C1 NAG H 1 1555 1555 1.43
LINK ND2 ASN C 194 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN F 23 C1 NAG F 606 1555 1555 1.43
LINK ND2 ASN F 194 C1 NAG J 1 1555 1555 1.43
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.42
LINK O6 NAG G 1 C1 FUC G 5 1555 1555 1.40
LINK O4 NAG G 2 C1 MAN G 3 1555 1555 1.43
LINK O3 MAN G 3 C1 MAN G 4 1555 1555 1.43
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43
LINK O6 NAG H 1 C1 FUC H 3 1555 1555 1.41
LINK O6 NAG I 1 C1 FUC I 2 1555 1555 1.41
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.42
LINK O6 NAG J 1 C1 FUC J 5 1555 1555 1.40
LINK O4 NAG J 2 C1 MAN J 3 1555 1555 1.43
LINK O3 MAN J 3 C1 MAN J 4 1555 1555 1.43
CISPEP 1 ASN A 17 PHE A 18 0 4.61
CISPEP 2 TYR A 62 PRO A 63 0 -3.29
CISPEP 3 GLU A 102 PRO A 103 0 -4.38
CISPEP 4 TYR B 62 PRO B 63 0 -1.16
CISPEP 5 PRO B 103 PRO B 104 0 14.36
CISPEP 6 PRO B 107 ASN B 108 0 7.71
CISPEP 7 LEU C 133 PRO C 134 0 2.39
CISPEP 8 TYR D 62 PRO D 63 0 -0.58
CISPEP 9 GLU D 102 PRO D 103 0 4.19
CISPEP 10 TYR E 62 PRO E 63 0 -1.23
CISPEP 11 PRO E 103 PRO E 104 0 18.96
CISPEP 12 PRO E 107 ASN E 108 0 5.01
CISPEP 13 LEU F 133 PRO F 134 0 2.76
CRYST1 138.710 138.710 179.090 90.00 90.00 120.00 P 31 2 1 24
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 0.007209 0.004162 0.000000 0.00000
SCALE2 0.000000 0.008325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005584 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
