HEADER SIGNALING PROTEIN 24-FEB-17 5N9B
TITLE CRYSTAL STRUCTURE OF UNLIGANDED HUMAN IL-17RA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-17 RECEPTOR A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RSIDUES 33-318;
COMPND 5 SYNONYM: IL-17RA,CDW217;
COMPND 6 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: IL17RA, IL17R;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PRS5
KEYWDS FIBRONECTIN TYPE III, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-M.RONDEAU,A.GOEPFERT
REVDAT 3 29-JUL-20 5N9B 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 12-JUN-19 5N9B 1 JRNL
REVDAT 1 13-JUN-18 5N9B 0
JRNL AUTH A.GOEPFERT,S.LEHMANN,E.WIRTH,J.-M.RONDEAU
JRNL TITL X-RAY STUDIES ON THE IL-17A/F HETERODIMER REVEAL A TWO-FACED
JRNL TITL 2 CYTOKINE AND PROVIDE NEW STRUCTURAL INSIGHTS INTO IL-17
JRNL TITL 3 SIGNALING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 24918
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1246
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2755
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2280
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2618
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.97
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1989
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 189
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.45620
REMARK 3 B22 (A**2) : 6.13200
REMARK 3 B33 (A**2) : 2.32420
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) : 0.240
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.144
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.138
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.135
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.133
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 : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2109 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2877 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 730 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 51 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 306 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2109 ; 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 : 284 ; 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 : 2304 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.71
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.30
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9972 -19.7529 17.5814
REMARK 3 T TENSOR
REMARK 3 T11: -0.0475 T22: -0.0188
REMARK 3 T33: -0.1011 T12: -0.0038
REMARK 3 T13: -0.0243 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.3594 L22: 1.6146
REMARK 3 L33: 0.6070 L12: 0.3473
REMARK 3 L13: -0.2233 L23: -0.7511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: 0.0590 S13: 0.0053
REMARK 3 S21: -0.1848 S22: -0.0109 S23: 0.0561
REMARK 3 S31: 0.0673 S32: 0.0139 S33: 0.0307
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5N9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000010
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24921
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 59.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.263
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.53
REMARK 200 R MERGE FOR SHELL (I) : 1.12500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.730
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4HSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, PEG 2000 MME, LITHIUM
REMARK 280 SULFATE, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293K
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 20.29650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.69250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.84250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.69250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.29650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.84250
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASP A 59
REMARK 465 ASP A 60
REMARK 465 SER A 61
REMARK 465 TRP A 62
REMARK 465 ILE A 63
REMARK 465 HIS A 64
REMARK 465 PRO A 65
REMARK 465 ARG A 66
REMARK 465 ASN A 67
REMARK 465 LEU A 68
REMARK 465 THR A 69
REMARK 465 PRO A 70
REMARK 465 SER A 71
REMARK 465 SER A 133
REMARK 465 LYS A 134
REMARK 465 LEU A 135
REMARK 465 ARG A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 LYS A 166
REMARK 465 PRO A 167
REMARK 465 ILE A 168
REMARK 465 PRO A 169
REMARK 465 ASP A 170
REMARK 465 GLY A 171
REMARK 465 ASP A 172
REMARK 465 PRO A 173
REMARK 465 ASN A 174
REMARK 465 MET A 306
REMARK 465 PRO A 307
REMARK 465 ASP A 308
REMARK 465 THR A 309
REMARK 465 PRO A 310
REMARK 465 GLU A 311
REMARK 465 PRO A 312
REMARK 465 ILE A 313
REMARK 465 PRO A 314
REMARK 465 ASP A 315
REMARK 465 TYR A 316
REMARK 465 MET A 317
REMARK 465 PRO A 318
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 ALA A 214 56.89 -101.11
REMARK 500 TRP A 224 -159.76 -93.98
REMARK 500 LEU A 291 -109.66 47.38
REMARK 500 PRO A 304 45.51 -87.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5N92 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FREE IL-17A/F
DBREF 5N9B A 33 318 UNP Q96F46 I17RA_HUMAN 33 318
SEQRES 1 A 286 LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER GLN
SEQRES 2 A 286 PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS LEU
SEQRES 3 A 286 ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO SER
SEQRES 4 A 286 SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA HIS
SEQRES 5 A 286 THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE GLU
SEQRES 6 A 286 TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU GLU
SEQRES 7 A 286 GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN GLU
SEQRES 8 A 286 ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU ARG
SEQRES 9 A 286 HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS PHE
SEQRES 10 A 286 VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL HIS
SEQRES 11 A 286 HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN HIS
SEQRES 12 A 286 GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS ALA
SEQRES 13 A 286 ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY SER
SEQRES 14 A 286 LEU TRP ASP PRO ASN ILE THR VAL GLU THR LEU GLU ALA
SEQRES 15 A 286 HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU SER
SEQRES 16 A 286 THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS MET
SEQRES 17 A 286 GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE PRO
SEQRES 18 A 286 ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASN VAL
SEQRES 19 A 286 THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG HIS
SEQRES 20 A 286 GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU ASN
SEQRES 21 A 286 ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO GLU
SEQRES 22 A 286 MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET PRO
HET NAG A 401 14
HET NAG A 402 14
HET NAG A 403 14
HET NAG A 404 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 6 HOH *189(H2 O)
HELIX 1 AA1 HIS A 187 VAL A 192 1 6
HELIX 2 AA2 THR A 193 SER A 199 1 7
HELIX 3 AA3 ARG A 256 PHE A 260 5 5
SHEET 1 AA1 4 ARG A 34 LEU A 35 0
SHEET 2 AA1 4 ARG A 141 VAL A 150 -1 O VAL A 150 N ARG A 34
SHEET 3 AA1 4 LEU A 90 GLN A 101 -1 N TRP A 98 O PHE A 144
SHEET 4 AA1 4 LYS A 74 HIS A 84 -1 N GLN A 79 O HIS A 95
SHEET 1 AA2 6 LEU A 41 VAL A 42 0
SHEET 2 AA2 6 CYS A 50 SER A 55 -1 O VAL A 52 N LEU A 41
SHEET 3 AA2 6 ARG A 124 PHE A 131 -1 O GLU A 130 N THR A 51
SHEET 4 AA2 6 GLY A 111 GLN A 118 -1 N ALA A 112 O PHE A 129
SHEET 5 AA2 6 GLU A 156 LEU A 164 -1 O HIS A 162 N GLU A 113
SHEET 6 AA2 6 GLN A 176 LEU A 181 -1 O LYS A 178 N VAL A 159
SHEET 1 AA3 3 THR A 208 LEU A 212 0
SHEET 2 AA3 3 GLN A 216 THR A 222 -1 O GLN A 216 N LEU A 212
SHEET 3 AA3 3 ARG A 263 THR A 269 -1 O VAL A 266 N VAL A 219
SHEET 1 AA4 4 PHE A 246 ILE A 252 0
SHEET 2 AA4 4 TYR A 230 PHE A 237 -1 N LEU A 234 O HIS A 248
SHEET 3 AA4 4 ARG A 278 PRO A 285 -1 O GLN A 280 N THR A 235
SHEET 4 AA4 4 HIS A 297 VAL A 301 -1 O HIS A 297 N ILE A 283
SSBOND 1 CYS A 43 CYS A 50 1555 1555 2.06
SSBOND 2 CYS A 57 CYS A 126 1555 1555 2.05
SSBOND 3 CYS A 185 CYS A 196 1555 1555 2.06
SSBOND 4 CYS A 245 CYS A 276 1555 1555 2.04
SSBOND 5 CYS A 277 CYS A 303 1555 1555 2.03
SSBOND 6 CYS A 290 CYS A 294 1555 1555 2.03
LINK ND2 ASN A 206 C1 NAG A 402 1555 1555 1.43
LINK ND2 ASN A 225 C1 NAG A 404 1555 1555 1.43
LINK ND2 ASN A 242 C1 NAG A 403 1555 1555 1.43
LINK ND2 ASN A 265 C1 NAG A 401 1555 1555 1.43
CISPEP 1 LEU A 164 PRO A 165 0 -2.27
CRYST1 40.593 71.685 105.385 90.00 90.00 90.00 P 21 21 21 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 0.024635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END