HEADER IMMUNE SYSTEM 07-FEB-15 4Y19
TITLE IMMUNE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 26-206;
COMPND 5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-4 BETA CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 30-219;
COMPND 11 SYNONYM: MHC CLASS II ANTIGEN DRB1*4,DR4;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: INSULIN;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: UNP RESIDUES 75-90;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: FS18_ALPHA;
COMPND 20 CHAIN: D;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: FS18_BETA;
COMPND 24 CHAIN: E;
COMPND 25 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: HLA-DRA, HLA-DRA1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: HLA-DRB1;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 20 ORGANISM_COMMON: HUMAN;
SOURCE 21 ORGANISM_TAXID: 9606;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 27 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 28 MOL_ID: 5;
SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 33 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS TCR MHC, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.X.BERINGER,J.PETERSEN,H.H.REID,J.ROSSJOHN
REVDAT 8 27-SEP-23 4Y19 1 HETSYN LINK
REVDAT 7 29-JUL-20 4Y19 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE ATOM
REVDAT 6 01-JAN-20 4Y19 1 REMARK
REVDAT 5 17-JAN-18 4Y19 1 REMARK
REVDAT 4 13-SEP-17 4Y19 1 REMARK
REVDAT 3 04-NOV-15 4Y19 1 JRNL
REVDAT 2 21-OCT-15 4Y19 1 JRNL REMARK
REVDAT 1 23-SEP-15 4Y19 0
JRNL AUTH D.X.BERINGER,F.S.KLEIJWEGT,F.WIEDE,A.R.VAN DER SLIK,K.L.LOH,
JRNL AUTH 2 J.PETERSEN,N.L.DUDEK,G.DUINKERKEN,S.LABAN,A.JOOSTEN,
JRNL AUTH 3 J.P.VIVIAN,Z.CHEN,A.P.ULDRICH,D.I.GODFREY,J.MCCLUSKEY,
JRNL AUTH 4 D.A.PRICE,K.J.RADFORD,A.W.PURCELL,T.NIKOLIC,H.H.REID,
JRNL AUTH 5 T.TIGANIS,B.O.ROEP,J.ROSSJOHN
JRNL TITL T CELL RECEPTOR REVERSED POLARITY RECOGNITION OF A
JRNL TITL 2 SELF-ANTIGEN MAJOR HISTOCOMPATIBILITY COMPLEX.
JRNL REF NAT.IMMUNOL. V. 16 1153 2015
JRNL REFN ESSN 1529-2916
JRNL PMID 26437244
JRNL DOI 10.1038/NI.3271
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.1
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 47150
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2351
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3438
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2003
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3267
REMARK 3 BIN R VALUE (WORKING SET) : 0.1984
REMARK 3 BIN FREE R VALUE : 0.2382
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.97
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 171
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 : 6588
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.58590
REMARK 3 B22 (A**2) : 8.66000
REMARK 3 B33 (A**2) : 2.92590
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) : 0.262
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.246
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.188
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.243
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.189
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 : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6945 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9469 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3139 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 183 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1001 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6945 ; 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 : 901 ; 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 : 7733 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.91
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7172 -48.7633 -11.4688
REMARK 3 T TENSOR
REMARK 3 T11: 0.0103 T22: -0.0975
REMARK 3 T33: -0.0963 T12: -0.0827
REMARK 3 T13: 0.0312 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.8479 L22: 1.4041
REMARK 3 L33: 1.3177 L12: 0.3382
REMARK 3 L13: 0.0792 L23: -0.7690
REMARK 3 S TENSOR
REMARK 3 S11: 0.0861 S12: -0.1058 S13: 0.1183
REMARK 3 S21: 0.3268 S22: -0.1455 S23: 0.0085
REMARK 3 S31: -0.3377 S32: 0.1570 S33: 0.0594
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2284 -45.7853 -28.2165
REMARK 3 T TENSOR
REMARK 3 T11: 0.0260 T22: -0.0475
REMARK 3 T33: -0.0191 T12: -0.0586
REMARK 3 T13: -0.0014 T23: 0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 0.3594 L22: 1.2696
REMARK 3 L33: 0.0247 L12: 0.4904
REMARK 3 L13: -0.2120 L23: -0.5031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0116 S12: -0.0010 S13: 0.0157
REMARK 3 S21: 0.0496 S22: -0.0831 S23: -0.1090
REMARK 3 S31: -0.0379 S32: 0.1064 S33: 0.0715
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -83.4681 -66.2653 -20.2161
REMARK 3 T TENSOR
REMARK 3 T11: -0.0679 T22: -0.1257
REMARK 3 T33: -0.0262 T12: 0.0287
REMARK 3 T13: 0.0504 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 1.9669 L22: 0.8107
REMARK 3 L33: 1.9882 L12: 0.1278
REMARK 3 L13: 1.0703 L23: -0.3933
REMARK 3 S TENSOR
REMARK 3 S11: 0.0845 S12: -0.0662 S13: 0.0516
REMARK 3 S21: 0.1175 S22: 0.0594 S23: 0.1714
REMARK 3 S31: -0.0233 S32: -0.2090 S33: -0.1440
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -74.0181 -60.8649 -36.2927
REMARK 3 T TENSOR
REMARK 3 T11: -0.0475 T22: -0.1309
REMARK 3 T33: -0.0237 T12: 0.0292
REMARK 3 T13: 0.0322 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 1.2435 L22: 0.7168
REMARK 3 L33: 0.9748 L12: -0.0229
REMARK 3 L13: 0.1023 L23: -0.2662
REMARK 3 S TENSOR
REMARK 3 S11: 0.1117 S12: 0.0839 S13: 0.1331
REMARK 3 S21: -0.0391 S22: -0.0144 S23: 0.1154
REMARK 3 S31: -0.0223 S32: -0.0675 S33: -0.0973
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Y19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47168
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.62900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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: 4G8F, 1BD2, 4MDI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 2 M AMMONIUM
REMARK 280 SULFATE AND 0.2 M SODIUM MALONATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 57.88000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.37000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 76.54500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 57.88000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.37000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.54500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 57.88000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.37000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.54500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 57.88000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.37000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 76.54500
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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 ILE A 1
REMARK 465 LYS A 2
REMARK 465 THR A 182
REMARK 465 SER A 183
REMARK 465 GLY A 184
REMARK 465 ASP A 185
REMARK 465 ASP A 186
REMARK 465 ASP A 187
REMARK 465 ASP A 188
REMARK 465 LYS A 189
REMARK 465 GLY B -1
REMARK 465 LYS B 105
REMARK 465 THR B 106
REMARK 465 GLN B 107
REMARK 465 PRO B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
REMARK 465 HIS B 111
REMARK 465 HIS B 112
REMARK 465 GLY B 192
REMARK 465 GLY B 193
REMARK 465 ASP B 194
REMARK 465 ASP B 195
REMARK 465 ASP B 196
REMARK 465 ASP B 197
REMARK 465 LYS B 198
REMARK 465 GLY C -4
REMARK 465 SER C -3
REMARK 465 LEU C -2
REMARK 465 SER D 220
REMARK 465 PRO D 221
REMARK 465 GLU D 222
REMARK 465 SER D 223
REMARK 465 SER D 224
REMARK 465 MET E 0
REMARK 465 ASN E 1
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 GLU A 3 CG CD OE1 OE2
REMARK 470 THR B 191 OG1 CG2
REMARK 470 GLN C -1 CG CD OE1 NE2
REMARK 470 MET D 1 CG SD CE
REMARK 470 LYS D 146 CG CD CE NZ
REMARK 470 SER D 147 OG
REMARK 470 SER D 148 OG
REMARK 470 ASP D 149 CG OD1 OD2
REMARK 470 LYS D 150 CG CD CE NZ
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 HIS B 33 -99.69 71.34
REMARK 500 THR B 90 -79.51 -125.14
REMARK 500 THR B 140 -79.43 -77.30
REMARK 500 TRP B 153 32.83 70.52
REMARK 500 LEU D 53 -66.95 -107.13
REMARK 500 TYR D 109 123.76 -39.95
REMARK 500 SER D 114 141.18 -170.83
REMARK 500 ASP D 149 -73.76 -69.91
REMARK 500 ILE E 53 -61.55 -90.28
REMARK 500 SER E 93 85.18 -151.80
REMARK 500 HIS E 165 61.89 -119.70
REMARK 500 ASP E 196 59.86 -106.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Y1A RELATED DB: PDB
DBREF 4Y19 A 1 181 UNP P01903 DRA_HUMAN 26 206
DBREF 4Y19 B 1 190 UNP P13760 2B14_HUMAN 30 219
DBREF 4Y19 C -4 11 UNP P01308 INS_HUMAN 75 90
DBREF 4Y19 D 1 224 PDB 4Y19 4Y19 1 224
DBREF 4Y19 E 0 255 PDB 4Y19 4Y19 0 255
SEQADV 4Y19 THR A 182 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 SER A 183 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 GLY A 184 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 ASP A 185 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 ASP A 186 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 ASP A 187 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 ASP A 188 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 LYS A 189 UNP P01903 EXPRESSION TAG
SEQADV 4Y19 GLY B -1 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 SER B 0 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 THR B 191 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 GLY B 192 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 GLY B 193 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 ASP B 194 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 ASP B 195 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 ASP B 196 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 ASP B 197 UNP P13760 EXPRESSION TAG
SEQADV 4Y19 LYS B 198 UNP P13760 EXPRESSION TAG
SEQRES 1 A 189 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 189 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 189 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 189 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 189 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 189 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 189 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 189 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 189 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 189 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 189 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 189 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 189 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 189 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP THR
SEQRES 15 A 189 SER GLY ASP ASP ASP ASP LYS
SEQRES 1 B 200 GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU GLN VAL
SEQRES 2 B 200 LYS HIS GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL
SEQRES 3 B 200 ARG PHE LEU ASP ARG TYR PHE TYR HIS GLN GLU GLU TYR
SEQRES 4 B 200 VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL
SEQRES 5 B 200 THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER
SEQRES 6 B 200 GLN LYS ASP LEU LEU GLU GLN LYS ARG ALA ALA VAL ASP
SEQRES 7 B 200 THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE
SEQRES 8 B 200 THR VAL GLN ARG ARG VAL TYR PRO GLU VAL THR VAL TYR
SEQRES 9 B 200 PRO ALA LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU
SEQRES 10 B 200 VAL CYS SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU
SEQRES 11 B 200 VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY
SEQRES 12 B 200 VAL VAL SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR
SEQRES 13 B 200 PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER
SEQRES 14 B 200 GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER LEU
SEQRES 15 B 200 THR SER PRO LEU THR VAL GLU TRP ARG ALA THR GLY GLY
SEQRES 16 B 200 ASP ASP ASP ASP LYS
SEQRES 1 C 16 GLY SER LEU GLN PRO LEU ALA LEU GLU GLY SER LEU GLN
SEQRES 2 C 16 LYS ARG GLY
SEQRES 1 D 210 MET GLN GLN VAL LYS GLN ASN SER PRO SER LEU SER VAL
SEQRES 2 D 210 GLN GLU GLY ARG ILE SER ILE LEU ASN CYS ASP TYR THR
SEQRES 3 D 210 ASN SER MET PHE ASP TYR PHE LEU TRP TYR LYS LYS TYR
SEQRES 4 D 210 PRO ALA GLU GLY PRO THR PHE LEU ILE SER ILE SER SER
SEQRES 5 D 210 ILE LYS ASP LYS ASN GLU ASP GLY ARG PHE THR VAL PHE
SEQRES 6 D 210 LEU ASN LYS SER ALA LYS HIS LEU SER LEU HIS ILE VAL
SEQRES 7 D 210 PRO SER GLN PRO GLY ASP SER ALA VAL TYR PHE CYS ALA
SEQRES 8 D 210 ALA SER VAL TYR ALA GLY GLY THR SER TYR GLY LYS LEU
SEQRES 9 D 210 THR PHE GLY GLN GLY THR ILE LEU THR VAL HIS PRO ASN
SEQRES 10 D 210 ILE GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP
SEQRES 11 D 210 SER LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP
SEQRES 12 D 210 PHE ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER
SEQRES 13 D 210 ASP VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG
SEQRES 14 D 210 SER MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER
SEQRES 15 D 210 ASN LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN
SEQRES 16 D 210 SER ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU
SEQRES 17 D 210 SER SER
SEQRES 1 E 243 MET ASN ALA GLY VAL THR GLN THR PRO LYS PHE ARG VAL
SEQRES 2 E 243 LEU LYS THR GLY GLN SER MET THR LEU LEU CYS ALA GLN
SEQRES 3 E 243 ASP MET ASN HIS GLU TYR MET TYR TRP TYR ARG GLN ASP
SEQRES 4 E 243 PRO GLY MET GLY LEU ARG LEU ILE HIS TYR SER VAL GLY
SEQRES 5 E 243 GLU GLY THR THR ALA LYS GLY GLU VAL PRO ASP GLY TYR
SEQRES 6 E 243 ASN VAL SER ARG LEU LYS LYS GLN ASN PHE LEU LEU GLY
SEQRES 7 E 243 LEU GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE
SEQRES 8 E 243 CYS ALA SER ARG PRO ARG ARG ASP ASN GLU GLN PHE PHE
SEQRES 9 E 243 GLY PRO GLY THR ARG LEU THR VAL LEU GLU ASP LEU LYS
SEQRES 10 E 243 ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER
SEQRES 11 E 243 GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL
SEQRES 12 E 243 CYS LEU ALA THR GLY PHE PHE PRO ASP HIS VAL GLU LEU
SEQRES 13 E 243 SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL
SEQRES 14 E 243 CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU
SEQRES 15 E 243 ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL
SEQRES 16 E 243 SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG
SEQRES 17 E 243 CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU
SEQRES 18 E 243 TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL
SEQRES 19 E 243 SER ALA GLU ALA TRP GLY ARG ALA ASP
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET MAN F 4 11
HET MAN F 5 11
HET MAN F 6 11
HET MAN F 7 11
HET NAG G 1 14
HET NAG G 2 14
HET MLI B 201 7
HET MLI B 202 7
HET MLI D 301 7
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM MLI MALONATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 6 NAG 4(C8 H15 N O6)
FORMUL 6 BMA C6 H12 O6
FORMUL 6 MAN 4(C6 H12 O6)
FORMUL 8 MLI 3(C3 H2 O4 2-)
FORMUL 11 HOH *306(H2 O)
HELIX 1 AA1 GLU A 47 ALA A 52 1 6
HELIX 2 AA2 GLU A 55 SER A 77 1 23
HELIX 3 AA3 THR B 51 LEU B 53 5 3
HELIX 4 AA4 GLY B 54 SER B 63 1 10
HELIX 5 AA5 GLN B 64 TYR B 78 1 15
HELIX 6 AA6 TYR B 78 GLU B 87 1 10
HELIX 7 AA7 SER B 88 THR B 90 5 3
HELIX 8 AA8 LYS D 82 ALA D 84 5 3
HELIX 9 AA9 GLN D 95 SER D 99 5 5
HELIX 10 AB1 ALA D 202 PHE D 207 1 6
HELIX 11 AB2 ALA E 95 THR E 99 5 5
HELIX 12 AB3 ASP E 127 VAL E 131 5 5
HELIX 13 AB4 SER E 142 GLN E 150 1 9
HELIX 14 AB5 ALA E 209 GLN E 213 1 5
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N HIS A 33 O VAL A 42
SHEET 3 AA1 8 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 AA1 8 HIS A 5 ASN A 15 -1 N ALA A 10 O MET A 23
SHEET 5 AA1 8 PHE B 7 PHE B 18 -1 O PHE B 7 N ASN A 15
SHEET 6 AA1 8 ARG B 23 TYR B 32 -1 O LEU B 27 N GLU B 14
SHEET 7 AA1 8 GLU B 35 ASP B 41 -1 O GLU B 35 N TYR B 32
SHEET 8 AA1 8 TYR B 47 ALA B 49 -1 O ARG B 48 N ARG B 39
SHEET 1 AA2 4 GLU A 88 THR A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O HIS A 149 N CYS A 107
SHEET 4 AA2 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 THR A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O HIS A 149 N CYS A 107
SHEET 4 AA3 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 AA4 4 LYS A 126 PRO A 127 0
SHEET 2 AA4 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 AA4 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 AA5 4 GLU B 98 PRO B 103 0
SHEET 2 AA5 4 LEU B 114 PHE B 122 -1 O SER B 118 N THR B 100
SHEET 3 AA5 4 PHE B 155 GLU B 162 -1 O LEU B 161 N LEU B 115
SHEET 4 AA5 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 AA6 4 GLU B 98 PRO B 103 0
SHEET 2 AA6 4 LEU B 114 PHE B 122 -1 O SER B 118 N THR B 100
SHEET 3 AA6 4 PHE B 155 GLU B 162 -1 O LEU B 161 N LEU B 115
SHEET 4 AA6 4 ILE B 148 GLN B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 AA7 4 GLN B 136 GLU B 138 0
SHEET 2 AA7 4 GLU B 128 ARG B 133 -1 N TRP B 131 O GLU B 138
SHEET 3 AA7 4 VAL B 170 GLU B 176 -1 O GLN B 174 N ARG B 130
SHEET 4 AA7 4 LEU B 184 ARG B 189 -1 O TRP B 188 N TYR B 171
SHEET 1 AA8 5 VAL D 4 LYS D 5 0
SHEET 2 AA8 5 SER D 19 TYR D 25 -1 O ASP D 24 N LYS D 5
SHEET 3 AA8 5 HIS D 86 ILE D 91 -1 O LEU D 87 N CYS D 23
SHEET 4 AA8 5 PHE D 76 ASN D 81 -1 N ASN D 81 O HIS D 86
SHEET 5 AA8 5 LYS D 65 ASP D 68 -1 N ASP D 68 O PHE D 76
SHEET 1 AA9 5 SER D 10 GLN D 14 0
SHEET 2 AA9 5 THR D 124 HIS D 129 1 O ILE D 125 N LEU D 11
SHEET 3 AA9 5 ALA D 100 SER D 107 -1 N ALA D 100 O LEU D 126
SHEET 4 AA9 5 TYR D 38 LYS D 44 -1 N TYR D 42 O PHE D 103
SHEET 5 AA9 5 THR D 51 SER D 57 -1 O THR D 51 N LYS D 43
SHEET 1 AB1 4 SER D 10 GLN D 14 0
SHEET 2 AB1 4 THR D 124 HIS D 129 1 O ILE D 125 N LEU D 11
SHEET 3 AB1 4 ALA D 100 SER D 107 -1 N ALA D 100 O LEU D 126
SHEET 4 AB1 4 THR D 119 PHE D 120 -1 O THR D 119 N ALA D 106
SHEET 1 AB2 4 ALA D 138 ARG D 143 0
SHEET 2 AB2 4 SER D 151 THR D 156 -1 O LEU D 154 N TYR D 140
SHEET 3 AB2 4 PHE D 187 SER D 196 -1 O ALA D 194 N CYS D 153
SHEET 4 AB2 4 VAL D 172 ILE D 174 -1 N TYR D 173 O TRP D 195
SHEET 1 AB3 4 ALA D 138 ARG D 143 0
SHEET 2 AB3 4 SER D 151 THR D 156 -1 O LEU D 154 N TYR D 140
SHEET 3 AB3 4 PHE D 187 SER D 196 -1 O ALA D 194 N CYS D 153
SHEET 4 AB3 4 CYS D 178 MET D 182 -1 N MET D 182 O PHE D 187
SHEET 1 AB4 4 VAL E 4 THR E 7 0
SHEET 2 AB4 4 MET E 19 GLN E 25 -1 O ALA E 24 N THR E 5
SHEET 3 AB4 4 ASN E 86 LEU E 91 -1 O LEU E 89 N LEU E 21
SHEET 4 AB4 4 ASN E 77 SER E 79 -1 N ASN E 77 O GLY E 90
SHEET 1 AB5 6 PHE E 10 LYS E 14 0
SHEET 2 AB5 6 THR E 120 LEU E 125 1 O LEU E 125 N LEU E 13
SHEET 3 AB5 6 SER E 100 ARG E 107 -1 N SER E 100 O LEU E 122
SHEET 4 AB5 6 TYR E 38 ASP E 45 -1 N TYR E 42 O PHE E 103
SHEET 5 AB5 6 GLY E 49 SER E 56 -1 O ILE E 53 N TRP E 41
SHEET 6 AB5 6 ALA E 67 LYS E 68 -1 O ALA E 67 N TYR E 55
SHEET 1 AB6 4 PHE E 10 LYS E 14 0
SHEET 2 AB6 4 THR E 120 LEU E 125 1 O LEU E 125 N LEU E 13
SHEET 3 AB6 4 SER E 100 ARG E 107 -1 N SER E 100 O LEU E 122
SHEET 4 AB6 4 PHE E 115 PHE E 116 -1 O PHE E 115 N SER E 106
SHEET 1 AB7 4 GLU E 135 PHE E 139 0
SHEET 2 AB7 4 LYS E 151 PHE E 161 -1 O LEU E 157 N ALA E 137
SHEET 3 AB7 4 TYR E 199 SER E 208 -1 O VAL E 207 N ALA E 152
SHEET 4 AB7 4 VAL E 181 THR E 183 -1 N CYS E 182 O ARG E 204
SHEET 1 AB8 4 GLU E 135 PHE E 139 0
SHEET 2 AB8 4 LYS E 151 PHE E 161 -1 O LEU E 157 N ALA E 137
SHEET 3 AB8 4 TYR E 199 SER E 208 -1 O VAL E 207 N ALA E 152
SHEET 4 AB8 4 LEU E 188 LYS E 189 -1 N LEU E 188 O ALA E 200
SHEET 1 AB9 4 LYS E 175 VAL E 177 0
SHEET 2 AB9 4 VAL E 166 VAL E 172 -1 N VAL E 172 O LYS E 175
SHEET 3 AB9 4 HIS E 218 PHE E 225 -1 O GLN E 222 N SER E 169
SHEET 4 AB9 4 GLN E 244 TRP E 251 -1 O GLN E 244 N PHE E 225
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.07
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.02
SSBOND 4 CYS D 23 CYS D 104 1555 1555 2.03
SSBOND 5 CYS D 153 CYS D 203 1555 1555 2.04
SSBOND 6 CYS D 178 CYS E 182 1555 1555 2.04
SSBOND 7 CYS E 23 CYS E 104 1555 1555 2.02
SSBOND 8 CYS E 156 CYS E 221 1555 1555 2.02
LINK ND2 ASN A 78 C1 NAG F 1 1555 1555 1.43
LINK ND2 ASN A 118 C1 NAG G 1 1555 1555 1.43
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.41
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.39
LINK O6 BMA F 3 C1 MAN F 4 1555 1555 1.39
LINK O3 BMA F 3 C1 MAN F 7 1555 1555 1.42
LINK O3 MAN F 4 C1 MAN F 5 1555 1555 1.45
LINK O6 MAN F 4 C1 MAN F 6 1555 1555 1.41
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43
CISPEP 1 ASN A 15 PRO A 16 0 2.58
CISPEP 2 THR A 113 PRO A 114 0 -1.23
CISPEP 3 TYR B 123 PRO B 124 0 2.07
CISPEP 4 VAL D 92 PRO D 93 0 -13.04
CISPEP 5 THR E 7 PRO E 8 0 -6.50
CISPEP 6 PHE E 162 PRO E 163 0 -3.76
CRYST1 115.760 152.740 153.090 90.00 90.00 90.00 I 2 2 2 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 0.008639 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006547 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
