HEADER IMMUNE SYSTEM 02-MAR-17 5NBQ
TITLE THE STRUCTURE OF THE TRIPARTITE COMPLEX BETWEEN OSPE, THE C-TERMINAL
TITLE 2 DOMAINS OF FACTOR H AND C3DG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT C3;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING
COMPND 5 PROTEIN 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: COMPLEMENT FACTOR H;
COMPND 10 CHAIN: D, E, F;
COMPND 11 SYNONYM: H FACTOR 1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: OUTER SURFACE PROTEIN E;
COMPND 15 CHAIN: G, I;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: OUTER SURFACE PROTEIN E,OUTER SURFACE PROTEIN E;
COMPND 19 CHAIN: H;
COMPND 20 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: C3, CPAMD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-22B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: CFH, HF, HF1, HF2;
SOURCE 15 EXPRESSION_SYSTEM: PICHIA;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 4919;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: BORRELIELLA BURGDORFERI;
SOURCE 19 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;
SOURCE 20 ORGANISM_TAXID: 139;
SOURCE 21 GENE: OSPE;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 MOL_ID: 4;
SOURCE 25 ORGANISM_SCIENTIFIC: BORRELIELLA BURGDORFERI;
SOURCE 26 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;
SOURCE 27 ORGANISM_TAXID: 139;
SOURCE 28 GENE: OSPE;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEMENT, REGULATION, MICROBE, EVASION, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KOLODZIEJCZYK,K.M.MIKULA,T.M.KOTILA,V.L.G.POSTIS,J.T.SAKARI,T.MERI
REVDAT 2 13-DEC-17 5NBQ 1 JRNL
REVDAT 1 06-DEC-17 5NBQ 0
JRNL AUTH R.KOLODZIEJCZYK,K.M.MIKULA,T.KOTILA,V.L.G.POSTIS,
JRNL AUTH 2 T.S.JOKIRANTA,A.GOLDMAN,T.MERI
JRNL TITL CRYSTAL STRUCTURE OF A TRIPARTITE COMPLEX BETWEEN C3DG,
JRNL TITL 2 C-TERMINAL DOMAINS OF FACTOR H AND OSPE OF BORRELIA
JRNL TITL 3 BURGDORFERI.
JRNL REF PLOS ONE V. 12 88127 2017
JRNL REFN ESSN 1932-6203
JRNL PMID 29190743
JRNL DOI 10.1371/JOURNAL.PONE.0188127
REMARK 2
REMARK 2 RESOLUTION. 3.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
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) : 3.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 29068
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840
REMARK 3 FREE R VALUE TEST SET COUNT : 1406
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 : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.18
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.29
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.21
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2061
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2596
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1971
REMARK 3 BIN R VALUE (WORKING SET) : 0.2602
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 90
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 : 11752
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 2
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 91.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.00500
REMARK 3 B22 (A**2) : -17.34660
REMARK 3 B33 (A**2) : 9.34160
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) : 0.500
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.519
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 : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12011 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 16276 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4142 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 317 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1709 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12011 ; 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 : 1561 ; 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 : 13741 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.40
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.86
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4722 30.4740 39.1732
REMARK 3 T TENSOR
REMARK 3 T11: -0.0439 T22: -0.0711
REMARK 3 T33: -0.1284 T12: 0.0833
REMARK 3 T13: 0.0917 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 2.3054 L22: 3.6974
REMARK 3 L33: 2.6305 L12: -0.9082
REMARK 3 L13: -0.9203 L23: 1.8022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0523 S12: -0.4504 S13: 0.3868
REMARK 3 S21: 0.0368 S22: 0.2375 S23: -0.4992
REMARK 3 S31: -0.1254 S32: 0.5422 S33: -0.2897
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9521 -1.7324 14.5549
REMARK 3 T TENSOR
REMARK 3 T11: -0.1356 T22: -0.0783
REMARK 3 T33: 0.0963 T12: -0.0438
REMARK 3 T13: -0.0161 T23: 0.1177
REMARK 3 L TENSOR
REMARK 3 L11: 2.1517 L22: 2.0951
REMARK 3 L33: 1.9636 L12: -0.1863
REMARK 3 L13: 0.3325 L23: -0.3585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0400 S12: -0.2500 S13: -0.3892
REMARK 3 S21: 0.0071 S22: 0.1852 S23: 0.5442
REMARK 3 S31: -0.0145 S32: -0.3822 S33: -0.2251
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7731 18.4172 -14.7699
REMARK 3 T TENSOR
REMARK 3 T11: -0.1582 T22: -0.0496
REMARK 3 T33: 0.0567 T12: 0.0126
REMARK 3 T13: 0.0217 T23: 0.1311
REMARK 3 L TENSOR
REMARK 3 L11: 2.4023 L22: 2.4582
REMARK 3 L33: 2.0683 L12: 0.4794
REMARK 3 L13: 0.4150 L23: 0.3708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0918 S12: 0.1060 S13: 0.4346
REMARK 3 S21: 0.2075 S22: -0.0019 S23: 0.1013
REMARK 3 S31: -0.1323 S32: -0.2154 S33: -0.0899
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9537 28.5805 46.6692
REMARK 3 T TENSOR
REMARK 3 T11: 0.0782 T22: -0.0694
REMARK 3 T33: -0.0505 T12: 0.1134
REMARK 3 T13: 0.0821 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.6758 L22: 4.4590
REMARK 3 L33: 0.0758 L12: 0.8238
REMARK 3 L13: 0.2435 L23: 0.7809
REMARK 3 S TENSOR
REMARK 3 S11: 0.0429 S12: -0.2645 S13: 0.0756
REMARK 3 S21: -0.1631 S22: 0.0060 S23: 0.0909
REMARK 3 S31: -0.0904 S32: -0.0970 S33: -0.0489
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 52.1920 24.5777 15.9792
REMARK 3 T TENSOR
REMARK 3 T11: -0.0312 T22: -0.1018
REMARK 3 T33: -0.0121 T12: -0.0419
REMARK 3 T13: 0.0566 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 4.4204 L22: 3.4837
REMARK 3 L33: 2.6858 L12: -1.4941
REMARK 3 L13: 2.5057 L23: -0.4657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0922 S12: -0.0171 S13: 0.5352
REMARK 3 S21: -0.1850 S22: 0.1698 S23: 0.2568
REMARK 3 S31: -0.2107 S32: -0.0583 S33: -0.0776
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4052 -9.7384 -8.5794
REMARK 3 T TENSOR
REMARK 3 T11: -0.1193 T22: -0.1071
REMARK 3 T33: 0.1530 T12: -0.1520
REMARK 3 T13: -0.1382 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 6.2242 L22: 0.1328
REMARK 3 L33: 3.4760 L12: 0.3991
REMARK 3 L13: -2.7268 L23: -0.1930
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: -0.2070 S13: -0.2584
REMARK 3 S21: 0.1130 S22: 0.1650 S23: -0.0521
REMARK 3 S31: 0.2757 S32: -0.0383 S33: -0.1560
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { G|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1857 23.7833 24.6374
REMARK 3 T TENSOR
REMARK 3 T11: -0.0406 T22: 0.1669
REMARK 3 T33: -0.2614 T12: 0.1520
REMARK 3 T13: 0.0069 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 3.4481 L22: 1.3259
REMARK 3 L33: 4.5394 L12: -1.5742
REMARK 3 L13: 1.0812 L23: -0.6995
REMARK 3 S TENSOR
REMARK 3 S11: 0.0739 S12: 0.2716 S13: 0.1327
REMARK 3 S21: -0.2020 S22: 0.0017 S23: 0.2903
REMARK 3 S31: -0.0210 S32: -0.1584 S33: -0.0756
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { I|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0573 -23.1729 -29.3408
REMARK 3 T TENSOR
REMARK 3 T11: 0.0215 T22: -0.1778
REMARK 3 T33: 0.0155 T12: -0.0597
REMARK 3 T13: -0.0975 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 2.0468 L22: 4.8043
REMARK 3 L33: 5.9061 L12: -0.2250
REMARK 3 L13: -2.8903 L23: 2.5426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0665 S12: -0.0147 S13: 0.0128
REMARK 3 S21: 0.1577 S22: 0.0780 S23: -0.0949
REMARK 3 S31: 0.1226 S32: 0.0693 S33: -0.0116
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200003842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.969
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29070
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.180
REMARK 200 RESOLUTION RANGE LOW (A) : 29.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.419
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.89200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1 M HEPES PH 7.5, 0.2 M
REMARK 280 MGCL2 OR 24% PEG3350, 0.1 M HEPES PH 7.5, 0.2 M MGCL2 OR 16%
REMARK 280 PEG3350, TRIS PH 8.5, 0.2 M AMMONIUM ACETATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
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 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 62.45350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.53150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.45350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.53150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 APPLY THE FOLLOWING TO CHAINS: A, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, H
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F, 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 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 ALA A 994
REMARK 465 VAL A 995
REMARK 465 ALA A 1286
REMARK 465 PRO A 1287
REMARK 465 ALA B 994
REMARK 465 PRO C 1287
REMARK 465 ASP E 1104
REMARK 465 SER E 1209
REMARK 465 ARG E 1210
REMARK 465 SER E 1211
REMARK 465 LYS E 1230
REMARK 465 ASP F 1104
REMARK 465 SER F 1105
REMARK 465 ARG F 1210
REMARK 465 SER F 1211
REMARK 465 HIS F 1212
REMARK 465 ALA F 1229
REMARK 465 LYS F 1230
REMARK 465 SER H -86
REMARK 465 LYS H -85
REMARK 465 PHE H -84
REMARK 465 THR H -83
REMARK 465 VAL H -82
REMARK 465 LYS H -81
REMARK 465 ILE H -80
REMARK 465 LYS H -79
REMARK 465 ASN H -78
REMARK 465 LYS H -77
REMARK 465 ASP H -76
REMARK 465 LYS H -75
REMARK 465 SER H -74
REMARK 465 GLY H -73
REMARK 465 ASN H -72
REMARK 465 TRP H -71
REMARK 465 THR H -70
REMARK 465 ASP H -69
REMARK 465 LEU H -68
REMARK 465 GLY H -67
REMARK 465 ASP H -66
REMARK 465 LEU H -65
REMARK 465 VAL H -64
REMARK 465 VAL H -63
REMARK 465 ARG H -62
REMARK 465 LYS H -61
REMARK 465 GLU H -60
REMARK 465 GLU H -59
REMARK 465 ASN H -58
REMARK 465 GLY H -57
REMARK 465 ILE H -56
REMARK 465 ASP H -55
REMARK 465 THR H -54
REMARK 465 GLY H -53
REMARK 465 LEU H -52
REMARK 465 ASN H -51
REMARK 465 ALA H -50
REMARK 465 GLY H -49
REMARK 465 GLY H -48
REMARK 465 HIS H -47
REMARK 465 SER H -46
REMARK 465 ALA H -45
REMARK 465 THR H -44
REMARK 465 PHE H -43
REMARK 465 PHE H -42
REMARK 465 SER H -41
REMARK 465 LEU H -40
REMARK 465 GLU H -39
REMARK 465 GLU H -38
REMARK 465 GLU H -37
REMARK 465 VAL H -36
REMARK 465 VAL H -35
REMARK 465 ASN H -34
REMARK 465 ASN H -33
REMARK 465 PHE H -32
REMARK 465 VAL H -31
REMARK 465 LYS H -30
REMARK 465 VAL H -29
REMARK 465 MET H -28
REMARK 465 THR H -27
REMARK 465 GLU H -26
REMARK 465 GLY H -25
REMARK 465 GLY H -24
REMARK 465 SER H -23
REMARK 465 PHE H -22
REMARK 465 LYS H -21
REMARK 465 THR H -20
REMARK 465 SER H -19
REMARK 465 LEU H -18
REMARK 465 TYR H -17
REMARK 465 TYR H -16
REMARK 465 GLY H -15
REMARK 465 TYR H -14
REMARK 465 LYS H -13
REMARK 465 GLU H -12
REMARK 465 GLU H -11
REMARK 465 GLN H -10
REMARK 465 SER H -9
REMARK 465 VAL H -8
REMARK 465 ILE H -7
REMARK 465 ASN H -6
REMARK 465 GLY H -5
REMARK 465 ILE H -4
REMARK 465 GLN H -3
REMARK 465 ASN H -2
REMARK 465 LYS H -1
REMARK 465 GLU H 0
REMARK 465 ILE H 1
REMARK 465 ILE H 2
REMARK 465 THR H 3
REMARK 465 LYS H 4
REMARK 465 ILE H 5
REMARK 465 GLU H 6
REMARK 465 LYS H 7
REMARK 465 ILE H 8
REMARK 465 ASP H 9
REMARK 465 GLY H 10
REMARK 465 THR H 11
REMARK 465 GLU H 12
REMARK 465 TYR H 13
REMARK 465 ILE H 14
REMARK 465 THR H 15
REMARK 465 PHE H 16
REMARK 465 SER H 17
REMARK 465 GLY H 18
REMARK 465 ASP H 19
REMARK 465 LYS H 20
REMARK 465 ILE H 21
REMARK 465 LYS H 22
REMARK 465 ASN H 23
REMARK 465 SER H 24
REMARK 465 GLY H 25
REMARK 465 ASP H 26
REMARK 465 LYS H 27
REMARK 465 VAL H 28
REMARK 465 ALA H 29
REMARK 465 GLU H 30
REMARK 465 TYR H 31
REMARK 465 ALA H 32
REMARK 465 ILE H 33
REMARK 465 SER H 34
REMARK 465 LEU H 35
REMARK 465 GLU H 36
REMARK 465 GLU H 37
REMARK 465 LEU H 38
REMARK 465 LYS H 39
REMARK 465 LYS H 40
REMARK 465 ASN H 41
REMARK 465 LEU H 42
REMARK 465 ASN I 151
REMARK 465 SER I 152
REMARK 465 GLY I 153
REMARK 465 ASP I 154
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 998 CG CD OE1 OE2
REMARK 470 LYS A1001 CG CD CE NZ
REMARK 470 GLU A1032 CG CD OE1 OE2
REMARK 470 GLU A1035 CG CD OE1 OE2
REMARK 470 LYS A1036 CG CD CE NZ
REMARK 470 LEU A1039 CB CG CD1 CD2
REMARK 470 GLU A1040 CG CD OE1 OE2
REMARK 470 LYS A1041 CG CD CE NZ
REMARK 470 ARG A1042 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1043 CG CD OE1 NE2
REMARK 470 TYR B1282 OH
REMARK 470 LYS C1001 CG CD CE NZ
REMARK 470 TYR C1262 OH
REMARK 470 GLU E1172 CG CD OE1 OE2
REMARK 470 ARG E1182 CG CD NE CZ NH1 NH2
REMARK 470 ARG E1203 CG CD NE CZ NH1 NH2
REMARK 470 ARG E1206 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 53 CG CD CE NZ
REMARK 470 LYS G 98 CG CD CE NZ
REMARK 470 LYS G 107 CG CD CE NZ
REMARK 470 LYS G 135 CG CD CE NZ
REMARK 470 LYS G 155 CG CD CE NZ
REMARK 470 LEU G 163 CG CD1 CD2
REMARK 470 LYS I 43 CG CD CE NZ
REMARK 470 GLU I 69 CG CD OE1 OE2
REMARK 470 LEU I 110 CG CD1 CD2
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 997 -59.88 66.95
REMARK 500 ASN B1218 -17.17 -140.67
REMARK 500 ALA C1010 -162.20 -78.01
REMARK 500 LYS C1155 -51.87 -24.22
REMARK 500 ASP C1285 56.92 -106.78
REMARK 500 ALA D1131 -2.72 75.90
REMARK 500 ARG D1203 120.47 -34.76
REMARK 500 ALA E1131 -1.08 77.49
REMARK 500 ASN E1140 -67.92 -28.00
REMARK 500 THR E1184 139.87 175.16
REMARK 500 CYS E1201 -133.20 58.70
REMARK 500 ALA F1131 -2.68 75.12
REMARK 500 LEU F1141 -1.37 79.70
REMARK 500 ARG F1203 107.45 -48.54
REMARK 500 GLU G 68 -151.97 -113.41
REMARK 500 SER G 82 77.00 -153.79
REMARK 500 GLU G 102 -42.67 -135.92
REMARK 500 LYS G 150 -122.30 39.22
REMARK 500 ASP G 154 86.89 35.84
REMARK 500 ASP I 52 -157.72 -83.13
REMARK 500 SER I 82 77.92 -152.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5NBQ A 994 1287 UNP P01024 CO3_HUMAN 994 1287
DBREF 5NBQ B 994 1287 UNP P01024 CO3_HUMAN 994 1287
DBREF 5NBQ C 994 1287 UNP P01024 CO3_HUMAN 994 1287
DBREF 5NBQ D 1104 1230 UNP P08603 CFAH_HUMAN 1104 1230
DBREF 5NBQ E 1104 1230 UNP P08603 CFAH_HUMAN 1104 1230
DBREF 5NBQ F 1104 1230 UNP P08603 CFAH_HUMAN 1104 1230
DBREF 5NBQ G 42 170 UNP Q45001 Q45001_BORBG 42 170
DBREF 5NBQ H -86 42 UNP Q45001 Q45001_BORBG 42 170
DBREF 5NBQ H 43 47 PDB 5NBQ 5NBQ 43 47
DBREF 5NBQ I 42 170 UNP Q45001 Q45001_BORBG 42 170
SEQADV 5NBQ ALA A 1010 UNP P01024 CYS 1010 ENGINEERED MUTATION
SEQADV 5NBQ ALA B 1010 UNP P01024 CYS 1010 ENGINEERED MUTATION
SEQADV 5NBQ ALA C 1010 UNP P01024 CYS 1010 ENGINEERED MUTATION
SEQRES 1 A 294 ALA VAL ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR
SEQRES 2 A 294 PRO SER GLY ALA GLY GLU GLN ASN MET ILE GLY MET THR
SEQRES 3 A 294 PRO THR VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU
SEQRES 4 A 294 GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA
SEQRES 5 A 294 LEU GLU LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA
SEQRES 6 A 294 PHE ARG GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS
SEQRES 7 A 294 ARG ALA PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS
SEQRES 8 A 294 VAL PHE SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER
SEQRES 9 A 294 GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU
SEQRES 10 A 294 LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO
SEQRES 11 A 294 VAL ILE HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN
SEQRES 12 A 294 ASN GLU LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE
SEQRES 13 A 294 SER LEU GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL
SEQRES 14 A 294 ASN SER LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE
SEQRES 15 A 294 LEU GLU ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR
SEQRES 16 A 294 VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG
SEQRES 17 A 294 LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA
SEQRES 18 A 294 LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU
SEQRES 19 A 294 TYR ASN VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU
SEQRES 20 A 294 LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL
SEQRES 21 A 294 ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR
SEQRES 22 A 294 GLY SER THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU
SEQRES 23 A 294 ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 B 294 ALA VAL ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR
SEQRES 2 B 294 PRO SER GLY ALA GLY GLU GLN ASN MET ILE GLY MET THR
SEQRES 3 B 294 PRO THR VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU
SEQRES 4 B 294 GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA
SEQRES 5 B 294 LEU GLU LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA
SEQRES 6 B 294 PHE ARG GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS
SEQRES 7 B 294 ARG ALA PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS
SEQRES 8 B 294 VAL PHE SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER
SEQRES 9 B 294 GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU
SEQRES 10 B 294 LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO
SEQRES 11 B 294 VAL ILE HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN
SEQRES 12 B 294 ASN GLU LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE
SEQRES 13 B 294 SER LEU GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL
SEQRES 14 B 294 ASN SER LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE
SEQRES 15 B 294 LEU GLU ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR
SEQRES 16 B 294 VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG
SEQRES 17 B 294 LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA
SEQRES 18 B 294 LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU
SEQRES 19 B 294 TYR ASN VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU
SEQRES 20 B 294 LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL
SEQRES 21 B 294 ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR
SEQRES 22 B 294 GLY SER THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU
SEQRES 23 B 294 ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 C 294 ALA VAL ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR
SEQRES 2 C 294 PRO SER GLY ALA GLY GLU GLN ASN MET ILE GLY MET THR
SEQRES 3 C 294 PRO THR VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU
SEQRES 4 C 294 GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA
SEQRES 5 C 294 LEU GLU LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA
SEQRES 6 C 294 PHE ARG GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS
SEQRES 7 C 294 ARG ALA PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS
SEQRES 8 C 294 VAL PHE SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER
SEQRES 9 C 294 GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU
SEQRES 10 C 294 LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO
SEQRES 11 C 294 VAL ILE HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN
SEQRES 12 C 294 ASN GLU LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE
SEQRES 13 C 294 SER LEU GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL
SEQRES 14 C 294 ASN SER LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE
SEQRES 15 C 294 LEU GLU ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR
SEQRES 16 C 294 VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG
SEQRES 17 C 294 LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA
SEQRES 18 C 294 LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU
SEQRES 19 C 294 TYR ASN VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU
SEQRES 20 C 294 LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL
SEQRES 21 C 294 ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR
SEQRES 22 C 294 GLY SER THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU
SEQRES 23 C 294 ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 D 127 ASP SER THR GLY LYS CYS GLY PRO PRO PRO PRO ILE ASP
SEQRES 2 D 127 ASN GLY ASP ILE THR SER PHE PRO LEU SER VAL TYR ALA
SEQRES 3 D 127 PRO ALA SER SER VAL GLU TYR GLN CYS GLN ASN LEU TYR
SEQRES 4 D 127 GLN LEU GLU GLY ASN LYS ARG ILE THR CYS ARG ASN GLY
SEQRES 5 D 127 GLN TRP SER GLU PRO PRO LYS CYS LEU HIS PRO CYS VAL
SEQRES 6 D 127 ILE SER ARG GLU ILE MET GLU ASN TYR ASN ILE ALA LEU
SEQRES 7 D 127 ARG TRP THR ALA LYS GLN LYS LEU TYR SER ARG THR GLY
SEQRES 8 D 127 GLU SER VAL GLU PHE VAL CYS LYS ARG GLY TYR ARG LEU
SEQRES 9 D 127 SER SER ARG SER HIS THR LEU ARG THR THR CYS TRP ASP
SEQRES 10 D 127 GLY LYS LEU GLU TYR PRO THR CYS ALA LYS
SEQRES 1 E 127 ASP SER THR GLY LYS CYS GLY PRO PRO PRO PRO ILE ASP
SEQRES 2 E 127 ASN GLY ASP ILE THR SER PHE PRO LEU SER VAL TYR ALA
SEQRES 3 E 127 PRO ALA SER SER VAL GLU TYR GLN CYS GLN ASN LEU TYR
SEQRES 4 E 127 GLN LEU GLU GLY ASN LYS ARG ILE THR CYS ARG ASN GLY
SEQRES 5 E 127 GLN TRP SER GLU PRO PRO LYS CYS LEU HIS PRO CYS VAL
SEQRES 6 E 127 ILE SER ARG GLU ILE MET GLU ASN TYR ASN ILE ALA LEU
SEQRES 7 E 127 ARG TRP THR ALA LYS GLN LYS LEU TYR SER ARG THR GLY
SEQRES 8 E 127 GLU SER VAL GLU PHE VAL CYS LYS ARG GLY TYR ARG LEU
SEQRES 9 E 127 SER SER ARG SER HIS THR LEU ARG THR THR CYS TRP ASP
SEQRES 10 E 127 GLY LYS LEU GLU TYR PRO THR CYS ALA LYS
SEQRES 1 F 127 ASP SER THR GLY LYS CYS GLY PRO PRO PRO PRO ILE ASP
SEQRES 2 F 127 ASN GLY ASP ILE THR SER PHE PRO LEU SER VAL TYR ALA
SEQRES 3 F 127 PRO ALA SER SER VAL GLU TYR GLN CYS GLN ASN LEU TYR
SEQRES 4 F 127 GLN LEU GLU GLY ASN LYS ARG ILE THR CYS ARG ASN GLY
SEQRES 5 F 127 GLN TRP SER GLU PRO PRO LYS CYS LEU HIS PRO CYS VAL
SEQRES 6 F 127 ILE SER ARG GLU ILE MET GLU ASN TYR ASN ILE ALA LEU
SEQRES 7 F 127 ARG TRP THR ALA LYS GLN LYS LEU TYR SER ARG THR GLY
SEQRES 8 F 127 GLU SER VAL GLU PHE VAL CYS LYS ARG GLY TYR ARG LEU
SEQRES 9 F 127 SER SER ARG SER HIS THR LEU ARG THR THR CYS TRP ASP
SEQRES 10 F 127 GLY LYS LEU GLU TYR PRO THR CYS ALA LYS
SEQRES 1 G 129 SER LYS PHE THR VAL LYS ILE LYS ASN LYS ASP LYS SER
SEQRES 2 G 129 GLY ASN TRP THR ASP LEU GLY ASP LEU VAL VAL ARG LYS
SEQRES 3 G 129 GLU GLU ASN GLY ILE ASP THR GLY LEU ASN ALA GLY GLY
SEQRES 4 G 129 HIS SER ALA THR PHE PHE SER LEU GLU GLU GLU VAL VAL
SEQRES 5 G 129 ASN ASN PHE VAL LYS VAL MET THR GLU GLY GLY SER PHE
SEQRES 6 G 129 LYS THR SER LEU TYR TYR GLY TYR LYS GLU GLU GLN SER
SEQRES 7 G 129 VAL ILE ASN GLY ILE GLN ASN LYS GLU ILE ILE THR LYS
SEQRES 8 G 129 ILE GLU LYS ILE ASP GLY THR GLU TYR ILE THR PHE SER
SEQRES 9 G 129 GLY ASP LYS ILE LYS ASN SER GLY ASP LYS VAL ALA GLU
SEQRES 10 G 129 TYR ALA ILE SER LEU GLU GLU LEU LYS LYS ASN LEU
SEQRES 1 H 134 SER LYS PHE THR VAL LYS ILE LYS ASN LYS ASP LYS SER
SEQRES 2 H 134 GLY ASN TRP THR ASP LEU GLY ASP LEU VAL VAL ARG LYS
SEQRES 3 H 134 GLU GLU ASN GLY ILE ASP THR GLY LEU ASN ALA GLY GLY
SEQRES 4 H 134 HIS SER ALA THR PHE PHE SER LEU GLU GLU GLU VAL VAL
SEQRES 5 H 134 ASN ASN PHE VAL LYS VAL MET THR GLU GLY GLY SER PHE
SEQRES 6 H 134 LYS THR SER LEU TYR TYR GLY TYR LYS GLU GLU GLN SER
SEQRES 7 H 134 VAL ILE ASN GLY ILE GLN ASN LYS GLU ILE ILE THR LYS
SEQRES 8 H 134 ILE GLU LYS ILE ASP GLY THR GLU TYR ILE THR PHE SER
SEQRES 9 H 134 GLY ASP LYS ILE LYS ASN SER GLY ASP LYS VAL ALA GLU
SEQRES 10 H 134 TYR ALA ILE SER LEU GLU GLU LEU LYS LYS ASN LEU UNK
SEQRES 11 H 134 UNK UNK UNK UNK
SEQRES 1 I 129 SER LYS PHE THR VAL LYS ILE LYS ASN LYS ASP LYS SER
SEQRES 2 I 129 GLY ASN TRP THR ASP LEU GLY ASP LEU VAL VAL ARG LYS
SEQRES 3 I 129 GLU GLU ASN GLY ILE ASP THR GLY LEU ASN ALA GLY GLY
SEQRES 4 I 129 HIS SER ALA THR PHE PHE SER LEU GLU GLU GLU VAL VAL
SEQRES 5 I 129 ASN ASN PHE VAL LYS VAL MET THR GLU GLY GLY SER PHE
SEQRES 6 I 129 LYS THR SER LEU TYR TYR GLY TYR LYS GLU GLU GLN SER
SEQRES 7 I 129 VAL ILE ASN GLY ILE GLN ASN LYS GLU ILE ILE THR LYS
SEQRES 8 I 129 ILE GLU LYS ILE ASP GLY THR GLU TYR ILE THR PHE SER
SEQRES 9 I 129 GLY ASP LYS ILE LYS ASN SER GLY ASP LYS VAL ALA GLU
SEQRES 10 I 129 TYR ALA ILE SER LEU GLU GLU LEU LYS LYS ASN LEU
FORMUL 10 HOH *2(H2 O)
HELIX 1 AA1 GLU A 998 ILE A 1004 5 7
HELIX 2 AA2 GLU A 1012 GLU A 1032 1 21
HELIX 3 AA3 LEU A 1039 ALA A 1058 1 20
HELIX 4 AA4 SER A 1075 VAL A 1090 1 16
HELIX 5 AA5 ASP A 1096 GLN A 1112 1 17
HELIX 6 AA6 HIS A 1126 ASN A 1135 5 10
HELIX 7 AA7 GLU A 1138 GLU A 1159 1 22
HELIX 8 AA8 SER A 1164 TYR A 1180 1 17
HELIX 9 AA9 ARG A 1185 MET A 1199 1 15
HELIX 10 AB1 LYS A 1203 ALA A 1214 1 12
HELIX 11 AB2 LYS A 1215 ASN A 1218 5 4
HELIX 12 AB3 LYS A 1225 LYS A 1244 1 20
HELIX 13 AB4 PHE A 1248 GLN A 1259 1 12
HELIX 14 AB5 SER A 1268 ASP A 1285 1 18
HELIX 15 AB6 ASP B 996 ILE B 1004 5 9
HELIX 16 AB7 GLU B 1012 GLU B 1032 1 21
HELIX 17 AB8 GLN B 1033 GLY B 1038 1 6
HELIX 18 AB9 LEU B 1039 ALA B 1058 1 20
HELIX 19 AC1 SER B 1075 VAL B 1090 1 16
HELIX 20 AC2 ASP B 1096 GLN B 1112 1 17
HELIX 21 AC3 HIS B 1126 ASN B 1135 5 10
HELIX 22 AC4 GLU B 1138 GLU B 1159 1 22
HELIX 23 AC5 SER B 1164 TYR B 1180 1 17
HELIX 24 AC6 ARG B 1185 MET B 1199 1 15
HELIX 25 AC7 LYS B 1203 ALA B 1214 1 12
HELIX 26 AC8 LYS B 1215 ASN B 1218 5 4
HELIX 27 AC9 LYS B 1225 LYS B 1244 1 20
HELIX 28 AD1 PHE B 1248 GLN B 1259 1 12
HELIX 29 AD2 SER B 1268 ASP B 1285 1 18
HELIX 30 AD3 ASP C 996 ILE C 1004 5 9
HELIX 31 AD4 GLU C 1012 THR C 1031 1 20
HELIX 32 AD5 GLN C 1033 GLY C 1038 1 6
HELIX 33 AD6 LEU C 1039 ALA C 1058 1 20
HELIX 34 AD7 SER C 1075 VAL C 1090 1 16
HELIX 35 AD8 ASP C 1096 GLN C 1112 1 17
HELIX 36 AD9 HIS C 1126 ASN C 1135 5 10
HELIX 37 AE1 GLU C 1138 GLU C 1159 1 22
HELIX 38 AE2 SER C 1164 TYR C 1180 1 17
HELIX 39 AE3 ARG C 1185 MET C 1199 1 15
HELIX 40 AE4 LYS C 1203 ALA C 1214 1 12
HELIX 41 AE5 LYS C 1215 ASN C 1218 5 4
HELIX 42 AE6 LYS C 1225 LYS C 1244 1 20
HELIX 43 AE7 PHE C 1248 GLN C 1259 1 12
HELIX 44 AE8 SER C 1268 ASP C 1285 1 18
HELIX 45 AE9 SER D 1170 TYR D 1177 1 8
HELIX 46 AF1 ARG D 1210 THR D 1213 5 4
HELIX 47 AF2 SER E 1170 TYR E 1177 1 8
HELIX 48 AF3 SER F 1170 TYR F 1177 1 8
HELIX 49 AF4 VAL G 92 GLY G 103 1 12
HELIX 50 AF5 LEU G 163 LEU G 170 1 8
HELIX 51 AF6 VAL I 92 GLY I 103 1 12
HELIX 52 AF7 LEU I 163 LEU I 170 1 8
SHEET 1 AA1 3 GLY D1118 ILE D1120 0
SHEET 2 AA1 3 SER D1133 CYS D1138 -1 O GLN D1137 N ASP D1119
SHEET 3 AA1 3 ARG D1149 THR D1151 -1 O ILE D1150 N VAL D1134
SHEET 1 AA2 2 GLN D1143 GLU D1145 0
SHEET 2 AA2 2 LYS D1162 LEU D1164 -1 O LEU D1164 N GLN D1143
SHEET 1 AA3 2 CYS D1167 ILE D1169 0
SHEET 2 AA3 2 LEU D1189 SER D1191 -1 O SER D1191 N CYS D1167
SHEET 1 AA4 3 ILE D1179 LEU D1181 0
SHEET 2 AA4 3 SER D1196 CYS D1201 -1 O VAL D1200 N ALA D1180
SHEET 3 AA4 3 ARG D1215 THR D1217 -1 O THR D1216 N VAL D1197
SHEET 1 AA5 2 ARG D1206 LEU D1207 0
SHEET 2 AA5 2 CYS D1228 ALA D1229 -1 O ALA D1229 N ARG D1206
SHEET 1 AA6 4 GLY E1118 ILE E1120 0
SHEET 2 AA6 4 SER E1133 CYS E1138 -1 O GLN E1137 N ASP E1119
SHEET 3 AA6 4 ARG E1149 ARG E1153 -1 O ILE E1150 N VAL E1134
SHEET 4 AA6 4 GLN E1156 TRP E1157 -1 O GLN E1156 N ARG E1153
SHEET 1 AA7 2 GLN E1143 GLU E1145 0
SHEET 2 AA7 2 LYS E1162 LEU E1164 -1 O LEU E1164 N GLN E1143
SHEET 1 AA8 2 CYS E1167 ILE E1169 0
SHEET 2 AA8 2 LEU E1189 SER E1191 -1 O SER E1191 N CYS E1167
SHEET 1 AA9 2 SER E1196 GLU E1198 0
SHEET 2 AA9 2 ARG E1215 THR E1217 -1 O THR E1216 N VAL E1197
SHEET 1 AB1 4 GLY F1118 ILE F1120 0
SHEET 2 AB1 4 SER F1133 CYS F1138 -1 O GLN F1137 N ASP F1119
SHEET 3 AB1 4 ARG F1149 ARG F1153 -1 O ILE F1150 N VAL F1134
SHEET 4 AB1 4 GLN F1156 TRP F1157 -1 O GLN F1156 N ARG F1153
SHEET 1 AB2 2 GLN F1143 GLU F1145 0
SHEET 2 AB2 2 LYS F1162 LEU F1164 -1 O LEU F1164 N GLN F1143
SHEET 1 AB3 2 CYS F1167 ILE F1169 0
SHEET 2 AB3 2 LEU F1189 SER F1191 -1 O SER F1191 N CYS F1167
SHEET 1 AB4 3 ILE F1179 LEU F1181 0
SHEET 2 AB4 3 SER F1196 CYS F1201 -1 O VAL F1200 N ALA F1180
SHEET 3 AB4 3 ARG F1215 THR F1217 -1 O THR F1216 N VAL F1197
SHEET 1 AB510 GLY G 104 LYS G 107 0
SHEET 2 AB510 GLU G 128 ILE G 136 -1 O THR G 131 N GLY G 104
SHEET 3 AB510 THR G 139 LYS G 148 -1 O TYR G 141 N GLU G 134
SHEET 4 AB510 VAL G 156 SER G 162 -1 O ALA G 157 N GLY G 146
SHEET 5 AB510 LYS G 43 LYS G 51 -1 N LYS G 51 O GLU G 158
SHEET 6 AB510 TRP G 57 LYS G 67 -1 O LEU G 63 N VAL G 46
SHEET 7 AB510 ILE G 72 ALA G 78 -1 O ASN G 77 N ASP G 62
SHEET 8 AB510 HIS G 81 SER G 87 -1 O ALA G 83 N LEU G 76
SHEET 9 AB510 LEU G 110 TYR G 111 -1 O LEU G 110 N SER G 87
SHEET 10 AB510 ILE G 124 GLN G 125 -1 O ILE G 124 N TYR G 111
SHEET 1 AB610 GLY I 104 LYS I 107 0
SHEET 2 AB610 GLU I 128 ILE I 136 -1 O THR I 131 N GLY I 104
SHEET 3 AB610 THR I 139 LYS I 148 -1 O TYR I 141 N GLU I 134
SHEET 4 AB610 VAL I 156 SER I 162 -1 O ILE I 161 N ILE I 142
SHEET 5 AB610 LYS I 43 LYS I 51 -1 N LYS I 49 O ALA I 160
SHEET 6 AB610 TRP I 57 LYS I 67 -1 O LEU I 63 N VAL I 46
SHEET 7 AB610 ILE I 72 ALA I 78 -1 O ASP I 73 N ARG I 66
SHEET 8 AB610 HIS I 81 SER I 87 -1 O PHE I 85 N THR I 74
SHEET 9 AB610 LEU I 110 TYR I 111 -1 O LEU I 110 N SER I 87
SHEET 10 AB610 ILE I 124 GLN I 125 -1 O ILE I 124 N TYR I 111
SSBOND 1 CYS A 1101 CYS A 1158 1555 1555 2.04
SSBOND 2 CYS B 1101 CYS B 1158 1555 1555 2.05
SSBOND 3 CYS C 1101 CYS C 1158 1555 1555 2.03
SSBOND 4 CYS D 1109 CYS D 1152 1555 1555 2.04
SSBOND 5 CYS D 1138 CYS D 1163 1555 1555 2.04
SSBOND 6 CYS D 1167 CYS D 1218 1555 1555 2.04
SSBOND 7 CYS D 1201 CYS D 1228 1555 1555 2.04
SSBOND 8 CYS E 1109 CYS E 1152 1555 1555 2.02
SSBOND 9 CYS E 1138 CYS E 1163 1555 1555 2.03
SSBOND 10 CYS E 1167 CYS E 1218 1555 1555 2.03
SSBOND 11 CYS E 1201 CYS E 1228 1555 1555 2.03
SSBOND 12 CYS F 1109 CYS F 1152 1555 1555 2.03
SSBOND 13 CYS F 1138 CYS F 1163 1555 1555 2.03
SSBOND 14 CYS F 1167 CYS F 1218 1555 1555 2.04
SSBOND 15 CYS F 1201 CYS F 1228 1555 1555 2.03
CRYST1 124.907 165.063 84.185 90.00 90.00 90.00 P 21 21 2 12
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 0.008006 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006058 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
