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HEADER HYDROLASE/IMMUNE SYSTEM 17-JUL-14 4QWW
TITLE CRYSTAL STRUCTURE OF THE FAB410-BFACHE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 32-566;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FAB410 ANTIBODY LIGHT CHAIN;
COMPND 9 CHAIN: C, E;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: FAB410 ANTIBODY HEAVY CHAIN;
COMPND 12 CHAIN: D, F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS FASCIATUS;
SOURCE 3 ORGANISM_COMMON: BANDED KRAIT;
SOURCE 4 ORGANISM_TAXID: 8613;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090
KEYWDS A/B HYDROLASE FOLD, ACETYLCHOLINESTERASE, MONOCLONAL ANTIBODY,
KEYWDS 2 HYDROLASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,L.RENAULT,P.MARCHOT
REVDAT 1 26-NOV-14 4QWW 0
JRNL AUTH Y.BOURNE,L.RENAULT,P.MARCHOT
JRNL TITL CRYSTAL STRUCTURE OF SNAKE VENOM ACETYLCHOLINESTERASE IN
JRNL TITL 2 COMPLEX WITH INHIBITORY ANTIBODY FRAGMENT FAB410 BOUND AT
JRNL TITL 3 THE PERIPHERAL SITE: EVIDENCE FOR OPEN AND CLOSED STATES OF
JRNL TITL 4 A BACKDOOR CHANNEL
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M114.603902
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 81030
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4060
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.77
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5828
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2284
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5549
REMARK 3 BIN R VALUE (WORKING SET) : 0.2255
REMARK 3 BIN FREE R VALUE : 0.2899
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.79
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 279
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 : 14968
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 286
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.52770
REMARK 3 B22 (A**2) : 8.35650
REMARK 3 B33 (A**2) : 4.17120
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) : 0.446
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.467
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.274
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.481
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.280
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 : 0.908
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 15762 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 21541 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5217 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 341 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2279 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 15762 ; 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 : 2073 ; 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 : 17497 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.28
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.44
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5658 -38.2139 -41.6353
REMARK 3 T TENSOR
REMARK 3 T11: 0.3040 T22: -0.2386
REMARK 3 T33: -0.3040 T12: -0.1520
REMARK 3 T13: -0.0913 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.5712 L22: 2.1399
REMARK 3 L33: 2.1269 L12: 1.0093
REMARK 3 L13: -0.6991 L23: -0.1754
REMARK 3 S TENSOR
REMARK 3 S11: -0.3173 S12: 0.3646 S13: 0.1847
REMARK 3 S21: -0.5442 S22: 0.2270 S23: 0.1192
REMARK 3 S31: 0.5442 S32: -0.4142 S33: 0.0903
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5199 -76.5538 4.4392
REMARK 3 T TENSOR
REMARK 3 T11: 0.3040 T22: -0.3040
REMARK 3 T33: -0.3040 T12: 0.0234
REMARK 3 T13: 0.0302 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.9917 L22: 2.8015
REMARK 3 L33: 2.0930 L12: -0.3273
REMARK 3 L13: -0.0640 L23: -0.0658
REMARK 3 S TENSOR
REMARK 3 S11: -0.2008 S12: -0.1359 S13: -0.1120
REMARK 3 S21: 0.5442 S22: 0.0924 S23: 0.0926
REMARK 3 S31: -0.4036 S32: -0.1573 S33: 0.1084
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|1 - C|109 D|1 - D|124 }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8640 -108.6390 -13.4954
REMARK 3 T TENSOR
REMARK 3 T11: -0.0589 T22: -0.1506
REMARK 3 T33: 0.0755 T12: -0.0116
REMARK 3 T13: 0.0472 T23: -0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 0.7830 L22: 2.0388
REMARK 3 L33: 1.8099 L12: -0.2834
REMARK 3 L13: 0.5314 L23: -0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: -0.0123 S13: -0.1401
REMARK 3 S21: 0.1007 S22: -0.0291 S23: 0.5233
REMARK 3 S31: 0.0604 S32: 0.0099 S33: -0.0030
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { C|110 - C|212 D|125 - D|225 }
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4936 -138.8200 -27.8907
REMARK 3 T TENSOR
REMARK 3 T11: -0.0716 T22: -0.1089
REMARK 3 T33: 0.1756 T12: -0.0607
REMARK 3 T13: 0.0328 T23: -0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 2.0413 L22: 2.0604
REMARK 3 L33: 1.5476 L12: -1.3644
REMARK 3 L13: 0.6588 L23: -0.2405
REMARK 3 S TENSOR
REMARK 3 S11: -0.1305 S12: 0.1648 S13: -0.3662
REMARK 3 S21: -0.0354 S22: 0.0143 S23: 0.4921
REMARK 3 S31: 0.0008 S32: -0.1780 S33: 0.1162
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { E|1 - E|109 F|1 - F|124 }
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5715 -5.9225 -23.8396
REMARK 3 T TENSOR
REMARK 3 T11: -0.1549 T22: -0.1465
REMARK 3 T33: 0.1152 T12: 0.0421
REMARK 3 T13: -0.0649 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 1.0068 L22: 2.1281
REMARK 3 L33: 2.1740 L12: 0.4264
REMARK 3 L13: -0.1021 L23: -0.1145
REMARK 3 S TENSOR
REMARK 3 S11: 0.0651 S12: -0.1063 S13: 0.2040
REMARK 3 S21: 0.0168 S22: 0.0056 S23: 0.5438
REMARK 3 S31: -0.2219 S32: -0.1477 S33: -0.0707
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { E|110 - E|211 F|125 - F|225 }
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1552 23.7530 -9.0584
REMARK 3 T TENSOR
REMARK 3 T11: 0.0566 T22: -0.2362
REMARK 3 T33: 0.0698 T12: 0.1520
REMARK 3 T13: -0.1520 T23: -0.1454
REMARK 3 L TENSOR
REMARK 3 L11: 1.8094 L22: 1.7354
REMARK 3 L33: 2.4134 L12: 0.6010
REMARK 3 L13: -0.1690 L23: 0.7077
REMARK 3 S TENSOR
REMARK 3 S11: -0.2087 S12: -0.1446 S13: 0.3593
REMARK 3 S21: -0.2294 S22: -0.0907 S23: 0.5442
REMARK 3 S31: -0.4157 S32: -0.2572 S33: 0.2994
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QWW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-14.
REMARK 100 THE RCSB ID CODE IS RCSB086615.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 78.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10500
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.59400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRIES 1J06 & 1IQW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.0-12.5% PEG8000, 0.2 M SODIUM
REMARK 280 CITRATE, PH 5.0, VAPOR DIFFUSION, 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 78.29600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 125.66800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 78.29600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 125.66800
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 ARG A 2
REMARK 465 ASP A 487
REMARK 465 LYS A 488
REMARK 465 SER A 489
REMARK 465 GLY A 490
REMARK 465 VAL A 536
REMARK 465 ASP A 537
REMARK 465 PRO A 538
REMARK 465 PRO A 539
REMARK 465 ARG A 540
REMARK 465 ALA A 541
REMARK 465 ASP A 542
REMARK 465 GLY B 1
REMARK 465 ARG B 2
REMARK 465 ASP B 487
REMARK 465 LYS B 488
REMARK 465 SER B 489
REMARK 465 GLY B 490
REMARK 465 VAL B 536
REMARK 465 ASP B 537
REMARK 465 PRO B 538
REMARK 465 PRO B 539
REMARK 465 ARG B 540
REMARK 465 ALA B 541
REMARK 465 ASP B 542
REMARK 465 CYS C 213
REMARK 465 ASP D 226
REMARK 465 CYS D 227
REMARK 465 GLY D 228
REMARK 465 CYS D 229
REMARK 465 LYS D 230
REMARK 465 PRO D 231
REMARK 465 CYS D 232
REMARK 465 ILE D 233
REMARK 465 CYS D 234
REMARK 465 CYS E 213
REMARK 465 SER F 140
REMARK 465 ALA F 141
REMARK 465 ALA F 142
REMARK 465 GLN F 143
REMARK 465 THR F 144
REMARK 465 ASN F 145
REMARK 465 ASP F 226
REMARK 465 CYS F 227
REMARK 465 GLY F 228
REMARK 465 CYS F 229
REMARK 465 LYS F 230
REMARK 465 PRO F 231
REMARK 465 CYS F 232
REMARK 465 ILE F 233
REMARK 465 CYS F 234
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 THR A 213 N - CA - C ANGL. DEV. = 17.3 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 GLN A 11 -19.61 -47.10
REMARK 500 LEU A 23 -121.40 50.08
REMARK 500 HIS A 56 -76.28 -107.89
REMARK 500 ALA A 60 51.57 -114.89
REMARK 500 LYS A 107 -60.55 -100.95
REMARK 500 PHE A 155 24.60 -143.30
REMARK 500 ALA A 164 74.88 -160.72
REMARK 500 MET A 168 -36.34 -36.54
REMARK 500 SER A 200 -115.87 55.95
REMARK 500 GLN A 214 41.61 -93.48
REMARK 500 SER A 215 21.25 -150.42
REMARK 500 ASP A 299 -67.25 -109.64
REMARK 500 ASP A 303 -167.23 -165.93
REMARK 500 VAL A 360 76.46 -110.49
REMARK 500 VAL A 400 -70.31 -121.16
REMARK 500 LYS A 413 27.89 -74.72
REMARK 500 ARG A 414 14.47 -152.21
REMARK 500 ASN A 415 19.09 59.02
REMARK 500 ASN A 457 75.31 51.67
REMARK 500 PRO A 482 9.19 -58.05
REMARK 500 PRO A 500 44.61 -85.90
REMARK 500 THR A 507 36.35 -83.24
REMARK 500 LEU A 510 116.69 -39.86
REMARK 500 LEU B 23 -121.31 47.64
REMARK 500 HIS B 56 -75.47 -107.78
REMARK 500 ALA B 60 52.69 -116.48
REMARK 500 LYS B 107 -61.27 -102.14
REMARK 500 ALA B 164 74.62 -160.44
REMARK 500 ALA B 193 63.57 -103.73
REMARK 500 SER B 200 -116.56 56.56
REMARK 500 GLN B 220 -61.71 -90.78
REMARK 500 ASP B 303 -167.90 -168.57
REMARK 500 ASP B 326 78.52 -119.01
REMARK 500 VAL B 360 76.00 -110.37
REMARK 500 ASP B 380 58.74 -141.39
REMARK 500 VAL B 400 -70.96 -120.35
REMARK 500 ASN B 457 75.71 51.32
REMARK 500 ASP B 484 -55.79 -136.38
REMARK 500 PRO B 500 40.45 -83.49
REMARK 500 ASN B 506 -169.77 -162.70
REMARK 500 THR B 507 36.68 -83.84
REMARK 500 LEU B 510 115.37 -38.90
REMARK 500 ARG C 49 63.03 38.12
REMARK 500 THR C 50 -53.46 76.39
REMARK 500 SER C 170 17.44 58.08
REMARK 500 ASN C 211 58.81 -97.56
REMARK 500 LYS D 15 -1.03 82.93
REMARK 500 VAL D 48 -60.87 -105.50
REMARK 500 ASN D 56 36.88 -95.00
REMARK 500 ASN D 87 53.91 38.89
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 THR A 213 23.9 L L OUTSIDE RANGE
REMARK 500 LYS D 67 24.4 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 343 RESIDUES 601 TO 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 453 RESIDUES 607 TO 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE
REMARK 800 RESIDUES 601 TO 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 612 BOUND
REMARK 800 TO ASN B 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B
REMARK 800 343 RESIDUES 601 TO 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B
REMARK 800 453 RESIDUES 607 TO 611
DBREF 4QWW A 1 535 UNP Q92035 ACES_BUNFA 32 566
DBREF 4QWW B 1 535 UNP Q92035 ACES_BUNFA 32 566
DBREF 4QWW A 1 542 PDB 4QWW 4QWW 1 542
DBREF 4QWW B 1 542 PDB 4QWW 4QWW 1 542
DBREF 4QWW C 1 213 PDB 4QWW 4QWW 1 213
DBREF 4QWW E 1 213 PDB 4QWW 4QWW 1 213
DBREF 4QWW D 1 234 PDB 4QWW 4QWW 1 234
DBREF 4QWW F 1 234 PDB 4QWW 4QWW 1 234
SEQRES 1 A 542 GLY ARG ALA GLY GLU LEU LYS VAL SER THR GLN THR GLY
SEQRES 2 A 542 SER VAL ARG GLY LEU SER LEU PRO VAL LEU ASP GLY HIS
SEQRES 3 A 542 VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 542 LEU GLY ARG MET ARG PHE LEU ARG PRO GLU PRO VAL LYS
SEQRES 5 A 542 PRO TRP GLN HIS VAL LEU ASP ALA THR SER TYR LYS PRO
SEQRES 6 A 542 ALA CYS TYR GLN MET VAL ASP THR SER TYR PRO GLY PHE
SEQRES 7 A 542 GLN GLY THR GLU MET TRP ASN PRO ASN ARG GLY MET SER
SEQRES 8 A 542 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 542 ARG PRO LYS ASP ALA PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 A 542 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 A 542 ASP GLY ARG PHE LEU THR TYR THR GLN ASN VAL ILE LEU
SEQRES 12 A 542 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 542 GLY LEU PRO GLY SER PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 14 A 542 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP ILE GLN ASN
SEQRES 15 A 542 ASN ILE HIS PRO PHE GLY GLY ASN PRO ARG ALA VAL THR
SEQRES 16 A 542 VAL PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 A 542 HIS LEU LEU SER THR GLN SER ARG THR LEU PHE GLN ARG
SEQRES 18 A 542 ALA ILE LEU GLN SER GLY GLY PRO ASN ALA PRO TRP ALA
SEQRES 19 A 542 THR VAL THR PRO ALA GLU SER ARG GLY ARG ALA ALA LEU
SEQRES 20 A 542 LEU GLY LYS GLN LEU GLY CYS HIS PHE ASN ASN ASP SER
SEQRES 21 A 542 GLU LEU VAL SER CYS LEU ARG SER LYS ASN PRO GLN GLU
SEQRES 22 A 542 LEU ILE ASP GLU GLU TRP SER VAL LEU PRO TYR LYS SER
SEQRES 23 A 542 ILE PHE ARG PHE PRO PHE VAL PRO VAL ILE ASP GLY ASP
SEQRES 24 A 542 PHE PHE PRO ASP THR PRO GLU ALA MET LEU SER SER GLY
SEQRES 25 A 542 ASN PHE LYS GLU THR GLN VAL LEU LEU GLY VAL VAL LYS
SEQRES 26 A 542 ASP GLU GLY SER TYR PHE LEU ILE TYR GLY LEU PRO GLY
SEQRES 27 A 542 PHE SER LYS ASP ASN GLU SER LEU ILE SER ARG ALA ASP
SEQRES 28 A 542 PHE LEU GLU GLY VAL ARG MET SER VAL PRO HIS ALA ASN
SEQRES 29 A 542 ASP ILE ALA THR ASP ALA VAL VAL LEU GLN TYR THR ASP
SEQRES 30 A 542 TRP GLN ASP GLN ASP ASN ARG GLU LYS ASN ARG GLU ALA
SEQRES 31 A 542 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 542 VAL VAL GLN PHE ALA ASN ASP TYR ALA LYS ARG ASN SER
SEQRES 33 A 542 LYS VAL TYR ALA TYR LEU PHE ASP HIS ARG ALA SER ASN
SEQRES 34 A 542 LEU LEU TRP PRO PRO TRP MET GLY VAL PRO HIS GLY TYR
SEQRES 35 A 542 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU ASN ASP SER
SEQRES 36 A 542 LEU ASN TYR THR PRO GLN GLU LYS GLU LEU SER ARG ARG
SEQRES 37 A 542 MET MET ARG TYR TRP ALA ASN PHE ALA ARG THR GLY ASN
SEQRES 38 A 542 PRO THR ASP PRO ALA ASP LYS SER GLY ALA TRP PRO THR
SEQRES 39 A 542 TYR THR ALA SER GLN PRO GLN TYR VAL GLN LEU ASN THR
SEQRES 40 A 542 GLN PRO LEU ALA THR GLN PRO SER LEU ARG ALA GLN ILE
SEQRES 41 A 542 CYS ALA PHE TRP ASN HIS PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 542 ALA THR VAL ASP PRO PRO ARG ALA ASP
SEQRES 1 B 542 GLY ARG ALA GLY GLU LEU LYS VAL SER THR GLN THR GLY
SEQRES 2 B 542 SER VAL ARG GLY LEU SER LEU PRO VAL LEU ASP GLY HIS
SEQRES 3 B 542 VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 542 LEU GLY ARG MET ARG PHE LEU ARG PRO GLU PRO VAL LYS
SEQRES 5 B 542 PRO TRP GLN HIS VAL LEU ASP ALA THR SER TYR LYS PRO
SEQRES 6 B 542 ALA CYS TYR GLN MET VAL ASP THR SER TYR PRO GLY PHE
SEQRES 7 B 542 GLN GLY THR GLU MET TRP ASN PRO ASN ARG GLY MET SER
SEQRES 8 B 542 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 542 ARG PRO LYS ASP ALA PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 B 542 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 B 542 ASP GLY ARG PHE LEU THR TYR THR GLN ASN VAL ILE LEU
SEQRES 12 B 542 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 542 GLY LEU PRO GLY SER PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 14 B 542 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP ILE GLN ASN
SEQRES 15 B 542 ASN ILE HIS PRO PHE GLY GLY ASN PRO ARG ALA VAL THR
SEQRES 16 B 542 VAL PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 B 542 HIS LEU LEU SER THR GLN SER ARG THR LEU PHE GLN ARG
SEQRES 18 B 542 ALA ILE LEU GLN SER GLY GLY PRO ASN ALA PRO TRP ALA
SEQRES 19 B 542 THR VAL THR PRO ALA GLU SER ARG GLY ARG ALA ALA LEU
SEQRES 20 B 542 LEU GLY LYS GLN LEU GLY CYS HIS PHE ASN ASN ASP SER
SEQRES 21 B 542 GLU LEU VAL SER CYS LEU ARG SER LYS ASN PRO GLN GLU
SEQRES 22 B 542 LEU ILE ASP GLU GLU TRP SER VAL LEU PRO TYR LYS SER
SEQRES 23 B 542 ILE PHE ARG PHE PRO PHE VAL PRO VAL ILE ASP GLY ASP
SEQRES 24 B 542 PHE PHE PRO ASP THR PRO GLU ALA MET LEU SER SER GLY
SEQRES 25 B 542 ASN PHE LYS GLU THR GLN VAL LEU LEU GLY VAL VAL LYS
SEQRES 26 B 542 ASP GLU GLY SER TYR PHE LEU ILE TYR GLY LEU PRO GLY
SEQRES 27 B 542 PHE SER LYS ASP ASN GLU SER LEU ILE SER ARG ALA ASP
SEQRES 28 B 542 PHE LEU GLU GLY VAL ARG MET SER VAL PRO HIS ALA ASN
SEQRES 29 B 542 ASP ILE ALA THR ASP ALA VAL VAL LEU GLN TYR THR ASP
SEQRES 30 B 542 TRP GLN ASP GLN ASP ASN ARG GLU LYS ASN ARG GLU ALA
SEQRES 31 B 542 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 542 VAL VAL GLN PHE ALA ASN ASP TYR ALA LYS ARG ASN SER
SEQRES 33 B 542 LYS VAL TYR ALA TYR LEU PHE ASP HIS ARG ALA SER ASN
SEQRES 34 B 542 LEU LEU TRP PRO PRO TRP MET GLY VAL PRO HIS GLY TYR
SEQRES 35 B 542 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU ASN ASP SER
SEQRES 36 B 542 LEU ASN TYR THR PRO GLN GLU LYS GLU LEU SER ARG ARG
SEQRES 37 B 542 MET MET ARG TYR TRP ALA ASN PHE ALA ARG THR GLY ASN
SEQRES 38 B 542 PRO THR ASP PRO ALA ASP LYS SER GLY ALA TRP PRO THR
SEQRES 39 B 542 TYR THR ALA SER GLN PRO GLN TYR VAL GLN LEU ASN THR
SEQRES 40 B 542 GLN PRO LEU ALA THR GLN PRO SER LEU ARG ALA GLN ILE
SEQRES 41 B 542 CYS ALA PHE TRP ASN HIS PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 542 ALA THR VAL ASP PRO PRO ARG ALA ASP
SEQRES 1 C 213 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 C 213 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER
SEQRES 3 C 213 SER SER VAL SER TYR MET TYR TRP TYR HIS GLN LYS PRO
SEQRES 4 C 213 GLY SER SER PRO LYS PRO TRP ILE TYR ARG THR SER ASN
SEQRES 5 C 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY
SEQRES 6 C 213 SER GLY THR SER TYR SER LEU SER VAL SER SER VAL GLU
SEQRES 7 C 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TYR ASN
SEQRES 8 C 213 SER HIS PRO MET THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 C 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 C 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 C 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 C 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 C 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 C 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 C 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 C 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 C 213 ASN ARG ASN GLU CYS
SEQRES 1 D 234 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 D 234 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY
SEQRES 3 D 234 PHE THR PHE ASN THR TYR ALA MET HIS TRP VAL ARG GLN
SEQRES 4 D 234 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG
SEQRES 5 D 234 SER LYS SER ASN LYS TYR ALA THR HIS TYR ALA ASP SER
SEQRES 6 D 234 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN
SEQRES 7 D 234 THR MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU
SEQRES 8 D 234 ASP THR ALA MET TYR TYR CYS VAL ARG GLU GLY SER TYR
SEQRES 9 D 234 TYR ASP SER SER TYR GLY ALA MET ASP TYR TRP GLY GLN
SEQRES 10 D 234 GLY THR SER VAL THR VAL SER SER ALA LYS THR THR PRO
SEQRES 11 D 234 PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN
SEQRES 12 D 234 THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY
SEQRES 13 D 234 TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY
SEQRES 14 D 234 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU
SEQRES 15 D 234 GLU SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL
SEQRES 16 D 234 PRO SER SER PRO TRP PRO SER GLU THR VAL THR CYS ASN
SEQRES 17 D 234 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS
SEQRES 18 D 234 ILE VAL PRO ARG ASP CYS GLY CYS LYS PRO CYS ILE CYS
SEQRES 1 E 213 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 E 213 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER
SEQRES 3 E 213 SER SER VAL SER TYR MET TYR TRP TYR HIS GLN LYS PRO
SEQRES 4 E 213 GLY SER SER PRO LYS PRO TRP ILE TYR ARG THR SER ASN
SEQRES 5 E 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY
SEQRES 6 E 213 SER GLY THR SER TYR SER LEU SER VAL SER SER VAL GLU
SEQRES 7 E 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TYR ASN
SEQRES 8 E 213 SER HIS PRO MET THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 E 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 E 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 E 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 E 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 E 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 E 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 E 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 E 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 E 213 ASN ARG ASN GLU CYS
SEQRES 1 F 234 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 F 234 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY
SEQRES 3 F 234 PHE THR PHE ASN THR TYR ALA MET HIS TRP VAL ARG GLN
SEQRES 4 F 234 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG
SEQRES 5 F 234 SER LYS SER ASN LYS TYR ALA THR HIS TYR ALA ASP SER
SEQRES 6 F 234 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN
SEQRES 7 F 234 THR MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU
SEQRES 8 F 234 ASP THR ALA MET TYR TYR CYS VAL ARG GLU GLY SER TYR
SEQRES 9 F 234 TYR ASP SER SER TYR GLY ALA MET ASP TYR TRP GLY GLN
SEQRES 10 F 234 GLY THR SER VAL THR VAL SER SER ALA LYS THR THR PRO
SEQRES 11 F 234 PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN
SEQRES 12 F 234 THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY
SEQRES 13 F 234 TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY
SEQRES 14 F 234 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU
SEQRES 15 F 234 GLU SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL
SEQRES 16 F 234 PRO SER SER PRO TRP PRO SER GLU THR VAL THR CYS ASN
SEQRES 17 F 234 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS
SEQRES 18 F 234 ILE VAL PRO ARG ASP CYS GLY CYS LYS PRO CYS ILE CYS
MODRES 4QWW ASN A 453 ASN GLYCOSYLATION SITE
MODRES 4QWW ASN B 453 ASN GLYCOSYLATION SITE
MODRES 4QWW ASN A 343 ASN GLYCOSYLATION SITE
MODRES 4QWW ASN B 258 ASN GLYCOSYLATION SITE
MODRES 4QWW ASN B 343 ASN GLYCOSYLATION SITE
HET NAG A 601 14
HET MAN A 602 11
HET BMA A 603 11
HET MAN A 604 11
HET NAG A 605 14
HET FUC A 606 10
HET NAG A 607 14
HET NAG A 608 14
HET MAN A 609 11
HET BMA A 610 11
HET MAN A 611 11
HET EDO A 612 4
HET NAG B 601 14
HET NAG B 602 14
HET FUC B 603 10
HET MAN B 604 11
HET BMA B 605 11
HET MAN B 606 11
HET NAG B 607 14
HET NAG B 608 14
HET MAN B 609 11
HET BMA B 610 11
HET MAN B 611 11
HET NAG B 612 14
HET EDO B 613 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BMA BETA-D-MANNOSE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 NAG 9(C8 H15 N O6)
FORMUL 7 MAN 8(C6 H12 O6)
FORMUL 7 BMA 4(C6 H12 O6)
FORMUL 7 FUC 2(C6 H12 O5)
FORMUL 9 EDO 2(C2 H6 O2)
FORMUL 14 HOH *228(H2 O)
HELIX 1 1 LEU A 40 ARG A 44 5 5
HELIX 2 2 PHE A 78 MET A 83 1 6
HELIX 3 3 LEU A 127 ASP A 131 5 5
HELIX 4 4 GLY A 132 ASN A 140 1 9
HELIX 5 5 GLY A 151 LEU A 156 1 6
HELIX 6 6 ASN A 167 ILE A 184 1 18
HELIX 7 7 HIS A 185 PHE A 187 5 3
HELIX 8 8 SER A 200 SER A 212 1 13
HELIX 9 9 THR A 237 LEU A 252 1 16
HELIX 10 10 ASP A 259 LYS A 269 1 11
HELIX 11 11 ASN A 270 TRP A 279 1 10
HELIX 12 12 SER A 280 LEU A 282 5 3
HELIX 13 13 THR A 304 GLY A 312 1 9
HELIX 14 14 GLY A 328 ILE A 333 1 6
HELIX 15 15 SER A 348 VAL A 360 1 13
HELIX 16 16 ASN A 364 TYR A 375 1 12
HELIX 17 17 ASN A 383 VAL A 400 1 18
HELIX 18 18 VAL A 400 LYS A 413 1 14
HELIX 19 19 PRO A 433 GLY A 437 5 5
HELIX 20 20 GLU A 443 PHE A 448 1 6
HELIX 21 21 GLY A 449 ASN A 457 5 9
HELIX 22 22 THR A 459 THR A 479 1 21
HELIX 23 23 ARG A 517 HIS A 526 1 10
HELIX 24 24 HIS A 526 THR A 535 1 10
HELIX 25 25 LEU B 40 ARG B 44 5 5
HELIX 26 26 PHE B 78 MET B 83 1 6
HELIX 27 27 LEU B 127 ASP B 131 5 5
HELIX 28 28 GLY B 132 GLN B 139 1 8
HELIX 29 29 VAL B 150 LEU B 156 1 7
HELIX 30 30 ASN B 167 ILE B 184 1 18
HELIX 31 31 HIS B 185 PHE B 187 5 3
HELIX 32 32 SER B 200 SER B 212 1 13
HELIX 33 33 SER B 212 THR B 217 1 6
HELIX 34 34 THR B 237 LEU B 252 1 16
HELIX 35 35 ASN B 258 LYS B 269 1 12
HELIX 36 36 ASN B 270 TRP B 279 1 10
HELIX 37 37 SER B 280 LEU B 282 5 3
HELIX 38 38 THR B 304 GLY B 312 1 9
HELIX 39 39 GLY B 328 ILE B 333 1 6
HELIX 40 40 SER B 348 VAL B 360 1 13
HELIX 41 41 ASN B 364 TYR B 375 1 12
HELIX 42 42 ASN B 383 VAL B 400 1 18
HELIX 43 43 VAL B 400 LYS B 413 1 14
HELIX 44 44 PRO B 433 GLY B 437 5 5
HELIX 45 45 GLU B 443 PHE B 448 1 6
HELIX 46 46 GLY B 449 ASN B 457 5 9
HELIX 47 47 THR B 459 THR B 479 1 21
HELIX 48 48 ARG B 517 HIS B 526 1 10
HELIX 49 49 HIS B 526 THR B 535 1 10
HELIX 50 50 GLU C 78 ALA C 82 5 5
HELIX 51 51 SER C 120 SER C 126 1 7
HELIX 52 52 LYS C 182 GLU C 186 1 5
HELIX 53 53 THR D 28 TYR D 32 5 5
HELIX 54 54 ASP D 64 LYS D 67 5 4
HELIX 55 55 LYS D 89 THR D 93 5 5
HELIX 56 56 SER D 168 SER D 170 5 3
HELIX 57 57 PRO D 212 SER D 215 5 4
HELIX 58 58 GLU E 78 ALA E 82 5 5
HELIX 59 59 SER E 120 SER E 126 1 7
HELIX 60 60 LYS E 182 GLU E 186 1 5
HELIX 61 61 THR F 28 TYR F 32 5 5
HELIX 62 62 ASP F 64 LYS F 67 5 4
HELIX 63 63 LYS F 89 THR F 93 5 5
HELIX 64 64 SER F 168 SER F 170 5 3
HELIX 65 65 PRO F 212 SER F 215 5 4
SHEET 1 A 3 LYS A 7 THR A 10 0
SHEET 2 A 3 GLY A 13 ARG A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 A 3 VAL A 57 ASP A 59 1 O LEU A 58 N ARG A 16
SHEET 1 B11 LEU A 18 VAL A 22 0
SHEET 2 B11 GLY A 25 PRO A 34 -1 O ALA A 29 N LEU A 18
SHEET 3 B11 TYR A 96 PRO A 102 -1 O VAL A 101 N SER A 28
SHEET 4 B11 ILE A 142 SER A 145 -1 O SER A 145 N ASN A 98
SHEET 5 B11 ALA A 109 ILE A 115 1 N PRO A 110 O ILE A 142
SHEET 6 B11 GLY A 189 GLU A 199 1 O PHE A 197 N VAL A 113
SHEET 7 B11 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 B11 VAL A 319 VAL A 324 1 O LEU A 320 N LEU A 224
SHEET 9 B11 VAL A 418 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 B11 TYR A 502 LEU A 505 1 O LEU A 505 N LEU A 422
SHEET 11 B11 ALA A 511 GLN A 513 -1 O GLN A 513 N TYR A 502
SHEET 1 C 2 ALA A 66 CYS A 67 0
SHEET 2 C 2 MET A 90 SER A 91 1 O SER A 91 N ALA A 66
SHEET 1 D 3 LYS B 7 THR B 10 0
SHEET 2 D 3 GLY B 13 ARG B 16 -1 O GLY B 13 N THR B 10
SHEET 3 D 3 VAL B 57 ASP B 59 1 O LEU B 58 N ARG B 16
SHEET 1 E11 LEU B 18 VAL B 22 0
SHEET 2 E11 GLY B 25 PRO B 34 -1 O VAL B 27 N LEU B 20
SHEET 3 E11 TYR B 96 PRO B 102 -1 O VAL B 101 N SER B 28
SHEET 4 E11 ILE B 142 SER B 145 -1 O LEU B 143 N TRP B 100
SHEET 5 E11 ALA B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 E11 GLY B 189 GLU B 199 1 O PHE B 197 N ILE B 115
SHEET 7 E11 ARG B 221 GLN B 225 1 O GLN B 225 N GLY B 198
SHEET 8 E11 VAL B 319 VAL B 324 1 O LEU B 320 N LEU B 224
SHEET 9 E11 VAL B 418 PHE B 423 1 O TYR B 419 N LEU B 321
SHEET 10 E11 TYR B 502 LEU B 505 1 O LEU B 505 N LEU B 422
SHEET 11 E11 ALA B 511 GLN B 513 -1 O GLN B 513 N TYR B 502
SHEET 1 F 2 ALA B 66 CYS B 67 0
SHEET 2 F 2 MET B 90 SER B 91 1 O SER B 91 N ALA B 66
SHEET 1 G 4 LEU C 4 SER C 7 0
SHEET 2 G 4 VAL C 19 ALA C 25 -1 O SER C 24 N THR C 5
SHEET 3 G 4 SER C 69 VAL C 74 -1 O TYR C 70 N CYS C 23
SHEET 4 G 4 PHE C 61 SER C 66 -1 N SER C 62 O SER C 73
SHEET 1 H 6 ILE C 10 ALA C 13 0
SHEET 2 H 6 THR C 101 ILE C 105 1 O LYS C 102 N MET C 11
SHEET 3 H 6 ALA C 83 GLN C 89 -1 N ALA C 83 O LEU C 103
SHEET 4 H 6 TYR C 33 GLN C 37 -1 N TYR C 33 O GLN C 88
SHEET 5 H 6 LYS C 44 TYR C 48 -1 O TRP C 46 N TRP C 34
SHEET 6 H 6 ASN C 52 LEU C 53 -1 O ASN C 52 N TYR C 48
SHEET 1 I 4 ILE C 10 ALA C 13 0
SHEET 2 I 4 THR C 101 ILE C 105 1 O LYS C 102 N MET C 11
SHEET 3 I 4 ALA C 83 GLN C 89 -1 N ALA C 83 O LEU C 103
SHEET 4 I 4 THR C 96 PHE C 97 -1 O THR C 96 N GLN C 89
SHEET 1 J 4 THR C 113 PHE C 117 0
SHEET 2 J 4 GLY C 128 PHE C 138 -1 O ASN C 136 N THR C 113
SHEET 3 J 4 TYR C 172 THR C 181 -1 O TYR C 172 N PHE C 138
SHEET 4 J 4 VAL C 158 TRP C 162 -1 N SER C 161 O SER C 175
SHEET 1 K 4 SER C 152 ARG C 154 0
SHEET 2 K 4 ILE C 143 ILE C 149 -1 N ILE C 149 O SER C 152
SHEET 3 K 4 SER C 190 HIS C 197 -1 O GLU C 194 N LYS C 146
SHEET 4 K 4 ILE C 204 ASN C 209 -1 O ILE C 204 N ALA C 195
SHEET 1 L 4 GLN D 3 SER D 7 0
SHEET 2 L 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7
SHEET 3 L 4 MET D 80 MET D 85 -1 O MET D 85 N LEU D 18
SHEET 4 L 4 PHE D 70 ASP D 75 -1 N SER D 73 O TYR D 82
SHEET 1 M 6 LEU D 11 VAL D 12 0
SHEET 2 M 6 THR D 119 VAL D 123 1 O THR D 122 N VAL D 12
SHEET 3 M 6 ALA D 94 GLU D 101 -1 N ALA D 94 O VAL D 121
SHEET 4 M 6 ALA D 33 GLN D 39 -1 N VAL D 37 O TYR D 97
SHEET 5 M 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38
SHEET 6 M 6 THR D 60 TYR D 62 -1 O HIS D 61 N ARG D 50
SHEET 1 N 4 LEU D 11 VAL D 12 0
SHEET 2 N 4 THR D 119 VAL D 123 1 O THR D 122 N VAL D 12
SHEET 3 N 4 ALA D 94 GLU D 101 -1 N ALA D 94 O VAL D 121
SHEET 4 N 4 MET D 112 TRP D 115 -1 O TYR D 114 N ARG D 100
SHEET 1 O 4 SER D 132 LEU D 136 0
SHEET 2 O 4 MET D 147 TYR D 157 -1 O LEU D 153 N TYR D 134
SHEET 3 O 4 TYR D 187 PRO D 196 -1 O VAL D 193 N LEU D 150
SHEET 4 O 4 VAL D 175 THR D 177 -1 N HIS D 176 O SER D 192
SHEET 1 P 4 SER D 132 LEU D 136 0
SHEET 2 P 4 MET D 147 TYR D 157 -1 O LEU D 153 N TYR D 134
SHEET 3 P 4 TYR D 187 PRO D 196 -1 O VAL D 193 N LEU D 150
SHEET 4 P 4 VAL D 181 LEU D 182 -1 N VAL D 181 O THR D 188
SHEET 1 Q 3 THR D 163 TRP D 166 0
SHEET 2 Q 3 THR D 206 HIS D 211 -1 O ALA D 210 N THR D 163
SHEET 3 Q 3 THR D 216 LYS D 221 -1 O VAL D 218 N VAL D 209
SHEET 1 R 4 LEU E 4 SER E 7 0
SHEET 2 R 4 VAL E 19 ALA E 25 -1 O SER E 24 N THR E 5
SHEET 3 R 4 SER E 69 VAL E 74 -1 O TYR E 70 N CYS E 23
SHEET 4 R 4 PHE E 61 SER E 66 -1 N SER E 62 O SER E 73
SHEET 1 S 6 ILE E 10 ALA E 13 0
SHEET 2 S 6 THR E 101 ILE E 105 1 O LYS E 102 N MET E 11
SHEET 3 S 6 ALA E 83 GLN E 89 -1 N ALA E 83 O LEU E 103
SHEET 4 S 6 TYR E 33 GLN E 37 -1 N TYR E 33 O GLN E 88
SHEET 5 S 6 LYS E 44 TYR E 48 -1 O TRP E 46 N TRP E 34
SHEET 6 S 6 ASN E 52 LEU E 53 -1 O ASN E 52 N TYR E 48
SHEET 1 T 4 ILE E 10 ALA E 13 0
SHEET 2 T 4 THR E 101 ILE E 105 1 O LYS E 102 N MET E 11
SHEET 3 T 4 ALA E 83 GLN E 89 -1 N ALA E 83 O LEU E 103
SHEET 4 T 4 THR E 96 PHE E 97 -1 O THR E 96 N GLN E 89
SHEET 1 U 4 THR E 113 PHE E 117 0
SHEET 2 U 4 GLY E 128 PHE E 138 -1 O ASN E 136 N THR E 113
SHEET 3 U 4 TYR E 172 THR E 181 -1 O LEU E 178 N VAL E 131
SHEET 4 U 4 VAL E 158 TRP E 162 -1 N SER E 161 O SER E 175
SHEET 1 V 4 SER E 152 ARG E 154 0
SHEET 2 V 4 ILE E 143 ILE E 149 -1 N ILE E 149 O SER E 152
SHEET 3 V 4 SER E 190 HIS E 197 -1 O GLU E 194 N LYS E 146
SHEET 4 V 4 ILE E 204 ASN E 209 -1 O ILE E 204 N ALA E 195
SHEET 1 W 4 GLN F 3 SER F 7 0
SHEET 2 W 4 LEU F 18 SER F 25 -1 O SER F 21 N SER F 7
SHEET 3 W 4 MET F 80 MET F 85 -1 O MET F 85 N LEU F 18
SHEET 4 W 4 PHE F 70 ASP F 75 -1 N ASP F 75 O MET F 80
SHEET 1 X 6 LEU F 11 VAL F 12 0
SHEET 2 X 6 THR F 119 VAL F 123 1 O THR F 122 N VAL F 12
SHEET 3 X 6 ALA F 94 GLU F 101 -1 N ALA F 94 O VAL F 121
SHEET 4 X 6 ALA F 33 GLN F 39 -1 N VAL F 37 O TYR F 97
SHEET 5 X 6 GLU F 46 ILE F 51 -1 O GLU F 46 N ARG F 38
SHEET 6 X 6 THR F 60 TYR F 62 -1 O HIS F 61 N ARG F 50
SHEET 1 Y 4 LEU F 11 VAL F 12 0
SHEET 2 Y 4 THR F 119 VAL F 123 1 O THR F 122 N VAL F 12
SHEET 3 Y 4 ALA F 94 GLU F 101 -1 N ALA F 94 O VAL F 121
SHEET 4 Y 4 MET F 112 TRP F 115 -1 O TYR F 114 N ARG F 100
SHEET 1 Z 4 SER F 132 LEU F 136 0
SHEET 2 Z 4 MET F 147 TYR F 157 -1 O LEU F 153 N TYR F 134
SHEET 3 Z 4 TYR F 187 PRO F 196 -1 O VAL F 193 N LEU F 150
SHEET 4 Z 4 VAL F 175 THR F 177 -1 N HIS F 176 O SER F 192
SHEET 1 AA 4 SER F 132 LEU F 136 0
SHEET 2 AA 4 MET F 147 TYR F 157 -1 O LEU F 153 N TYR F 134
SHEET 3 AA 4 TYR F 187 PRO F 196 -1 O VAL F 193 N LEU F 150
SHEET 4 AA 4 VAL F 181 LEU F 182 -1 N VAL F 181 O THR F 188
SHEET 1 AB 3 THR F 163 TRP F 166 0
SHEET 2 AB 3 THR F 206 HIS F 211 -1 O ALA F 210 N THR F 163
SHEET 3 AB 3 THR F 216 LYS F 221 -1 O VAL F 218 N VAL F 209
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.04
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.04
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.05
SSBOND 7 CYS C 23 CYS C 87 1555 1555 2.08
SSBOND 8 CYS C 133 CYS C 193 1555 1555 2.02
SSBOND 9 CYS D 22 CYS D 98 1555 1555 2.05
SSBOND 10 CYS D 152 CYS D 207 1555 1555 2.04
SSBOND 11 CYS E 23 CYS E 87 1555 1555 2.08
SSBOND 12 CYS E 133 CYS E 193 1555 1555 2.02
SSBOND 13 CYS F 22 CYS F 98 1555 1555 2.04
SSBOND 14 CYS F 152 CYS F 207 1555 1555 2.05
LINK O6 NAG B 602 C1 FUC B 603 1555 1555 1.39
LINK O6 NAG A 605 C1 FUC A 606 1555 1555 1.39
LINK O4 NAG B 607 C1 BMA B 610 1555 1555 1.40
LINK O4 NAG A 601 C1 BMA A 603 1555 1555 1.40
LINK C1 NAG B 601 O4 NAG B 602 1555 1555 1.41
LINK O4 NAG A 607 C1 BMA A 610 1555 1555 1.41
LINK O4 NAG B 601 C1 BMA B 605 1555 1555 1.41
LINK O6 BMA A 610 C1 MAN A 611 1555 1555 1.41
LINK O6 BMA B 605 C1 MAN B 606 1555 1555 1.41
LINK C1 NAG B 607 O4 NAG B 608 1555 1555 1.41
LINK C1 NAG A 607 O4 NAG A 608 1555 1555 1.41
LINK O6 BMA A 603 C1 MAN A 604 1555 1555 1.41
LINK O6 BMA B 610 C1 MAN B 611 1555 1555 1.42
LINK C1 NAG A 601 O4 NAG A 605 1555 1555 1.42
LINK ND2 ASN A 453 C1 NAG A 608 1555 1555 1.43
LINK C1 MAN B 609 O3 BMA B 610 1555 1555 1.43
LINK ND2 ASN B 453 C1 NAG B 608 1555 1555 1.43
LINK C1 MAN A 609 O3 BMA A 610 1555 1555 1.43
LINK ND2 ASN A 343 C1 NAG A 605 1555 1555 1.43
LINK ND2 ASN B 258 C1 NAG B 612 1555 1555 1.44
LINK ND2 ASN B 343 C1 NAG B 602 1555 1555 1.44
LINK C1 MAN A 602 O3 BMA A 603 1555 1555 1.46
LINK C1 MAN B 604 O3 BMA B 605 1555 1555 1.47
CISPEP 1 ALA A 3 GLY A 4 0 -5.71
CISPEP 2 GLN A 55 HIS A 56 0 1.28
CISPEP 3 SER A 103 PRO A 104 0 1.94
CISPEP 4 ALA B 3 GLY B 4 0 0.19
CISPEP 5 GLN B 55 HIS B 56 0 0.15
CISPEP 6 SER B 103 PRO B 104 0 1.81
CISPEP 7 SER C 7 PRO C 8 0 -2.34
CISPEP 8 HIS C 93 PRO C 94 0 0.81
CISPEP 9 TYR C 139 PRO C 140 0 2.59
CISPEP 10 THR D 144 ASN D 145 0 8.24
CISPEP 11 ASN D 145 SER D 146 0 7.50
CISPEP 12 PHE D 158 PRO D 159 0 -2.14
CISPEP 13 GLU D 160 PRO D 161 0 8.32
CISPEP 14 TRP D 200 PRO D 201 0 4.17
CISPEP 15 SER E 7 PRO E 8 0 -1.65
CISPEP 16 HIS E 93 PRO E 94 0 1.44
CISPEP 17 TYR E 139 PRO E 140 0 2.33
CISPEP 18 PHE F 158 PRO F 159 0 -2.09
CISPEP 19 GLU F 160 PRO F 161 0 7.84
CISPEP 20 TRP F 200 PRO F 201 0 3.47
SITE 1 AC1 6 ARG A 289 VAL A 360 PRO A 361 HIS A 362
SITE 2 AC1 6 ALA A 363 HIS A 398
SITE 1 AC2 4 VAL B 360 PRO B 361 HIS B 362 HIS B 398
SITE 1 AC3 12 LYS A 285 GLY A 335 PRO A 337 GLY A 338
SITE 2 AC3 12 SER A 340 ASN A 343 THR F 60 HIS F 61
SITE 3 AC3 12 TYR F 62 LYS F 67 ASP F 68 THR F 71
SITE 1 AC4 9 THR A 61 SER A 62 ARG A 88 ARG A 133
SITE 2 AC4 9 PHE A 134 ASN A 453 THR C 201 SER C 202
SITE 3 AC4 9 PRO C 203
SITE 1 AC5 9 LYS A 285 GLY A 335 PRO A 337 GLY A 338
SITE 2 AC5 9 NAG A 605 FUC A 606 LYS F 67 ASP F 68
SITE 3 AC5 9 THR F 71
SITE 1 AC6 2 ASN B 258 GLU B 261
SITE 1 AC7 12 LYS B 285 GLY B 335 PRO B 337 GLY B 338
SITE 2 AC7 12 SER B 340 ASN B 343 THR D 60 HIS D 61
SITE 3 AC7 12 TYR D 62 LYS D 67 ASP D 68 THR D 71
SITE 1 AC8 9 THR B 61 SER B 62 ARG B 88 ARG B 133
SITE 2 AC8 9 PHE B 134 ASN B 453 THR E 201 SER E 202
SITE 3 AC8 9 PRO E 203
CRYST1 156.592 251.336 73.978 90.00 90.00 90.00 P 21 21 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 0.006386 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003979 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013518 0.00000
TER 4174 THR A 535
TER 8348 THR B 535
TER 9975 GLU C 212
TER 11699 ARG D 225
TER 13332 GLU E 212
TER 15016 ARG F 225
MASTER 512 0 25 65 126 0 19 615482 6 319 154
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