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HEADER HYDROLASE 04-NOV-98 1MAA
TITLE MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: MACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 BIOLOGICAL_UNIT: HOMODIMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 STRAIN: BLACK6CBA CROSS F1;
SOURCE 5 ORGAN: BRAIN (CDNA);
SOURCE 6 EXPRESSION_SYSTEM: HUMAN EMBRYONIC KIDNEY CELLS (HEK), HOMO
SOURCE 7 SAPIENS;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: 293;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: LAMBDA-ZAP AND LAMBDA-FIX CDNA
SOURCE 10 AND GENOMIC DNA;
SOURCE 11 EXPRESSION_SYSTEM_GENE: MOUSE ACHE
KEYWDS HYDROLASE, SERINE ESTERASE, ACETYLCHOLINESTERASE, TETRAMER,
KEYWDS 2 HYDROLASE FOLD, GLYCOSYLATED PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,P.TAYLOR,P.E.BOUGIS,P.MARCHOT
REVDAT 1 20-APR-99 1MAA 0
JRNL AUTH Y.BOURNE,P.TAYLOR,P.E.BOUGIS,P.MARCHOT
JRNL TITL CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE. A
JRNL TITL 2 PERIPHERAL SITE-OCCLUDING LOOP IN A TETRAMERIC
JRNL TITL 3 ASSEMBLY
JRNL REF J.BIOL.CHEM. V. 274 2963 1999
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.9
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92
REMARK 3 NUMBER OF REFLECTIONS : 107442
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 SET) : 0.20
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2
REMARK 3 FREE R VALUE TEST SET COUNT : 2166
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 (A) : 2.9
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.3
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6282
REMARK 3 BIN R VALUE (WORKING SET) : 0.32
REMARK 3 BIN FREE R VALUE : 0.39
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.84
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 124
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 : 16786
REMARK 3 NUCLEIC ACID ATOMS : NULL
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.7
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.6
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.5
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.07 ; 100
REMARK 3 GROUP 1 B-FACTOR (A**2) : 2.4 ; 2
REMARK 3 GROUP 2 POSITIONAL (A) : 0.17 ; 50
REMARK 3 GROUP 2 B-FACTOR (A**2) : 5.7 ; 5
REMARK 3 GROUP 3 POSITIONAL (A) : 0.27 ; 10
REMARK 3 GROUP 3 B-FACTOR (A**2) : 4.7 ; 10
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MAA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-1996
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.907
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107379
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.9
REMARK 200 RESOLUTION RANGE LOW (A) : 20.
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92
REMARK 200 DATA REDUNDANCY : 2.8
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.105
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.9
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.0
REMARK 200 COMPLETENESS FOR SHELL (%) : 83
REMARK 200 DATA REDUNDANCY IN SHELL : 2.7
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1MAH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS:
REMARK 280 1.7 M NAKPO4 PH 7.0, 10 MM CACL2 (COLD ROOM)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 68.27803
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.13277
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.56510
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.13277
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.27803
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.56510
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 D 7 .. 542 A 7 .. 542 0.06
REMARK 295 M 2 C 7 .. 542 B 7 .. 542 0.08
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: RESIDUES 1 - 6, 11, 13, 183 - 186, 230, 289 - 295,
REMARK 295 393, AND 493 - 497 WERE EXCLUDED FROM THE CALCULATION.
REMARK 460
REMARK 460 NON-IUPAC
REMARK 460 BY REQUEST OF THE DEPOSITOR, THE PROTEIN DATA BANK HAS NOT
REMARK 460 APPLIED THE IUPAC-IUB RECOMMENDATIONS REGARDING THE
REMARK 460 DESIGNATION OF BRANCHES 1 AND 2 OF SIDE-CHAIN ATOMS IN
REMARK 460 RESIDUES ARG, ASP, GLU, LEU, PHE, TYR, AND VAL TO THIS
REMARK 460 ENTRY.
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 GLU A 1 TO ARG A 3
REMARK 465 ASP A 544 TO PRO A 549
REMARK 465 GLU D 1 TO ARG D 3
REMARK 465 THR D 545 TO PRO D 549
REMARK 465 GLU B 1 TO GLY A 2
REMARK 465 PRO B 258 TO GLY B 264
REMARK 465 LEU B 546 TO PRO B 549
REMARK 465 PRO C 258 TO GLY C 264
REMARK 465 GLU C 548 TO PRO C 549
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 491 CG OD1 OD2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 494 CG OD1 OD2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 SER A 497 OG
REMARK 470 ASP B 491 CG OD1 OD2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 494 CG OD1 OD2
REMARK 470 ARG B 495 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 470 SER B 497 OG
REMARK 470 ASP B 544 CG OD1 OD2
REMARK 470 ARG C 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 491 CG OD1 OD2
REMARK 470 ARG C 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 494 CG OD1 OD2
REMARK 470 ARG C 495 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 496 CG CD CE NZ
REMARK 470 SER C 497 OG
REMARK 470 ASP C 544 CG OD1 OD2
REMARK 470 LEU C 546 CG CD1 CD2
REMARK 470 ASP C 547 CG OD1 OD2
REMARK 470 ASP D 491 CG OD1 OD2
REMARK 470 ARG D 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 494 CG OD1 OD2
REMARK 470 LYS D 496 CG CD CE NZ
REMARK 470 SER D 497 OG
REMARK 470 ASP D 544 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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 4*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,A4,A1,2X,
REMARK 500 A3,1X,A1,I4,A1,1X,A4,A1,4X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 0 MET C 195 SD MET C 195 CE 0.177
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 REFERENCE: RACHINSKY ET AL. (1990) NEURON, 5:317-327.
REMARK 999 THE ENZYME CONTAINS THE ALTERNATIVE SPLICE OF EXON 5, AND
REMARK 999 IS TRUNCATED AT CODON POSITION 549; WHICH YIELDS AN ENZYME
REMARK 999 TRUNCATED BY 7 RESIDUES.
REMARK 999 1MAA A SWS P21836 1 - 34 NOT IN ATOMS LIST
REMARK 999 1MAA A SWS P21836 575 - 614 NOT IN ATOMS LIST
REMARK 999 1MAA B SWS P21836 1 - 33 NOT IN ATOMS LIST
REMARK 999 1MAA B SWS P21836 577 - 614 NOT IN ATOMS LIST
REMARK 999 1MAA C SWS P21836 1 - 31 NOT IN ATOMS LIST
REMARK 999 1MAA C SWS P21836 579 - 614 NOT IN ATOMS LIST
REMARK 999 1MAA D SWS P21836 1 - 34 NOT IN ATOMS LIST
REMARK 999 1MAA D SWS P21836 576 - 614 NOT IN ATOMS LIST
DBREF 1MAA A 4 543 SWS P21836 ACES_MOUSE 35 574
DBREF 1MAA B 3 257 SWS P21836 ACES_MOUSE 34 288
DBREF 1MAA B 265 545 SWS P21836 ACES_MOUSE 296 576
DBREF 1MAA C 1 257 SWS P21836 ACES_MOUSE 32 288
DBREF 1MAA C 265 547 SWS P21836 ACES_MOUSE 296 578
DBREF 1MAA D 4 544 SWS P21836 ACES_MOUSE 35 575
SEQADV 1MAA ARG A 495 SWS P21836 SER 526 CONFLICT
SEQADV 1MAA B SWS P21836 PRO 289 GAP IN PDB ENTRY
SEQADV 1MAA B SWS P21836 PRO 290 GAP IN PDB ENTRY
SEQADV 1MAA B SWS P21836 GLY 291 GAP IN PDB ENTRY
SEQADV 1MAA B SWS P21836 GLY 292 GAP IN PDB ENTRY
SEQADV 1MAA B SWS P21836 ALA 293 GAP IN PDB ENTRY
SEQADV 1MAA B SWS P21836 GLY 294 GAP IN PDB ENTRY
SEQADV 1MAA B SWS P21836 GLY 295 GAP IN PDB ENTRY
SEQADV 1MAA ARG C 495 SWS P21836 SER 526 CONFLICT
SEQADV 1MAA C SWS P21836 PRO 289 GAP IN PDB ENTRY
SEQADV 1MAA C SWS P21836 PRO 290 GAP IN PDB ENTRY
SEQADV 1MAA C SWS P21836 GLY 291 GAP IN PDB ENTRY
SEQADV 1MAA C SWS P21836 GLY 292 GAP IN PDB ENTRY
SEQADV 1MAA C SWS P21836 ALA 293 GAP IN PDB ENTRY
SEQADV 1MAA C SWS P21836 GLY 294 GAP IN PDB ENTRY
SEQADV 1MAA C SWS P21836 GLY 295 GAP IN PDB ENTRY
SEQADV 1MAA ARG C 495 SWS P21836 SER 526 CONFLICT
SEQADV 1MAA ARG D 495 SWS P21836 SER 526 CONFLICT
SEQRES 1 A 547 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 547 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 547 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 547 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 547 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 547 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 547 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 547 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 547 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 547 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 547 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 547 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 547 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 547 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 547 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 547 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 547 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 547 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 547 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 547 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 547 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 547 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 547 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 547 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 547 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 547 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 547 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 547 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 547 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 547 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 547 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 547 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 547 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 547 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 547 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 547 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 547 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 547 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 547 ARG LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 547 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 547 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 547 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 A 547 ASP
SEQRES 1 B 547 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 547 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 547 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 547 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 547 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 547 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 547 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 547 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 547 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 547 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 547 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 547 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 547 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 547 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 547 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 547 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 547 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 547 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 547 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 547 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 547 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 547 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 547 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 547 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 547 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 547 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 547 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 547 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 547 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 547 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 547 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 547 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 547 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 547 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 547 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 547 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 547 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 547 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 547 ARG LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 547 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 547 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 547 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 B 547 ASP
SEQRES 1 C 547 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 C 547 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 C 547 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 C 547 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 C 547 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 C 547 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 C 547 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 C 547 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 C 547 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 C 547 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 C 547 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 C 547 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 C 547 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 C 547 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 C 547 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 C 547 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 C 547 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 C 547 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 C 547 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 C 547 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 C 547 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 C 547 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 C 547 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 C 547 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 C 547 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 C 547 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 C 547 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 C 547 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 C 547 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 C 547 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 C 547 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 C 547 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 C 547 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 C 547 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 C 547 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 C 547 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 C 547 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 C 547 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 C 547 ARG LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 C 547 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 C 547 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 C 547 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 C 547 ASP
SEQRES 1 D 547 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 D 547 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 D 547 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 D 547 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 D 547 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 D 547 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 D 547 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 D 547 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 D 547 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 D 547 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 D 547 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 D 547 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 D 547 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 D 547 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 D 547 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 D 547 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 D 547 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 D 547 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 D 547 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 D 547 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 D 547 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 D 547 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 D 547 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 D 547 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 D 547 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 D 547 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 D 547 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 D 547 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 D 547 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 D 547 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 D 547 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 D 547 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 D 547 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 D 547 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 D 547 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 D 547 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 D 547 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 D 547 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 D 547 ARG LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 D 547 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 D 547 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 D 547 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 D 547 ASP
MODRES 1MAA ASN A 350 ASN N-GLYCOSYLATED
MODRES 1MAA ASN D 350 ASN N-GLYCOSYLATED
HET PO4 349 5
HET DME 997 18
HET GOL 951 6
HET DME 999 18
HET NAG 608 14
HET NAG 609 14
HET FUC 610 10
HET GOL 952 6
HET PO4 1 5
HET PO4 101 5
HET DME 996 18
HET DME 998 18
HET GOL 953 6
HET GOL 954 6
HET NAG 709 14
HETNAM PO4 PHOSPHATE ION
HETNAM DME DECAMETHONIUM ION
HETNAM GOL GLYCEROL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC FUCOSE
FORMUL 5 PO4 3(O4 P1 3-)
FORMUL 6 DME 4(C16 H38 N2 2+)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 8 NAG 3(C8 H15 N1 O6)
FORMUL 9 FUC C6 H12 O5
FORMUL 10 HOH *187(H2 O1)
HELIX 1 1 GLY A 43 ARG A 45 5 3
HELIX 2 2 GLU A 81 TRP A 86 1 6
HELIX 3 3 ASP A 131 TYR A 133 5 3
HELIX 4 4 PHE A 137 GLN A 140 1 4
HELIX 5 5 GLY A 154 PHE A 158 1 5
HELIX 6 6 VAL A 171 PHE A 190 1 20
HELIX 7 7 SER A 203 LEU A 214 1 12
HELIX 8 8 LEU A 216 LEU A 221 1 6
HELIX 9 9 ALA A 241 VAL A 255 1 15
HELIX 10 10 ASP A 266 THR A 275 1 10
HELIX 11 11 ALA A 278 VAL A 288 1 11
HELIX 12 12 PRO A 312 THR A 318 1 7
HELIX 13 13 GLU A 334 LEU A 339 5 6
HELIX 14 14 ARG A 356 GLY A 366 1 11
HELIX 15 15 ASP A 372 TYR A 382 1 11
HELIX 16 16 PRO A 391 ASN A 406 1 16
HELIX 17 17 VAL A 408 GLN A 421 1 14
HELIX 18 18 LEU A 441 MET A 443 5 3
HELIX 19 19 ILE A 451 PHE A 455 1 5
HELIX 20 20 LEU A 457 LEU A 459 5 3
HELIX 21 21 THR A 467 ARG A 485 1 19
HELIX 22 22 ALA A 526 ASN A 533 1 8
HELIX 23 23 PHE A 535 LEU A 540 1 6
HELIX 24 24 GLY B 43 ARG B 45 5 3
HELIX 25 25 GLU B 81 TRP B 86 1 6
HELIX 26 26 ASP B 131 TYR B 133 5 3
HELIX 27 27 GLY B 135 GLU B 142 1 8
HELIX 28 28 GLY B 154 PHE B 158 1 5
HELIX 29 29 VAL B 171 PHE B 190 1 20
HELIX 30 30 SER B 203 ILE B 213 5 11
HELIX 31 31 LEU B 216 LEU B 221 1 6
HELIX 32 32 ALA B 241 VAL B 255 1 15
HELIX 33 33 ASP B 266 THR B 275 1 10
HELIX 34 34 ALA B 278 HIS B 284 1 7
HELIX 35 35 PRO B 312 ASN B 317 1 6
HELIX 36 36 SER B 336 GLY B 342 1 7
HELIX 37 37 ARG B 356 GLY B 366 1 11
HELIX 38 38 ASP B 372 TYR B 382 1 11
HELIX 39 39 PRO B 391 ASN B 406 1 16
HELIX 40 40 VAL B 408 ALA B 420 1 13
HELIX 41 41 LEU B 441 MET B 443 5 3
HELIX 42 42 ILE B 451 ILE B 454 1 4
HELIX 43 43 LEU B 457 LEU B 459 5 3
HELIX 44 44 THR B 467 THR B 486 1 20
HELIX 45 45 ALA B 526 ASN B 533 1 8
HELIX 46 46 LEU B 536 ALA B 542 1 7
HELIX 47 47 PRO C 6 LEU C 8 5 3
HELIX 48 48 GLY C 43 ARG C 45 5 3
HELIX 49 49 GLU C 81 TRP C 86 1 6
HELIX 50 50 ASP C 131 TYR C 133 5 3
HELIX 51 51 GLY C 135 GLU C 142 1 8
HELIX 52 52 GLY C 154 PHE C 158 1 5
HELIX 53 53 VAL C 171 PHE C 190 1 20
HELIX 54 54 PRO C 194 SER C 196 5 3
HELIX 55 55 SER C 203 ILE C 213 5 11
HELIX 56 56 LEU C 216 LEU C 221 1 6
HELIX 57 57 ALA C 241 LEU C 254 1 14
HELIX 58 58 ASP C 266 THR C 275 1 10
HELIX 59 59 ALA C 278 VAL C 288 1 11
HELIX 60 60 PRO C 312 ASN C 317 1 6
HELIX 61 61 SER C 336 TYR C 341 1 6
HELIX 62 62 ARG C 356 GLY C 366 1 11
HELIX 63 63 ASP C 372 TYR C 382 1 11
HELIX 64 64 PRO C 391 ASN C 406 1 16
HELIX 65 65 VAL C 408 GLN C 421 1 14
HELIX 66 66 LEU C 441 MET C 443 5 3
HELIX 67 67 ILE C 451 ILE C 454 1 4
HELIX 68 68 LEU C 457 LEU C 459 5 3
HELIX 69 69 THR C 467 THR C 486 1 20
HELIX 70 70 ALA C 526 ASN C 533 1 8
HELIX 71 71 LEU C 536 ALA C 542 1 7
HELIX 72 72 GLY D 43 ARG D 45 5 3
HELIX 73 73 GLU D 81 TRP D 86 1 6
HELIX 74 74 ASP D 131 TYR D 133 5 3
HELIX 75 75 PHE D 137 GLN D 140 1 4
HELIX 76 76 GLY D 154 PHE D 158 1 5
HELIX 77 77 VAL D 171 PHE D 190 1 20
HELIX 78 78 SER D 203 LEU D 214 1 12
HELIX 79 79 LEU D 216 LEU D 221 1 6
HELIX 80 80 ALA D 241 VAL D 255 1 15
HELIX 81 81 ASP D 266 THR D 275 1 10
HELIX 82 82 ALA D 278 VAL D 288 1 11
HELIX 83 83 PRO D 312 THR D 318 1 7
HELIX 84 84 GLU D 334 LEU D 339 5 6
HELIX 85 85 ARG D 356 GLY D 366 1 11
HELIX 86 86 ASP D 372 TYR D 382 1 11
HELIX 87 87 PRO D 391 ASN D 406 1 16
HELIX 88 88 VAL D 408 GLN D 421 1 14
HELIX 89 89 LEU D 441 MET D 443 5 3
HELIX 90 90 ILE D 451 PHE D 455 1 5
HELIX 91 91 LEU D 457 LEU D 459 5 3
HELIX 92 92 THR D 467 ARG D 485 1 19
HELIX 93 93 ALA D 526 ASN D 533 1 8
HELIX 94 94 PHE D 535 LEU D 540 1 6
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 N LEU A 17 O VAL A 10
SHEET 3 A 3 VAL A 59 ASP A 61 1 N LEU A 60 O GLN A 16
SHEET 1 B 9 ILE A 20 ALA A 24 0
SHEET 2 B 9 GLY A 27 ALA A 31 -1 N ALA A 31 O ILE A 20
SHEET 3 B 9 LEU A 99 PRO A 104 -1 N THR A 103 O SER A 30
SHEET 4 B 9 VAL A 145 MET A 149 -1 N SER A 148 O ASN A 100
SHEET 5 B 9 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 B 9 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 B 9 ARG A 224 GLN A 228 1 N ARG A 224 O LEU A 199
SHEET 8 B 9 GLN A 325 VAL A 328 1 N GLN A 325 O ALA A 225
SHEET 9 B 9 ARG A 424 TYR A 426 1 N ARG A 424 O VAL A 326
SHEET 1 C 2 ALA A 427 PHE A 430 0
SHEET 2 C 2 TYR A 510 LEU A 513 1 N VAL A 511 O ALA A 427
SHEET 1 D 3 LEU B 9 VAL B 12 0
SHEET 2 D 3 GLY B 15 ARG B 18 -1 N LEU B 17 O VAL B 10
SHEET 3 D 3 VAL B 59 ASP B 61 1 N LEU B 60 O GLN B 16
SHEET 1 E11 ILE B 20 ALA B 24 0
SHEET 2 E11 GLY B 27 PRO B 36 -1 N ALA B 31 O ILE B 20
SHEET 3 E11 TYR B 98 PRO B 104 -1 N THR B 103 O SER B 30
SHEET 4 E11 VAL B 145 MET B 149 -1 N SER B 148 O ASN B 100
SHEET 5 E11 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 145
SHEET 6 E11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 E11 ARG B 224 GLN B 228 1 N ARG B 224 O LEU B 199
SHEET 8 E11 GLN B 325 VAL B 331 1 N GLN B 325 O ALA B 225
SHEET 9 E11 ARG B 424 PHE B 430 1 N ARG B 424 O VAL B 326
SHEET 10 E11 GLN B 509 LEU B 513 1 N VAL B 511 O ILE B 429
SHEET 11 E11 VAL B 520 ARG B 522 -1 N ARG B 521 O TYR B 510
SHEET 1 F 3 LEU C 9 VAL C 12 0
SHEET 2 F 3 GLY C 15 ARG C 18 -1 N LEU C 17 O VAL C 10
SHEET 3 F 3 VAL C 59 ASP C 61 1 N LEU C 60 O GLN C 16
SHEET 1 G11 ILE C 20 ALA C 24 0
SHEET 2 G11 GLY C 27 PRO C 36 -1 N ALA C 31 O ILE C 20
SHEET 3 G11 TYR C 98 PRO C 104 -1 N THR C 103 O SER C 30
SHEET 4 G11 VAL C 145 MET C 149 -1 N SER C 148 O ASN C 100
SHEET 5 G11 THR C 112 ILE C 118 1 N LEU C 115 O VAL C 145
SHEET 6 G11 GLY C 192 GLU C 202 1 N ASP C 193 O THR C 112
SHEET 7 G11 ARG C 224 GLN C 228 1 N ARG C 224 O LEU C 199
SHEET 8 G11 GLN C 325 VAL C 331 1 N GLN C 325 O ALA C 225
SHEET 9 G11 ARG C 424 PHE C 430 1 N ARG C 424 O VAL C 326
SHEET 10 G11 GLN C 509 LEU C 513 1 N VAL C 511 O ILE C 429
SHEET 11 G11 VAL C 520 ARG C 522 -1 N ARG C 521 O TYR C 510
SHEET 1 H 3 LEU D 9 VAL D 12 0
SHEET 2 H 3 GLY D 15 ARG D 18 -1 N LEU D 17 O VAL D 10
SHEET 3 H 3 VAL D 59 ASP D 61 1 N LEU D 60 O GLN D 16
SHEET 1 I 9 ILE D 20 ALA D 24 0
SHEET 2 I 9 GLY D 27 ALA D 31 -1 N ALA D 31 O ILE D 20
SHEET 3 I 9 LEU D 99 PRO D 104 -1 N THR D 103 O SER D 30
SHEET 4 I 9 VAL D 145 MET D 149 -1 N SER D 148 O ASN D 100
SHEET 5 I 9 THR D 112 ILE D 118 1 N LEU D 115 O VAL D 145
SHEET 6 I 9 GLY D 192 GLU D 202 1 N ASP D 193 O THR D 112
SHEET 7 I 9 ARG D 224 GLN D 228 1 N ARG D 224 O LEU D 199
SHEET 8 I 9 GLN D 325 VAL D 328 1 N GLN D 325 O ALA D 225
SHEET 9 I 9 ARG D 424 TYR D 426 1 N ARG D 424 O VAL D 326
SHEET 1 J 3 ALA D 427 PHE D 430 0
SHEET 2 J 3 GLN D 509 LEU D 513 1 N VAL D 511 O ALA D 427
SHEET 3 J 3 VAL D 520 ARG D 522 -1 N ARG D 521 O TYR D 510
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
SSBOND 4 CYS B 69 CYS B 96
SSBOND 5 CYS B 257 CYS B 272
SSBOND 6 CYS B 409 CYS B 529
SSBOND 7 CYS C 69 CYS C 96
SSBOND 8 CYS C 257 CYS C 272
SSBOND 9 CYS C 409 CYS C 529
SSBOND 10 CYS D 69 CYS D 96
SSBOND 11 CYS D 257 CYS D 272
SSBOND 12 CYS D 409 CYS D 529
LINK C1 NAG 608 O4 NAG 609
LINK C1 NAG 609 ND2 ASN D 350
LINK O6 NAG 609 C1 FUC 610
LINK C1 NAG 709 ND2 ASN A 350
CISPEP 1 TYR A 105 PRO A 106 0 0.31
CISPEP 2 CYS A 257 PRO A 258 0 -0.47
CISPEP 3 TYR B 105 PRO B 106 0 0.06
CISPEP 4 TYR C 105 PRO C 106 0 0.21
CISPEP 5 TYR D 105 PRO D 106 0 0.36
CISPEP 6 CYS D 257 PRO D 258 0 -0.27
CRYST1 136.550 173.130 224.250 90.00 90.00 90.00 P 21 21 21 16
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 0.007323 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005776 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004459 0.00000
MTRIX1 1 -0.949000 -0.260000 0.179000 114.35200 1
MTRIX2 1 -0.249000 0.271000 -0.930000 123.35900 1
MTRIX3 1 0.193000 -0.927000 -0.322000 137.43401 1
MTRIX1 2 -0.948000 -0.266000 0.175000 115.27400 1
MTRIX2 2 -0.246000 0.262000 -0.933000 124.27000 1
MTRIX3 2 0.202000 -0.928000 -0.314000 136.49699 1 |