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HEADER HYDROLASE 16-OCT-15 5FKJ
TITLE CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 C-547, AN ALKYL AMMONIUM DERIVATIVE OF 6-METHYL URACIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 32-574;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE, ACETYLCHOLINESTERASE, C-547
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,M.VILLARD-WANDHAMMER,K.PETROV,P.MASSON
REVDAT 1 16-MAR-16 5FKJ 0
JRNL AUTH A.D.KHARLAMOVA,S.V.LUSHCHEKINA,K.A.PETROV,E.D.KOTS,
JRNL AUTH 2 F.V.NACHON,M.VILLARD-WANDHAMMER,I.V.ZUEVA,E.KREJCI,
JRNL AUTH 3 V.S.REZNIK,V.V.ZOBOV,E.E.NIKOLSKY,P.MASSON
JRNL TITL SLOW-BINDING INHIBITION OF ACETYLCHOLINESTERASE BY A 6-
JRNL TITL 2 METHYLURACIL ALKYL-AMMONIUM DERIVATIVE: MECHANISM AND
JRNL TITL 3 ADVANTAGES FOR MYASTHENIA GRAVIS TREATMENT.
JRNL REF BIOCHEM.J. 2016
JRNL REFN ESSN 1470-8728
JRNL PMID 26929400
JRNL DOI 10.1042/BCJ20160084
REMARK 2
REMARK 2 RESOLUTION. 3.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.133
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 94.524
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.35
REMARK 3 NUMBER OF REFLECTIONS : 94994
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.2078
REMARK 3 R VALUE (WORKING SET) : 0.2073
REMARK 3 FREE R VALUE : 0.2494
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1046
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE CCWORK
REMARK 3 1 94.5674 - 5.9930 1.00 13916 156 0.1849 0.2281 0.917
REMARK 3 2 5.9930 - 4.7568 1.00 13543 150 0.1779 0.2039 0.915
REMARK 3 3 4.7568 - 4.1555 1.00 13409 149 0.1695 0.2159 0.925
REMARK 3 4 4.1555 - 3.7756 1.00 13394 149 0.1960 0.2354 0.906
REMARK 3 5 3.7756 - 3.5049 1.00 13325 149 0.2417 0.2983 0.869
REMARK 3 6 3.5049 - 3.2983 1.00 13343 148 0.2742 0.3317 0.823
REMARK 3 7 3.2983 - 3.1331 0.98 13018 145 0.3357 0.3507 0.732
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.40
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.5
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 17565
REMARK 3 ANGLE : 0.847 24034
REMARK 3 CHIRALITY : 0.056 2561
REMARK 3 PLANARITY : 0.006 3155
REMARK 3 DIHEDRAL : 16.277 10287
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5597 -29.1297 85.8149
REMARK 3 T TENSOR
REMARK 3 T11: 0.4995 T22: 0.5212
REMARK 3 T33: 0.5105 T12: -0.0172
REMARK 3 T13: 0.0470 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.0281 L22: 2.7656
REMARK 3 L33: 1.5527 L12: 0.3122
REMARK 3 L13: -0.0857 L23: -0.3253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: 0.0119 S13: 0.0679
REMARK 3 S21: 0.1413 S22: 0.0234 S23: 0.0915
REMARK 3 S31: -0.1773 S32: -0.0083 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5087 26.9033 66.5270
REMARK 3 T TENSOR
REMARK 3 T11: 1.0833 T22: 0.7677
REMARK 3 T33: 0.7219 T12: 0.4272
REMARK 3 T13: 0.2488 T23: 0.0557
REMARK 3 L TENSOR
REMARK 3 L11: 1.8991 L22: 3.5387
REMARK 3 L33: 3.0336 L12: -0.7167
REMARK 3 L13: 0.4705 L23: -1.6586
REMARK 3 S TENSOR
REMARK 3 S11: -0.1228 S12: -0.3184 S13: 0.0898
REMARK 3 S21: 1.1332 S22: 0.4511 S23: 0.5077
REMARK 3 S31: -1.0931 S32: -0.8028 S33: 0.0741
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0097 12.4321 25.5550
REMARK 3 T TENSOR
REMARK 3 T11: 0.5305 T22: 0.4849
REMARK 3 T33: 0.5189 T12: 0.0280
REMARK 3 T13: 0.0634 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 1.0169 L22: 1.2441
REMARK 3 L33: 2.1137 L12: 0.0507
REMARK 3 L13: 0.1720 L23: -0.0790
REMARK 3 S TENSOR
REMARK 3 S11: -0.0913 S12: 0.0105 S13: -0.0543
REMARK 3 S21: 0.0512 S22: -0.0002 S23: -0.0728
REMARK 3 S31: 0.0818 S32: 0.2665 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8884 4.9577 81.3984
REMARK 3 T TENSOR
REMARK 3 T11: 0.4527 T22: 0.6304
REMARK 3 T33: 0.6193 T12: -0.0030
REMARK 3 T13: -0.0644 T23: 0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 1.1354 L22: 1.6123
REMARK 3 L33: 3.4087 L12: -0.1951
REMARK 3 L13: 0.5140 L23: -0.2662
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: 0.1550 S13: 0.1760
REMARK 3 S21: 0.0051 S22: -0.1115 S23: -0.2881
REMARK 3 S31: -0.1581 S32: 0.3452 S33: -0.0010
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-15.
REMARK 100 THE PDBE ID CODE IS EBI-65320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM Q210)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95147
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.13
REMARK 200 RESOLUTION RANGE LOW (A) : 87.72
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.7
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.69
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.7
REMARK 200 R MERGE FOR SHELL (I) : 0.84
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.57
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4A16
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE BUFFER PH 9, 1.6 M
REMARK 280 AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 68.57500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 87.72500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.57500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 87.72500
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -151.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLU A 1
REMARK 465 GLY A 2
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 ALA B 542
REMARK 465 THR B 543
REMARK 465 GLU C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 LEU C 540
REMARK 465 SER C 541
REMARK 465 ALA C 542
REMARK 465 THR C 543
REMARK 465 GLU D 1
REMARK 465 GLY D 2
REMARK 465 ARG D 3
REMARK 465 LEU D 540
REMARK 465 SER D 541
REMARK 465 ALA D 542
REMARK 465 THR D 543
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL A 300 O HOH A 2047 2.18
REMARK 500 O HOH A 2047 O HOH A 2048 2.13
REMARK 500 O HOH A 2048 O HOH A 2078 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 257 CA - CB - SG ANGL. DEV. = 9.4 DEGREES
REMARK 500 CYS C 257 CA - CB - SG ANGL. DEV. = 10.9 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 PHE A 47 -9.24 70.79
REMARK 500 PHE A 123 12.20 58.54
REMARK 500 SER A 203 -129.12 55.55
REMARK 500 HIS A 223 -56.42 -128.89
REMARK 500 ALA A 262 -24.74 56.41
REMARK 500 ASP A 306 -75.50 -123.16
REMARK 500 VAL A 407 -61.11 -126.72
REMARK 500 LYS A 496 -9.13 86.11
REMARK 500 ARG A 525 63.85 33.30
REMARK 500 LEU A 540 -143.99 50.43
REMARK 500 PHE B 47 -3.82 75.95
REMARK 500 PRO B 108 49.87 -75.44
REMARK 500 ALA B 109 -116.92 51.56
REMARK 500 PHE B 123 15.06 58.10
REMARK 500 SER B 203 -133.88 58.27
REMARK 500 HIS B 223 -59.44 -120.98
REMARK 500 PRO B 259 46.58 -89.11
REMARK 500 ASP B 306 -71.08 -129.63
REMARK 500 SER B 336 -70.68 -55.51
REMARK 500 VAL B 367 72.68 -119.17
REMARK 500 VAL B 407 -65.28 -130.45
REMARK 500 ASP B 494 -144.67 54.42
REMARK 500 SER B 497 176.41 73.16
REMARK 500 GLN B 499 -157.43 58.26
REMARK 500 TRP B 500 83.58 -157.52
REMARK 500 LEU B 515 -105.76 49.88
REMARK 500 PHE B 535 -62.63 -91.05
REMARK 500 PHE C 47 -9.17 71.21
REMARK 500 PHE C 123 13.79 58.09
REMARK 500 SER C 203 -128.12 51.61
REMARK 500 ALA C 262 -65.89 -143.56
REMARK 500 ASP C 306 -72.47 -126.46
REMARK 500 VAL C 367 71.67 -118.24
REMARK 500 VAL C 407 -64.12 -129.49
REMARK 500 ASP C 494 160.45 175.76
REMARK 500 ARG C 534 -61.39 -97.38
REMARK 500 PHE D 47 -5.60 73.78
REMARK 500 PHE D 123 13.13 58.69
REMARK 500 SER D 203 -130.12 57.05
REMARK 500 HIS D 223 -57.84 -120.65
REMARK 500 ALA D 262 -118.34 57.34
REMARK 500 ASP D 306 -77.31 -121.76
REMARK 500 VAL D 407 -64.73 -130.65
REMARK 500 ARG D 493 -115.31 56.54
REMARK 500 ASP D 494 -111.16 60.30
REMARK 500 SER D 495 -157.18 60.40
REMARK 500 LYS D 496 -9.83 56.60
REMARK 500 ARG D 525 63.40 32.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 260 GLY A 261 134.01
REMARK 500 LYS A 496 SER A 497 149.13
REMARK 500 LEU A 540 SER A 541 141.52
REMARK 500 GLY B 260 GLY B 261 -149.49
REMARK 500 SER B 497 PRO B 498 -141.28
REMARK 500 ALA C 262 GLY C 263 -124.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2029 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH D2099 DISTANCE = 9.07 ANGSTROMS
REMARK 525 HOH D2100 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH D2101 DISTANCE = 8.21 ANGSTROMS
REMARK 525 HOH D2102 DISTANCE = 5.68 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 G0W B 550
REMARK 610 G0W D 550
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G0W A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G0W B 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G0W C 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G0W D 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 560 BOUND TO ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 560 BOUND TO ASN B 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 561 BOUND TO ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG C 560 BOUND TO ASN C 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG D 560 BOUND TO ASN D 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG D 561 BOUND TO ASN D 350
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CONTAINS MUTATION D544STOP TO PRODUCE TRUNCATION
DBREF 5FKJ A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 5FKJ B 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 5FKJ C 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 5FKJ D 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 C 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 C 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 C 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 C 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 C 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 C 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 C 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 C 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 C 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 C 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 C 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 C 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 C 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 C 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 C 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 C 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 C 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 C 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 C 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 C 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 C 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 C 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 C 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 C 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 C 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 C 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 C 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 C 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 C 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 C 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 C 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 C 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 C 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 C 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 C 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 C 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 C 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 C 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 C 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 C 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 C 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 C 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 D 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 D 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 D 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 D 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 D 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 D 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 D 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 D 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 D 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 D 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 D 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 D 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 D 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 D 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 D 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 D 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 D 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 D 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 D 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 D 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 D 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 D 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 D 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 D 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 D 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 D 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 D 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 D 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 D 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 D 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 D 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 D 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 D 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 D 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 D 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 D 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 D 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 D 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 D 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 D 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 D 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 D 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
MODRES 5FKJ ASN A 265 ASN GLYCOSYLATION SITE
MODRES 5FKJ ASN B 265 ASN GLYCOSYLATION SITE
MODRES 5FKJ ASN B 350 ASN GLYCOSYLATION SITE
MODRES 5FKJ ASN C 265 ASN GLYCOSYLATION SITE
MODRES 5FKJ ASN D 265 ASN GLYCOSYLATION SITE
MODRES 5FKJ ASN D 350 ASN GLYCOSYLATION SITE
HET G0W A 550 49
HET NAG A 560 14
HET CL A 601 1
HET CL A 604 1
HET CL A 605 1
HET CL A 606 1
HET CL A 607 1
HET CL A 608 1
HET CL A 609 1
HET CL A 610 1
HET CL A 611 1
HET G0W B 550 31
HET NAG B 560 14
HET NAG B 561 14
HET CL B 605 1
HET CL B 606 1
HET CL B 607 1
HET CL B 608 1
HET SO4 B1542 5
HET G0W C 550 49
HET NAG C 560 14
HET CL C 603 1
HET CL C 605 1
HET CL C 606 1
HET CL C 607 1
HET CL C 608 1
HET CL C 609 1
HET CL C 610 1
HET CL C 611 1
HET CL C 612 1
HET SO4 C1541 5
HET G0W D 550 31
HET NAG D 560 14
HET NAG D 561 14
HET CL D 605 1
HET CL D 606 1
HET CL D 607 1
HET CL D 608 1
HET CL D 609 1
HET CL D 610 1
HET SO4 D1540 5
HETNAM G0W 1,3-BIS[5(DIETHYL-O-NITROBENZYLAMMONIUM)PENTYL]-6-
HETNAM 2 G0W METHYLURACIL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 5 G0W 4(C37 H56 N6 O6 2+)
FORMUL 6 NAG 6(C8 H15 N O6)
FORMUL 7 CL 28(CL 1-)
FORMUL 23 SO4 3(O4 S 2-)
FORMUL 46 HOH *374(H2 O)
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 215 SER A 220 1 6
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 ARG A 274 1 10
HELIX 12 12 PRO A 277 HIS A 284 1 8
HELIX 13 13 GLU A 285 LEU A 289 5 5
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 GLY A 342 5 8
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 ASP A 460 ASN A 464 5 5
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 ARG A 534 1 10
HELIX 26 26 PHE A 535 LEU A 540 5 6
HELIX 27 27 VAL B 42 ARG B 46 5 5
HELIX 28 28 PHE B 80 MET B 85 1 6
HELIX 29 29 LEU B 130 ASP B 134 5 5
HELIX 30 30 GLY B 135 GLY B 143 1 9
HELIX 31 31 VAL B 153 LEU B 159 1 7
HELIX 32 32 ASN B 170 ILE B 187 1 18
HELIX 33 33 ALA B 188 PHE B 190 5 3
HELIX 34 34 SER B 203 SER B 215 1 13
HELIX 35 35 LEU B 216 LEU B 221 5 6
HELIX 36 36 SER B 240 VAL B 255 1 16
HELIX 37 37 ASN B 265 THR B 275 1 11
HELIX 38 38 PRO B 277 HIS B 284 1 8
HELIX 39 39 GLU B 285 LEU B 289 5 5
HELIX 40 40 THR B 311 GLY B 319 1 9
HELIX 41 41 SER B 336 GLY B 342 5 7
HELIX 42 42 SER B 355 VAL B 367 1 13
HELIX 43 43 SER B 371 THR B 383 1 13
HELIX 44 44 ASP B 390 VAL B 407 1 18
HELIX 45 45 VAL B 407 GLN B 421 1 15
HELIX 46 46 PRO B 440 GLY B 444 5 5
HELIX 47 47 GLU B 450 PHE B 455 1 6
HELIX 48 48 GLY B 456 ASP B 460 5 5
HELIX 49 49 ASP B 460 ASN B 464 5 5
HELIX 50 50 THR B 466 GLY B 487 1 22
HELIX 51 51 ARG B 525 ARG B 534 1 10
HELIX 52 52 ARG B 534 SER B 541 1 8
HELIX 53 53 VAL C 42 ARG C 46 5 5
HELIX 54 54 PHE C 80 MET C 85 1 6
HELIX 55 55 LEU C 130 ASP C 134 5 5
HELIX 56 56 GLY C 135 GLY C 143 1 9
HELIX 57 57 GLY C 154 LEU C 159 1 6
HELIX 58 58 ASN C 170 ILE C 187 1 18
HELIX 59 59 ALA C 188 PHE C 190 5 3
HELIX 60 60 SER C 203 SER C 215 1 13
HELIX 61 61 LEU C 216 PHE C 222 5 7
HELIX 62 62 SER C 240 VAL C 255 1 16
HELIX 63 63 ASN C 265 ARG C 274 1 10
HELIX 64 64 PRO C 277 GLU C 285 1 9
HELIX 65 65 TRP C 286 LEU C 289 5 4
HELIX 66 66 THR C 311 GLY C 319 1 9
HELIX 67 67 GLY C 335 GLY C 342 5 8
HELIX 68 68 SER C 355 VAL C 367 1 13
HELIX 69 69 SER C 371 THR C 383 1 13
HELIX 70 70 ASP C 390 VAL C 407 1 18
HELIX 71 71 VAL C 407 GLN C 421 1 15
HELIX 72 72 PRO C 440 GLY C 444 5 5
HELIX 73 73 GLU C 450 PHE C 455 1 6
HELIX 74 74 GLY C 456 ASP C 460 5 5
HELIX 75 75 ASP C 460 ASN C 464 5 5
HELIX 76 76 THR C 466 GLY C 487 1 22
HELIX 77 77 ARG C 525 ARG C 534 1 10
HELIX 78 78 PHE C 535 LEU C 539 5 5
HELIX 79 79 ASP D 5 GLN D 7 5 3
HELIX 80 80 VAL D 42 ARG D 46 5 5
HELIX 81 81 PHE D 80 MET D 85 1 6
HELIX 82 82 LEU D 130 ASP D 134 5 5
HELIX 83 83 GLY D 135 GLY D 143 1 9
HELIX 84 84 VAL D 153 LEU D 159 1 7
HELIX 85 85 ASN D 170 ILE D 187 1 18
HELIX 86 86 ALA D 188 PHE D 190 5 3
HELIX 87 87 SER D 203 SER D 215 1 13
HELIX 88 88 LEU D 216 PHE D 222 5 7
HELIX 89 89 SER D 240 VAL D 255 1 16
HELIX 90 90 ASN D 265 ARG D 274 1 10
HELIX 91 91 PRO D 277 GLU D 285 1 9
HELIX 92 92 TRP D 286 LEU D 289 5 4
HELIX 93 93 THR D 311 GLY D 319 1 9
HELIX 94 94 SER D 336 GLY D 342 5 7
HELIX 95 95 SER D 355 VAL D 367 1 13
HELIX 96 96 SER D 371 THR D 383 1 13
HELIX 97 97 ASP D 390 VAL D 407 1 18
HELIX 98 98 VAL D 407 GLN D 421 1 15
HELIX 99 99 PRO D 440 GLY D 444 5 5
HELIX 100 100 GLU D 450 PHE D 455 1 6
HELIX 101 101 GLY D 456 ASP D 460 5 5
HELIX 102 102 ASP D 460 ASN D 464 5 5
HELIX 103 103 THR D 466 GLY D 487 1 22
HELIX 104 104 ARG D 525 LEU D 539 1 15
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 ILE B 35 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 LEU B 99 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SHEET 1 CA 3 LEU C 9 ARG C 11 0
SHEET 2 CA 3 GLN C 16 ARG C 18 -1 O LEU C 17 N VAL C 10
SHEET 3 CA 3 VAL C 59 ASP C 61 1 O LEU C 60 N ARG C 18
SHEET 1 CB11 ILE C 20 ALA C 24 0
SHEET 2 CB11 GLY C 27 PRO C 36 -1 O GLY C 27 N ALA C 24
SHEET 3 CB11 TYR C 98 PRO C 104 -1 O LEU C 99 N ILE C 35
SHEET 4 CB11 VAL C 145 MET C 149 -1 O LEU C 146 N TRP C 102
SHEET 5 CB11 THR C 112 ILE C 118 1 O PRO C 113 N VAL C 145
SHEET 6 CB11 GLY C 192 GLU C 202 1 N ASP C 193 O THR C 112
SHEET 7 CB11 ARG C 224 GLN C 228 1 O ARG C 224 N LEU C 199
SHEET 8 CB11 GLN C 325 VAL C 331 1 O GLN C 325 N ALA C 225
SHEET 9 CB11 ARG C 424 PHE C 430 1 O ARG C 424 N VAL C 326
SHEET 10 CB11 GLN C 509 LEU C 513 1 O VAL C 511 N ILE C 429
SHEET 11 CB11 GLU C 519 ARG C 522 -1 O GLU C 519 N SER C 512
SHEET 1 CC 2 ALA C 38 GLU C 39 0
SHEET 2 CC 2 GLU C 51 PRO C 52 -1 O GLU C 51 N GLU C 39
SHEET 1 CD 2 VAL C 68 CYS C 69 0
SHEET 2 CD 2 LEU C 92 SER C 93 1 N SER C 93 O VAL C 68
SHEET 1 DA 3 LEU D 9 ARG D 11 0
SHEET 2 DA 3 GLN D 16 ARG D 18 -1 O LEU D 17 N VAL D 10
SHEET 3 DA 3 VAL D 59 ASP D 61 1 O LEU D 60 N ARG D 18
SHEET 1 DB11 ILE D 20 ALA D 24 0
SHEET 2 DB11 GLY D 27 PRO D 36 -1 O GLY D 27 N ALA D 24
SHEET 3 DB11 TYR D 98 PRO D 104 -1 O LEU D 99 N ILE D 35
SHEET 4 DB11 VAL D 145 MET D 149 -1 O LEU D 146 N TRP D 102
SHEET 5 DB11 THR D 112 ILE D 118 1 O PRO D 113 N VAL D 145
SHEET 6 DB11 GLY D 192 GLU D 202 1 N ASP D 193 O THR D 112
SHEET 7 DB11 ARG D 224 GLN D 228 1 O ARG D 224 N LEU D 199
SHEET 8 DB11 GLN D 325 VAL D 331 1 O GLN D 325 N ALA D 225
SHEET 9 DB11 ARG D 424 PHE D 430 1 O ARG D 424 N VAL D 326
SHEET 10 DB11 GLN D 509 LEU D 513 1 O VAL D 511 N ILE D 429
SHEET 11 DB11 GLU D 519 ARG D 522 -1 O GLU D 519 N SER D 512
SHEET 1 DC 2 VAL D 68 CYS D 69 0
SHEET 2 DC 2 LEU D 92 SER D 93 1 N SER D 93 O VAL D 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.02
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.02
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
SSBOND 7 CYS C 69 CYS C 96 1555 1555 2.04
SSBOND 8 CYS C 257 CYS C 272 1555 1555 2.02
SSBOND 9 CYS C 409 CYS C 529 1555 1555 2.04
SSBOND 10 CYS D 69 CYS D 96 1555 1555 2.03
SSBOND 11 CYS D 257 CYS D 272 1555 1555 2.04
SSBOND 12 CYS D 409 CYS D 529 1555 1555 2.03
LINK ND2 ASN A 265 C1 NAG A 560 1555 1555 1.45
LINK ND2 ASN B 265 C1 NAG B 560 1555 1555 1.46
LINK ND2 ASN B 350 C1 NAG B 561 1555 1555 1.45
LINK ND2 ASN C 265 C1 NAG C 560 1555 1555 1.45
LINK ND2 ASN D 265 C1 NAG D 560 1555 1555 1.46
LINK ND2 ASN D 350 C1 NAG D 561 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 2.77
CISPEP 2 PRO A 258 PRO A 259 0 -6.34
CISPEP 3 TYR B 105 PRO B 106 0 -1.02
CISPEP 4 CYS B 257 PRO B 258 0 -12.13
CISPEP 5 TYR C 105 PRO C 106 0 3.66
CISPEP 6 PRO C 258 PRO C 259 0 -6.72
CISPEP 7 SER C 497 PRO C 498 0 5.53
CISPEP 8 TYR D 105 PRO D 106 0 1.89
CISPEP 9 CYS D 257 PRO D 258 0 -7.45
SITE 1 AC1 22 TYR A 72 ASP A 74 TRP A 86 GLY A 121
SITE 2 AC1 22 TYR A 124 GLU A 202 SER A 203 ASP A 283
SITE 3 AC1 22 TRP A 286 HIS A 287 SER A 293 PHE A 295
SITE 4 AC1 22 TYR A 337 PHE A 338 TYR A 341 HIS A 447
SITE 5 AC1 22 ARG D 253 GLY D 256 PRO D 258 PRO D 259
SITE 6 AC1 22 GLY D 261 ALA D 262
SITE 1 AC2 11 TRP B 86 GLY B 121 TYR B 124 SER B 203
SITE 2 AC2 11 TRP B 286 SER B 293 PHE B 295 TYR B 337
SITE 3 AC2 11 PHE B 338 TYR B 341 TRP B 439
SITE 1 AC3 22 ARG B 253 PRO B 258 PRO B 259 GLY B 261
SITE 2 AC3 22 ALA B 262 TYR C 72 ASP C 74 TRP C 86
SITE 3 AC3 22 GLY C 121 TYR C 124 GLU C 202 SER C 203
SITE 4 AC3 22 ASP C 283 TRP C 286 HIS C 287 ILE C 294
SITE 5 AC3 22 PHE C 295 ARG C 296 TYR C 337 PHE C 338
SITE 6 AC3 22 TYR C 341 HOH C2017
SITE 1 AC4 12 ASP D 74 TRP D 86 GLY D 121 TYR D 124
SITE 2 AC4 12 GLU D 202 SER D 203 TRP D 286 PHE D 295
SITE 3 AC4 12 TYR D 337 PHE D 338 TYR D 341 HOH D2022
SITE 1 AC5 4 ARG D 525 ALA D 526 GLN D 527 THR D 528
SITE 1 AC6 4 ARG B 525 ALA B 526 GLN B 527 THR B 528
SITE 1 AC7 4 ARG C 525 ALA C 526 GLN C 527 THR C 528
SITE 1 AC8 1 GLN A 413
SITE 1 AC9 1 LEU A 515
SITE 1 BC1 1 GLN A 527
SITE 1 BC2 1 ARG A 356
SITE 1 BC3 1 ARG A 136
SITE 1 BC4 1 HOH B2049
SITE 1 BC5 1 ARG B 356
SITE 1 BC6 1 LYS B 332
SITE 1 BC7 1 GLN B 413
SITE 1 BC8 1 SER B 240
SITE 1 BC9 1 ARG C 356
SITE 1 CC1 1 SER C 44
SITE 1 CC2 1 ASP C 333
SITE 1 CC3 1 ARG D 45
SITE 1 CC4 1 GLN C 413
SITE 1 CC5 1 SER C 240
SITE 1 CC6 1 ARG D 356
SITE 1 CC7 1 ARG D 136
SITE 1 CC8 1 ARG C 11
SITE 1 CC9 1 ARG D 525
SITE 1 DC1 2 ASN A 265 GLU A 268
SITE 1 DC2 1 ASN B 265
SITE 1 DC3 2 ASN B 350 LEU B 353
SITE 1 DC4 2 ASN C 265 GLU C 268
SITE 1 DC5 2 ASN D 265 THR D 267
SITE 1 DC6 2 SER D 347 ASN D 350
CRYST1 137.150 175.450 224.400 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 0.007291 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005700 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004456 0.00000
TER 4212 THR A 543
TER 8420 SER B 541
TER 12606 LEU C 539
TER 16780 LEU D 539
MASTER 579 0 41 104 66 0 47 617437 4 289 168
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