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HEADER HYDROLASE 16-APR-12 4AQD
TITLE CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN BUTYRYLCHOLINESTERASE
CAVEAT 4AQD NAG A 651 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 4AQD NAG B 641 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 4AQD NAG A 671 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BUTYRYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 27-557;
COMPND 5 EC: 3.1.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: S2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMT-BIP
KEYWDS HYDROLASE, ACETYLCHOLINESTERASE, EXPRESSION, HUPRINE, SERINE
KEYWDS 2 HYDROLASE, CATALYTIC TRIAD, INSECT CELLS, GLYCOSYLATIONS
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,M.WANDHAMMER,C.RONCO,M.TROVASLET,L.JEAN,O.LOCKRIDGE,
AUTHOR 2 P.Y.RENARD,F.NACHON
REVDAT 1 04-JUL-12 4AQD 0
JRNL AUTH X.BRAZZOLOTTO,M.WANDHAMMER,C.RONCO,M.TROVASLET,L.JEAN,
JRNL AUTH 2 O.LOCKRIDGE,P.Y.RENARD,F.NACHON
JRNL TITL HUMAN BUTYRYLCHOLINESTERASE PRODUCED IN INSECT CELLS:
JRNL TITL 2 HUPRINE-BASED AFFINITY PURIFICATION, CRYSTAL STRUCTURE
JRNL REF FEBS J. 2012
JRNL REFN ESSN 1742-4658
JRNL DOI 10.1111/J.1742-4658.2012.08672.X
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.500
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.041
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.39
REMARK 3 NUMBER OF REFLECTIONS : 46071
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1652
REMARK 3 R VALUE (WORKING SET) : 0.1632
REMARK 3 FREE R VALUE : 0.2320
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.0453 - 5.3823 0.99 4716 145 0.1708 0.2153
REMARK 3 2 5.3823 - 4.2738 1.00 4532 140 0.1366 0.1978
REMARK 3 3 4.2738 - 3.7340 1.00 4533 140 0.1394 0.1991
REMARK 3 4 3.7340 - 3.3928 1.00 4464 138 0.1637 0.2370
REMARK 3 5 3.3928 - 3.1498 1.00 4439 138 0.1691 0.2790
REMARK 3 6 3.1498 - 2.9641 1.00 4461 138 0.1636 0.2576
REMARK 3 7 2.9641 - 2.8157 1.00 4412 136 0.1720 0.2477
REMARK 3 8 2.8157 - 2.6932 1.00 4399 136 0.1862 0.2446
REMARK 3 9 2.6932 - 2.5895 0.99 4426 137 0.2142 0.3217
REMARK 3 10 2.5895 - 2.5002 0.98 4308 133 0.2453 0.3135
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.362
REMARK 3 B_SOL : 61.675
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.35
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.76
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.5507
REMARK 3 B22 (A**2) : -5.2688
REMARK 3 B33 (A**2) : 0.7181
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
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 : 0.008 9212
REMARK 3 ANGLE : 1.231 12488
REMARK 3 CHIRALITY : 0.077 1386
REMARK 3 PLANARITY : 0.005 1550
REMARK 3 DIHEDRAL : 22.726 3471
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 3:315)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8838 -10.3045 -8.4504
REMARK 3 T TENSOR
REMARK 3 T11: 0.2550 T22: 0.2297
REMARK 3 T33: 0.1640 T12: -0.0305
REMARK 3 T13: -0.0073 T23: 0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 1.8420 L22: 2.0559
REMARK 3 L33: 1.7580 L12: -0.1064
REMARK 3 L13: -0.3574 L23: 0.0401
REMARK 3 S TENSOR
REMARK 3 S11: -0.0176 S12: -0.3549 S13: -0.2566
REMARK 3 S21: 0.2116 S22: -0.0029 S23: 0.0995
REMARK 3 S31: 0.2822 S32: 0.0970 S33: -0.0173
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 316:529)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2755 0.7050 -25.0057
REMARK 3 T TENSOR
REMARK 3 T11: 0.2518 T22: 0.1438
REMARK 3 T33: 0.0841 T12: -0.0554
REMARK 3 T13: -0.0240 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 2.3869 L22: 1.8759
REMARK 3 L33: 2.4847 L12: -0.5403
REMARK 3 L13: -0.7871 L23: 0.5015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: -0.0652 S13: 0.0247
REMARK 3 S21: -0.2249 S22: 0.0287 S23: -0.2040
REMARK 3 S31: -0.1154 S32: 0.3819 S33: -0.0039
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:315)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9127 25.0871 -37.2007
REMARK 3 T TENSOR
REMARK 3 T11: 0.2116 T22: 0.2144
REMARK 3 T33: 0.2053 T12: 0.0130
REMARK 3 T13: -0.0229 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 2.2006 L22: 3.2124
REMARK 3 L33: 2.4515 L12: 0.7362
REMARK 3 L13: -0.1416 L23: -0.6667
REMARK 3 S TENSOR
REMARK 3 S11: 0.1855 S12: -0.0179 S13: 0.1313
REMARK 3 S21: 0.2722 S22: 0.0193 S23: 0.5592
REMARK 3 S31: -0.0716 S32: -0.4262 S33: -0.0881
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 316:529)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2567 37.8569 -51.8162
REMARK 3 T TENSOR
REMARK 3 T11: 0.5127 T22: 0.1228
REMARK 3 T33: 0.2338 T12: -0.0139
REMARK 3 T13: -0.0571 T23: 0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 1.4876 L22: 1.7886
REMARK 3 L33: 2.6521 L12: 0.5247
REMARK 3 L13: -0.4438 L23: -0.3396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0827 S12: 0.2510 S13: 0.4237
REMARK 3 S21: -0.4997 S22: 0.0629 S23: 0.0607
REMARK 3 S31: -0.7299 S32: 0.0650 S33: -0.0501
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A BETA-ALANINE WAS MODELED AT BOND
REMARK 3 DISTANCE TO THE CATALYTIC SERINE. A PEAK OF ELECTRON DENSITY
REMARK 3 CLOSE TO A PEAK OF ELECTRON DENSITY CLOSE TO TRP82 WAS MODELED
REMARK 3 AS DUMMY ATOMS (RESIDUES UNX).
REMARK 4
REMARK 4 4AQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-12.
REMARK 100 THE PDBE ID CODE IS EBI-52078.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-11
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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97939
REMARK 200 MONOCHROMATOR : SILICON (1 1 1)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
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 : 46071
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 39.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.1
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.3
REMARK 200 R MERGE FOR SHELL (I) : 0.64
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX AUTOMR
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 20% PEG 3350, 0.2 M NH4OAC PH 7.4, AT 293 K
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 36.37500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.63000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.60000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.37500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.63000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 IN ADDITION APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -39.63000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -113.60000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ARG A -1
REMARK 465 SER A 0
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ARG B -1
REMARK 465 SER B 0
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 380 CB CG CD OE1
REMARK 480 ARG A 453 CD NE CZ NH1 NH2
REMARK 480 GLU A 506 CD OE1 OE2
REMARK 480 ILE B 4 O CG1 CG2 CD1
REMARK 480 LYS B 51 CB CG CD CE NZ
REMARK 480 SER B 53 CB OG
REMARK 480 ASP B 54 CB CG OD1 OD2
REMARK 480 GLN B 484 CG CD OE1 NE2
REMARK 480 ASN B 485 CB CG OD1 ND2
REMARK 480 ASN B 486 CG OD1 ND2
REMARK 480 GLU B 506 CG CD OE1
REMARK 480 SER B 507 CB OG
REMARK 480 ARG B 509 NE CZ NH1 NH2
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 ND2 ASN A 17 C2 NAG A 601 2.14
REMARK 500 OG SER A 198 C BAL A 550 2.07
REMARK 500 NH2B ARG A 465 O HOH A 2129 2.17
REMARK 500 OE1 GLU A 497 O HOH A 2145 2.12
REMARK 500 ND2 ASN B 17 C2 NAG B 601 1.64
REMARK 500 ND2 ASN B 57 C2 NAG B 611 2.16
REMARK 500 OG SER B 198 C BAL B 550 2.08
REMARK 500 ND2 ASN B 241 C2 NAG B 631 2.11
REMARK 500 O ASN B 455 O1 EDO B 1534 2.13
REMARK 500 O4 NAG A 651 X UNX B 1548 1.94
REMARK 500 X UNX A 1542 X UNX A 1544 2.04
REMARK 500 X UNX B 1542 X UNX B 1544 1.80
REMARK 500 X UNX B 1543 X UNX B 1545 2.16
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 43 -13.39 76.55
REMARK 500 THR A 50 -83.70 -75.56
REMARK 500 ASP A 54 -150.46 59.93
REMARK 500 ASN A 106 55.60 -160.24
REMARK 500 ALA A 162 68.27 -161.18
REMARK 500 SER A 198 -117.64 60.88
REMARK 500 GLU A 255 -74.98 -45.84
REMARK 500 ASP A 297 -72.74 -105.40
REMARK 500 ASP A 324 60.43 -119.85
REMARK 500 ARG A 381 90.99 24.40
REMARK 500 PHE A 398 -61.89 -127.22
REMARK 500 GLU A 482 -74.29 -109.91
REMARK 500 ASN A 485 133.01 82.14
REMARK 500 PHE B 43 -16.24 81.02
REMARK 500 LYS B 51 153.18 -49.52
REMARK 500 ASP B 54 -157.69 -75.39
REMARK 500 ASN B 106 52.76 -155.55
REMARK 500 ASP B 129 109.16 -57.38
REMARK 500 ALA B 162 75.95 -161.39
REMARK 500 SER B 198 -115.24 58.91
REMARK 500 THR B 218 -55.66 -120.78
REMARK 500 ASP B 297 -77.91 -127.68
REMARK 500 ASP B 324 62.15 -118.71
REMARK 500 TYR B 332 38.32 -99.92
REMARK 500 SER B 338 142.03 -174.92
REMARK 500 PHE B 398 -63.48 -128.98
REMARK 500 ASN B 455 -154.43 66.35
REMARK 500 TYR B 456 151.25 78.83
REMARK 500 THR B 483 -142.98 -83.23
REMARK 500 GLN B 484 95.44 51.65
REMARK 500 ASN B 485 -20.07 -38.90
REMARK 500 ASN B 486 -76.90 -65.61
REMARK 500 SER B 487 -148.69 50.38
REMARK 500 THR B 488 6.61 -170.29
REMARK 500 SER B 489 97.42 54.98
REMARK 500 GLU B 506 77.36 -101.37
REMARK 500 SER B 507 112.16 75.56
REMARK 500 PRO B 527 2.96 -61.95
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 BAL A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1643
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BAL B 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1642
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 17 RESIDUES 601 TO 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 57 RESIDUES 611 TO 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 106 RESIDUES 621 TO 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 241 RESIDUES 631 TO 633
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 651 BOUND TO ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 481 RESIDUES 671 TO 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 486 RESIDUES 681 TO 683
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 601 BOUND TO ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 611 BOUND TO ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 621 BOUND TO ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 241 RESIDUES 631 TO 633
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 256 RESIDUES 641 TO 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 651 BOUND TO ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 455 RESIDUES 661 TO 663
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 671 BOUND TO ASN B 481
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 INCOMPLEX WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE
REMARK 900 ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (
REMARK 900 DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900 REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED
REMARK 900 BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 10MM HGCL2
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH SULFATE
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FLUORIDE ANION
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH VX
REMARK 900 RELATED ID: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VX
REMARK 900 RELATED ID: 2XQG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VR
REMARK 900 RELATED ID: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC CVX
REMARK 900 RELATED ID: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 2XQK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(S)
REMARK 900 RELATED ID: 2Y1K RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (12H SOAK): PHOSPHOSERINE ADDUCT
DBREF 4AQD A -1 529 UNP P06276 CHLE_HUMAN 27 557
DBREF 4AQD B -1 529 UNP P06276 CHLE_HUMAN 27 557
SEQRES 1 A 531 ARG SER GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY
SEQRES 2 A 531 LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR
SEQRES 3 A 531 VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 A 531 LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR
SEQRES 5 A 531 LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN
SEQRES 6 A 531 SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE
SEQRES 7 A 531 HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER
SEQRES 8 A 531 GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO
SEQRES 9 A 531 LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 A 531 GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR
SEQRES 11 A 531 ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL
SEQRES 12 A 531 VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU
SEQRES 13 A 531 ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 14 A 531 LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS
SEQRES 15 A 531 ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR
SEQRES 16 A 531 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU
SEQRES 17 A 531 HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG
SEQRES 18 A 531 ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA
SEQRES 19 A 531 VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN
SEQRES 20 A 531 LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR
SEQRES 21 A 531 GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU
SEQRES 22 A 531 ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR
SEQRES 23 A 531 PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP
SEQRES 24 A 531 PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY
SEQRES 25 A 531 GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS
SEQRES 26 A 531 ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY
SEQRES 27 A 531 PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU
SEQRES 28 A 531 PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER
SEQRES 29 A 531 GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP
SEQRES 30 A 531 TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA
SEQRES 31 A 531 LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO
SEQRES 32 A 531 ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN
SEQRES 33 A 531 ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS
SEQRES 34 A 531 LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR
SEQRES 35 A 531 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG
SEQRES 36 A 531 ASP ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER
SEQRES 37 A 531 ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN
SEQRES 38 A 531 PRO ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL
SEQRES 39 A 531 PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR
SEQRES 40 A 531 GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN
SEQRES 41 A 531 CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 531 ARG SER GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY
SEQRES 2 B 531 LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR
SEQRES 3 B 531 VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 B 531 LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR
SEQRES 5 B 531 LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN
SEQRES 6 B 531 SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE
SEQRES 7 B 531 HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER
SEQRES 8 B 531 GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO
SEQRES 9 B 531 LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 B 531 GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR
SEQRES 11 B 531 ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL
SEQRES 12 B 531 VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU
SEQRES 13 B 531 ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 14 B 531 LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS
SEQRES 15 B 531 ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR
SEQRES 16 B 531 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU
SEQRES 17 B 531 HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG
SEQRES 18 B 531 ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA
SEQRES 19 B 531 VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN
SEQRES 20 B 531 LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR
SEQRES 21 B 531 GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU
SEQRES 22 B 531 ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR
SEQRES 23 B 531 PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP
SEQRES 24 B 531 PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY
SEQRES 25 B 531 GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS
SEQRES 26 B 531 ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY
SEQRES 27 B 531 PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU
SEQRES 28 B 531 PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER
SEQRES 29 B 531 GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP
SEQRES 30 B 531 TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA
SEQRES 31 B 531 LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO
SEQRES 32 B 531 ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN
SEQRES 33 B 531 ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS
SEQRES 34 B 531 LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR
SEQRES 35 B 531 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG
SEQRES 36 B 531 ASP ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER
SEQRES 37 B 531 ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN
SEQRES 38 B 531 PRO ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL
SEQRES 39 B 531 PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR
SEQRES 40 B 531 GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN
SEQRES 41 B 531 CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL
HET BAL A 550 6
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 611 14
HET NAG A 612 14
HET FUL A 613 10
HET NAG A 621 14
HET NAG A 622 14
HET NAG A 631 14
HET NAG A 632 14
HET FUL A 633 10
HET NAG A 651 14
HET NAG A 671 14
HET NAG A 672 14
HET MAN A 673 11
HET NAG A 681 14
HET NAG A 682 14
HET FUL A 683 10
HET PG4 A1530 13
HET PG4 A1531 13
HET EDO A1532 4
HET EDO A1533 4
HET EDO A1534 4
HET EDO A1535 4
HET EDO A1536 4
HET EDO A1537 4
HET EDO A1538 4
HET EDO A1539 4
HET EDO A1540 4
HET CL A1545 1
HET CL A1546 1
HET CL A1547 1
HET GLY A1643 5
HET BAL B 550 6
HET NAG B 601 14
HET NAG B 611 14
HET NAG B 621 14
HET NAG B 631 14
HET NAG B 632 14
HET FUL B 633 10
HET NAG B 641 14
HET NAG B 642 14
HET FUL B 643 10
HET NAG B 651 14
HET NAG B 661 14
HET NAG B 662 14
HET FUL B 663 10
HET NAG B 671 14
HET PEG B1530 7
HET PEG B1531 7
HET EDO B1532 4
HET EDO B1533 4
HET EDO B1534 4
HET EDO B1535 4
HET EDO B1536 4
HET EDO B1537 4
HET EDO B1538 4
HET EDO B1539 4
HET EDO B1540 4
HET EDO B1541 4
HET CL B1546 1
HET CL B1547 1
HET CL B1549 1
HET CL B1550 1
HET GLY B1642 5
HET UNX A1541
HET UNX A1542
HET UNX A1543
HET UNX A1544
HET UNX A1548
HET UNX B1542
HET UNX B1543
HET UNX B1544
HET UNX B1545
HET UNX B1548
HETNAM BAL BETA-ALANINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM CL CHLORIDE ION
HETNAM GLY GLYCINE
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 BAL 2(C3 H7 N O2)
FORMUL 3 NAG 24(C8 H15 N O6)
FORMUL 4 FUL 6(C6 H12 O5)
FORMUL 5 MAN C6 H12 O6
FORMUL 6 PG4 2(C8 H18 O5)
FORMUL 7 EDO 19(C2 H6 O2)
FORMUL 9 CL 7(CL 1-)
FORMUL 10 PEG 2(C4 H10 O3)
FORMUL 11 UNX 10(X)
FORMUL 12 GLY 2(C2 H5 N O2)
FORMUL 13 HOH *278(H2 O)
HELIX 1 1 LEU A 38 ARG A 42 5 5
HELIX 2 2 PHE A 76 MET A 81 1 6
HELIX 3 3 LEU A 125 ASP A 129 5 5
HELIX 4 4 GLY A 130 ARG A 138 1 9
HELIX 5 5 VAL A 148 LEU A 154 1 7
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 SER A 198 SER A 210 1 13
HELIX 9 9 SER A 235 THR A 250 1 16
HELIX 10 10 ASN A 256 ARG A 265 1 10
HELIX 11 11 ASP A 268 LEU A 274 1 7
HELIX 12 12 ASN A 275 VAL A 279 5 5
HELIX 13 13 MET A 302 LEU A 309 1 8
HELIX 14 14 GLY A 326 VAL A 331 1 6
HELIX 15 15 THR A 346 PHE A 358 1 13
HELIX 16 16 SER A 362 TYR A 373 1 12
HELIX 17 17 GLU A 383 PHE A 398 1 16
HELIX 18 18 PHE A 398 GLU A 411 1 14
HELIX 19 19 PRO A 431 GLY A 435 5 5
HELIX 20 20 GLU A 441 PHE A 446 1 6
HELIX 21 21 GLY A 447 GLU A 451 5 5
HELIX 22 22 GLU A 451 ASN A 455 5 5
HELIX 23 23 THR A 457 GLY A 478 1 22
HELIX 24 24 ARG A 515 PHE A 525 1 11
HELIX 25 25 PHE A 526 VAL A 529 5 4
HELIX 26 26 LEU B 38 ARG B 42 5 5
HELIX 27 27 PHE B 76 MET B 81 1 6
HELIX 28 28 LEU B 125 ASP B 129 5 5
HELIX 29 29 GLY B 130 ARG B 138 1 9
HELIX 30 30 VAL B 148 LEU B 154 1 7
HELIX 31 31 ASN B 165 ILE B 182 1 18
HELIX 32 32 ALA B 183 PHE B 185 5 3
HELIX 33 33 SER B 198 LEU B 208 1 11
HELIX 34 34 SER B 210 PHE B 217 5 8
HELIX 35 35 SER B 235 THR B 250 1 16
HELIX 36 36 ASN B 256 LYS B 267 1 12
HELIX 37 37 ASP B 268 LEU B 274 1 7
HELIX 38 38 ASN B 275 VAL B 279 5 5
HELIX 39 39 MET B 302 GLY B 310 1 9
HELIX 40 40 GLY B 326 VAL B 331 1 6
HELIX 41 41 THR B 346 PHE B 358 1 13
HELIX 42 42 SER B 362 TYR B 373 1 12
HELIX 43 43 GLU B 383 PHE B 398 1 16
HELIX 44 44 PHE B 398 GLU B 411 1 14
HELIX 45 45 PRO B 431 GLY B 435 5 5
HELIX 46 46 GLU B 441 PHE B 446 1 6
HELIX 47 47 GLY B 447 GLU B 451 5 5
HELIX 48 48 THR B 457 GLY B 478 1 22
HELIX 49 49 ARG B 515 PHE B 525 1 11
HELIX 50 50 PHE B 526 VAL B 529 5 4
SHEET 1 AA 3 ILE A 5 THR A 8 0
SHEET 2 AA 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA 3 TRP A 56 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AB11 MET A 16 VAL A 20 0
SHEET 2 AB11 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 AB11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AB11 ILE A 140 MET A 144 -1 O VAL A 141 N TRP A 98
SHEET 5 AB11 ALA A 107 ILE A 113 1 O THR A 108 N ILE A 140
SHEET 6 AB11 GLY A 187 GLU A 197 1 N ASN A 188 O ALA A 107
SHEET 7 AB11 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AB11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AB11 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AB11 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AB11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AC 2 SER A 64 CYS A 65 0
SHEET 2 AC 2 LEU A 88 SER A 89 1 N SER A 89 O SER A 64
SHEET 1 BA 3 ILE B 5 ALA B 7 0
SHEET 2 BA 3 LYS B 12 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 BA 3 TRP B 56 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 BB11 MET B 16 VAL B 20 0
SHEET 2 BB11 GLY B 23 PRO B 32 -1 O GLY B 23 N VAL B 20
SHEET 3 BB11 TYR B 94 PRO B 100 -1 O LEU B 95 N ILE B 31
SHEET 4 BB11 ILE B 140 MET B 144 -1 O VAL B 141 N TRP B 98
SHEET 5 BB11 ALA B 107 ILE B 113 1 O THR B 108 N ILE B 140
SHEET 6 BB11 GLY B 187 GLU B 197 1 N ASN B 188 O ALA B 107
SHEET 7 BB11 ARG B 219 GLN B 223 1 O ARG B 219 N LEU B 194
SHEET 8 BB11 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 BB11 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 BB11 LYS B 499 LEU B 503 1 O LEU B 501 N TYR B 420
SHEET 11 BB11 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SHEET 1 BC 2 SER B 64 CYS B 65 0
SHEET 2 BC 2 LEU B 88 SER B 89 1 N SER B 89 O SER B 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.06
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.07
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.05
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.06
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.06
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 57 C1 NAG A 611 1555 1555 1.45
LINK ND2 ASN A 106 C1 NAG A 621 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 631 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A 651 1555 1555 1.44
LINK ND2 ASN A 481 C1 NAG A 671 1555 1555 1.45
LINK ND2 ASN A 486 C1 NAG A 681 1555 1555 1.44
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.45
LINK O6 NAG A 611 C1 FUL A 613 1555 1555 1.44
LINK O4 NAG A 611 C1 NAG A 612 1555 1555 1.45
LINK O4 NAG A 621 C1 NAG A 622 1555 1555 1.46
LINK O6 NAG A 631 C1 FUL A 633 1555 1555 1.45
LINK O4 NAG A 631 C1 NAG A 632 1555 1555 1.45
LINK O4 NAG A 671 C1 NAG A 672 1555 1555 1.44
LINK O4 NAG A 672 C1 MAN A 673 1555 1555 1.45
LINK O6 NAG A 681 C1 FUL A 683 1555 1555 1.44
LINK O4 NAG A 681 C1 NAG A 682 1555 1555 1.45
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.45
LINK ND2 ASN B 57 C1 NAG B 611 1555 1555 1.44
LINK ND2 ASN B 106 C1 NAG B 621 1555 1555 1.45
LINK ND2 ASN B 241 C1 NAG B 631 1555 1555 1.45
LINK ND2 ASN B 256 C1 NAG B 641 1555 1555 1.45
LINK ND2 ASN B 341 C1 NAG B 651 1555 1555 1.46
LINK ND2 ASN B 455 C1 NAG B 661 1555 1555 1.47
LINK ND2 ASN B 481 C1 NAG B 671 1555 1555 1.45
LINK O6 NAG B 631 C1 FUL B 633 1555 1555 1.45
LINK O4 NAG B 631 C1 NAG B 632 1555 1555 1.44
LINK O6 NAG B 641 C1 FUL B 643 1555 1555 1.43
LINK O4 NAG B 641 C1 NAG B 642 1555 1555 1.44
LINK O6 NAG B 661 C1 FUL B 663 1555 1555 1.46
LINK O4 NAG B 661 C1 NAG B 662 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 -0.57
CISPEP 2 ASP A 379 GLN A 380 0 -3.65
CISPEP 3 ALA B 101 PRO B 102 0 -0.70
SITE 1 AC1 6 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC1 6 HIS A 438 HOH A2156
SITE 1 AC2 2 ASN A 455 NAG A 602
SITE 1 AC3 7 LEU A 307 GLU A 308 LYS A 408 GLU A 411
SITE 2 AC3 7 TRP A 412 LYS B 248 GLY B 251
SITE 1 AC4 3 CYS A 400 PRO A 401 THR A 523
SITE 1 AC5 4 PHE A 21 LEU A 450 GLU A 451 ARG A 452
SITE 1 AC6 3 HIS A 77 LYS A 427 GLU A 443
SITE 1 AC7 2 LYS A 494 THR A 496
SITE 1 AC8 4 HIS A 423 ASN A 504 THR A 505 HOH A2123
SITE 1 AC9 4 ASN A 479 TRP A 490 HOH A2137 GLN B 71
SITE 1 BC1 7 LEU A 29 GLY A 30 TRP A 56 ASN A 57
SITE 2 BC1 7 LYS A 60 ALA A 62 HOH A2021
SITE 1 BC2 3 GLY A 116 THR A 120 HOH A2156
SITE 1 BC3 4 TYR A 33 SER A 48 LEU A 49 LYS A 180
SITE 1 BC4 1 ARG A 465
SITE 1 BC5 4 ARG A 470 ASN A 481 SER A 489 TRP A 490
SITE 1 BC6 1 ARG A 386
SITE 1 BC7 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 BC7 5 LYS A 131
SITE 1 BC8 6 GLY B 116 GLY B 117 SER B 198 ALA B 199
SITE 2 BC8 6 HIS B 438 HOH B2070
SITE 1 BC9 7 HIS B 207 LEU B 208 LEU B 209 SER B 210
SITE 2 BC9 7 HIS B 214 GLN B 311 LYS B 313
SITE 1 CC1 8 HIS B 77 MET B 81 SER B 425 LYS B 427
SITE 2 CC1 8 LEU B 428 PRO B 429 GLU B 443 HOH B2114
SITE 1 CC2 4 SER A 368 PHE A 371 HIS A 372 PHE B 525
SITE 1 CC3 3 TYR B 33 LEU B 49 LYS B 180
SITE 1 CC4 6 PRO B 449 GLU B 451 ARG B 452 ASN B 455
SITE 2 CC4 6 TYR B 456 GLU B 461
SITE 1 CC5 3 ASP B 295 GLU B 497 LYS B 499
SITE 1 CC6 1 PRO B 285
SITE 1 CC7 4 ARG B 265 ASN B 266 LYS B 267 ASP B 268
SITE 1 CC8 5 THR B 284 PHE B 357 TYR B 396 ASN B 397
SITE 2 CC8 5 HOH B2116
SITE 1 CC9 8 GLN B 35 PRO B 37 LEU B 41 LYS B 44
SITE 2 CC9 8 LYS B 45 PRO B 46 GLN B 47 ARG B 147
SITE 1 DC1 4 ASN B 68 ASP B 70 THR B 120 HOH B2117
SITE 1 DC2 5 LYS B 60 TYR B 61 ASN B 63 THR B 86
SITE 2 DC2 5 ASP B 87
SITE 1 DC3 2 TRP B 231 VAL B 288
SITE 1 DC4 2 LYS B 458 ILE B 462
SITE 1 DC5 3 LEU B 18 ASP B 129 LYS B 131
SITE 1 DC6 3 ILE A 4 ASN A 17 PG4 A1530
SITE 1 DC7 4 ARG A 14 ILE A 55 ASN A 57 LYS B 12
SITE 1 DC8 3 ASN A 106 ASN A 188 LYS A 190
SITE 1 DC9 7 ASN A 241 ASN A 245 LYS A 248 PHE A 278
SITE 2 DC9 7 PRO A 281 NAG B 661 FUL B 663
SITE 1 EC1 3 SER A 338 ASN A 341 HOH A2158
SITE 1 EC2 10 TYR A 477 ASN A 479 ASN A 481 GLU A 482
SITE 2 EC2 10 THR A 483 GLN A 484 HOH A2159 ASP B 87
SITE 3 EC2 10 LEU B 88 GLN B 270
SITE 1 EC3 6 ASN A 486 SER A 487 THR A 488 GLU A 506
SITE 2 EC3 6 THR A 508 GLY B 75
SITE 1 EC4 2 ASN B 17 THR B 24
SITE 1 EC5 2 ARG B 14 ASN B 57
SITE 1 EC6 3 ASN B 106 ASN B 188 LYS B 190
SITE 1 EC7 7 TYR B 237 ASN B 241 ASN B 245 LYS B 248
SITE 2 EC7 7 LEU B 249 PHE B 278 TYR B 282
SITE 1 EC8 4 GLU B 255 ASN B 256 GLU B 259 GLU B 411
SITE 1 EC9 3 SER B 338 ASN B 341 ASN B 342
SITE 1 FC1 6 TYR A 237 LEU A 244 NAG A 631 LYS B 427
SITE 2 FC1 6 ASP B 454 ASN B 455
SITE 1 FC2 2 TYR B 477 ASN B 481
CRYST1 72.750 79.260 227.200 90.00 90.00 90.00 P 21 21 21 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 0.013746 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004401 0.00000
TER 4223 VAL A 529
TER 8415 VAL B 529
MASTER 679 0 75 50 32 0 64 6 9253 2 572 82
END |