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HEADER HYDROLASE 14-NOV-17 6EZ2
TITLE HUMAN BUTYRYLCHOLINESTERASE CARBAMYLATED.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227
KEYWDS BUTYRYLCHOLINESTERASE, RIVASTIGMINE ANALOGUES, ALZHEIMER DISEASE,
KEYWDS 2 CENTRAL NERVOUS SYSTEM, INHIBITOR., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,E.DE LA MORA,S.N.DIGHE,B.P.ROSS
REVDAT 1 12-DEC-18 6EZ2 0
JRNL AUTH S.N.DIGHE,E.DE LA MORA,S.CHAN,S.KANTHAM,M.MCCOLL,
JRNL AUTH 2 S.K.VELIYATH,J.A.MILES,Z.NESSAR,R.P.MCGEARY,I.SILMAN,
JRNL AUTH 3 M.O.PARAT,M.WEIK,X.BRAZZOLOTTO,B.P.ROS
JRNL TITL ANALOGUES OF RIVASTIGMINE AND NAP FOR THE CNS DELIVERY OF
JRNL TITL 2 POLYPHENOLS WITH PUTATIVE ALZHEIMER DISEASE-MODIFYING
JRNL TITL 3 PROPERTIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 39398
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
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 39.9744 - 5.3962 0.99 5028 155 0.1976 0.2276
REMARK 3 2 5.3962 - 4.2847 1.00 4830 150 0.1556 0.1777
REMARK 3 3 4.2847 - 3.7436 1.00 4801 148 0.1566 0.1701
REMARK 3 4 3.7436 - 3.4015 1.00 4770 148 0.1777 0.2477
REMARK 3 5 3.4015 - 3.1578 1.00 4716 146 0.2081 0.2519
REMARK 3 6 3.1578 - 2.9717 1.00 4750 147 0.2104 0.2957
REMARK 3 7 2.9717 - 2.8229 1.00 4720 146 0.2344 0.3309
REMARK 3 8 2.8229 - 2.7000 0.97 4601 142 0.2715 0.3262
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 8651
REMARK 3 ANGLE : 1.159 11816
REMARK 3 CHIRALITY : 0.091 1317
REMARK 3 PLANARITY : 0.005 1520
REMARK 3 DIHEDRAL : 19.190 3050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5318 6.1289 16.5545
REMARK 3 T TENSOR
REMARK 3 T11: 0.3344 T22: 0.4199
REMARK 3 T33: 0.2962 T12: 0.0465
REMARK 3 T13: -0.0087 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.0675 L22: 1.9388
REMARK 3 L33: 2.7197 L12: -0.4073
REMARK 3 L13: 0.5694 L23: -0.6516
REMARK 3 S TENSOR
REMARK 3 S11: 0.1022 S12: 0.3342 S13: -0.0900
REMARK 3 S21: -0.1224 S22: -0.1570 S23: -0.0803
REMARK 3 S31: 0.1330 S32: 0.2860 S33: 0.0209
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1238 -30.1307 44.2079
REMARK 3 T TENSOR
REMARK 3 T11: 0.3815 T22: 0.3731
REMARK 3 T33: 0.3597 T12: -0.0386
REMARK 3 T13: -0.0185 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 1.8978 L22: 3.0067
REMARK 3 L33: 3.1968 L12: -0.4240
REMARK 3 L13: 0.3363 L23: 0.1670
REMARK 3 S TENSOR
REMARK 3 S11: 0.1728 S12: 0.0279 S13: -0.1651
REMARK 3 S21: 0.0910 S22: 0.0412 S23: 0.0869
REMARK 3 S31: 0.3555 S32: -0.1685 S33: -0.1880
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 6EZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39535
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 39.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.02500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.690
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4AQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM AMMONIUM ACETATE, PH 7.40, 13%
REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 38.00500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.74500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.74500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.00500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.97000
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: MONOMERIC
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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 ASP B 3
REMARK 465 SER B 53
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 LYS A 9 NZ
REMARK 470 LYS A 44 NZ
REMARK 470 SER A 53 OG
REMARK 470 LYS A 60 CE NZ
REMARK 470 LYS A 103 CD CE NZ
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 ARG A 138 CD NE CZ NH1 NH2
REMARK 470 LYS A 180 CE NZ
REMARK 470 LYS A 190 CE NZ
REMARK 470 TYR A 237 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 240 NE CZ NH1 NH2
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 470 GLU A 255 CG CD OE1 OE2
REMARK 470 GLU A 259 CG CD OE1 OE2
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 ASP A 268 CG OD1 OD2
REMARK 470 GLN A 270 CG CD OE1 NE2
REMARK 470 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 308 OE1 OE2
REMARK 470 LYS A 323 NZ
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 GLU A 352 OE1 OE2
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 PHE A 364 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 366 NZ
REMARK 470 LYS A 408 CE NZ
REMARK 470 LYS A 427 NZ
REMARK 470 GLU A 432 CD OE1 OE2
REMARK 470 ARG A 453 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 458 CD CE NZ
REMARK 470 GLU A 506 CG CD OE1 OE2
REMARK 470 LYS A 513 NZ
REMARK 470 LYS A 528 CG CD CE NZ
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 GLN B 35 CG CD OE1 NE2
REMARK 470 ARG B 40 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 44 CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 ASP B 54 CG OD1 OD2
REMARK 470 LYS B 60 CE NZ
REMARK 470 LYS B 103 NZ
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 GLU B 161 OE1 OE2
REMARK 470 LYS B 180 CE NZ
REMARK 470 TYR B 237 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 238 CG CD OE1 OE2
REMARK 470 ARG B 240 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 248 CG CD CE NZ
REMARK 470 GLU B 255 CG CD OE1 OE2
REMARK 470 LYS B 262 CG CD CE NZ
REMARK 470 TYR B 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 308 CD OE1 OE2
REMARK 470 LYS B 314 NZ
REMARK 470 LYS B 323 CE NZ
REMARK 470 LYS B 339 NZ
REMARK 470 ASN B 342 CG OD1 ND2
REMARK 470 LYS B 348 CG CD CE NZ
REMARK 470 LYS B 355 CG CD CE NZ
REMARK 470 PHE B 364 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 380 CG CD OE1 NE2
REMARK 470 LYS B 407 NZ
REMARK 470 LYS B 427 NZ
REMARK 470 LYS B 469 CG CD CE NZ
REMARK 470 LYS B 476 CG CD CE NZ
REMARK 470 THR B 483 OG1 CG2
REMARK 470 GLN B 484 CG CD OE1 NE2
REMARK 470 GLU B 506 CG CD OE1 OE2
REMARK 470 LYS B 513 CD CE NZ
REMARK 470 LYS B 528 NZ
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 NH1 ARG B 381 OE1 GLU B 383 1.52
REMARK 500 O ASP A 378 N GLN A 380 2.08
REMARK 500 O PHE B 217 NZ LYS B 313 2.10
REMARK 500 ND2 ASN A 341 O5 NAG A 605 2.15
REMARK 500 OE1 GLN B 119 O HOH B 701 2.18
REMARK 500 O PHE A 217 NZ LYS A 313 2.18
REMARK 500 OE2 GLU B 451 O HOH B 702 2.19
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 ILE B 55 CG1 - CB - CG2 ANGL. DEV. = -18.9 DEGREES
REMARK 500 ILE B 55 CA - CB - CG1 ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG B 381 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 SER B 489 N - CA - CB ANGL. DEV. = -15.6 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 THR A 50 -94.52 -104.76
REMARK 500 ASP A 54 -168.06 -174.78
REMARK 500 ASN A 106 49.92 -147.74
REMARK 500 PHE A 153 10.69 -141.92
REMARK 500 ALA A 162 73.18 -162.35
REMARK 500 BXT A 198 -121.34 55.95
REMARK 500 TYR A 282 160.62 173.83
REMARK 500 THR A 284 142.53 -34.54
REMARK 500 ASP A 297 -67.64 -140.86
REMARK 500 TYR A 332 44.26 -105.55
REMARK 500 ASP A 379 -16.77 -17.07
REMARK 500 GLU A 383 -4.55 -51.86
REMARK 500 PHE A 398 -60.65 -136.60
REMARK 500 PRO A 480 45.09 -77.56
REMARK 500 SER B 89 146.09 -170.18
REMARK 500 ASN B 106 47.80 -144.10
REMARK 500 PHE B 153 10.66 -142.38
REMARK 500 ALA B 162 71.78 -161.23
REMARK 500 BXT B 198 -121.33 55.97
REMARK 500 ASP B 297 -67.84 -139.90
REMARK 500 TYR B 332 42.81 -106.59
REMARK 500 GLN B 380 0.69 81.41
REMARK 500 PHE B 398 -61.48 -136.51
REMARK 500 GLU B 411 4.59 -69.32
REMARK 500 ASN B 455 6.88 84.05
REMARK 500 PRO B 480 44.29 -75.51
REMARK 500 ASN B 486 -30.76 -38.15
REMARK 500 SER B 507 -66.44 -127.38
REMARK 500 ARG B 509 -156.38 -85.47
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 GOL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound
REMARK 800 to ASN A 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through NAG A 608 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 606 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 607 bound
REMARK 800 to ASN B 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLU B 197 and BXT B
REMARK 800 198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BXT B 198 and ALA B
REMARK 800 199
DBREF 6EZ2 A 3 529 UNP P06276 CHLE_HUMAN 31 557
DBREF 6EZ2 B 3 529 UNP P06276 CHLE_HUMAN 31 557
SEQADV 6EZ2 BXT A 198 UNP P06276 SER 226 CONFLICT
SEQADV 6EZ2 BXT B 198 UNP P06276 SER 226 CONFLICT
SEQRES 1 A 527 ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY
SEQRES 2 A 527 MET ASN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE
SEQRES 3 A 527 LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU
SEQRES 4 A 527 ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP
SEQRES 5 A 527 ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN
SEQRES 6 A 527 ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU
SEQRES 7 A 527 MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU
SEQRES 8 A 527 TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN
SEQRES 9 A 527 ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN
SEQRES 10 A 527 THR GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE
SEQRES 11 A 527 LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN
SEQRES 12 A 527 TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY
SEQRES 13 A 527 ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN
SEQRES 14 A 527 GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA
SEQRES 15 A 527 PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU
SEQRES 16 A 527 BXT ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER
SEQRES 17 A 527 PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN
SEQRES 18 A 527 SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU
SEQRES 19 A 527 TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU
SEQRES 20 A 527 THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS
SEQRES 21 A 527 CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN
SEQRES 22 A 527 GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL
SEQRES 23 A 527 ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP
SEQRES 24 A 527 MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS
SEQRES 25 A 527 THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR
SEQRES 26 A 527 ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP
SEQRES 27 A 527 ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY
SEQRES 28 A 527 LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS
SEQRES 29 A 527 GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP
SEQRES 30 A 527 GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL
SEQRES 31 A 527 VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE
SEQRES 32 A 527 THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE
SEQRES 33 A 527 TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO
SEQRES 34 A 527 GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE
SEQRES 35 A 527 VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN TYR THR
SEQRES 36 A 527 LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG
SEQRES 37 A 527 TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN GLU THR
SEQRES 38 A 527 GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS SER THR
SEQRES 39 A 527 GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG
SEQRES 40 A 527 ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP
SEQRES 41 A 527 THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 527 ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY
SEQRES 2 B 527 MET ASN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE
SEQRES 3 B 527 LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU
SEQRES 4 B 527 ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP
SEQRES 5 B 527 ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN
SEQRES 6 B 527 ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU
SEQRES 7 B 527 MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU
SEQRES 8 B 527 TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN
SEQRES 9 B 527 ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN
SEQRES 10 B 527 THR GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE
SEQRES 11 B 527 LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN
SEQRES 12 B 527 TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY
SEQRES 13 B 527 ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN
SEQRES 14 B 527 GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA
SEQRES 15 B 527 PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU
SEQRES 16 B 527 BXT ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER
SEQRES 17 B 527 PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN
SEQRES 18 B 527 SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU
SEQRES 19 B 527 TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU
SEQRES 20 B 527 THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS
SEQRES 21 B 527 CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN
SEQRES 22 B 527 GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL
SEQRES 23 B 527 ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP
SEQRES 24 B 527 MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS
SEQRES 25 B 527 THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR
SEQRES 26 B 527 ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP
SEQRES 27 B 527 ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY
SEQRES 28 B 527 LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS
SEQRES 29 B 527 GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP
SEQRES 30 B 527 GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL
SEQRES 31 B 527 VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE
SEQRES 32 B 527 THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE
SEQRES 33 B 527 TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO
SEQRES 34 B 527 GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE
SEQRES 35 B 527 VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN TYR THR
SEQRES 36 B 527 LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG
SEQRES 37 B 527 TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN GLU THR
SEQRES 38 B 527 GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS SER THR
SEQRES 39 B 527 GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG
SEQRES 40 B 527 ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP
SEQRES 41 B 527 THR SER PHE PHE PRO LYS VAL
HET BXT A 198 12
HET BXT B 198 12
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET GOL A 609 6
HET CL A 610 1
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET NAG B 606 14
HET NAG B 607 14
HET EDO B 608 4
HET EDO B 609 4
HET GOL B 610 6
HETNAM BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-
HETNAM 2 BXT PROPANOIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 BXT 2(C7 H14 N2 O4)
FORMUL 3 NAG 15(C8 H15 N O6)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 11 CL CL 1-
FORMUL 19 EDO 2(C2 H6 O2)
FORMUL 22 HOH *122(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 BXT A 198 LEU A 208 1 11
HELIX 9 AA9 SER A 210 HIS A 214 5 5
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 ASN A 266 1 11
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 MET A 302 LEU A 309 1 8
HELIX 14 AB5 GLY A 326 VAL A 331 1 6
HELIX 15 AB6 THR A 346 PHE A 358 1 13
HELIX 16 AB7 SER A 362 TYR A 373 1 12
HELIX 17 AB8 GLU A 383 PHE A 398 1 16
HELIX 18 AB9 PHE A 398 GLU A 411 1 14
HELIX 19 AC1 PRO A 431 GLY A 435 5 5
HELIX 20 AC2 GLU A 441 PHE A 446 1 6
HELIX 21 AC3 GLY A 447 GLU A 451 5 5
HELIX 22 AC4 THR A 457 GLY A 478 1 22
HELIX 23 AC5 ARG A 515 PHE A 525 1 11
HELIX 24 AC6 PHE A 526 VAL A 529 5 4
HELIX 25 AC7 LEU B 38 ARG B 42 5 5
HELIX 26 AC8 PHE B 76 MET B 81 1 6
HELIX 27 AC9 LEU B 125 ASP B 129 5 5
HELIX 28 AD1 GLY B 130 ARG B 138 1 9
HELIX 29 AD2 GLY B 149 LEU B 154 1 6
HELIX 30 AD3 ASN B 165 ILE B 182 1 18
HELIX 31 AD4 ALA B 183 PHE B 185 5 3
HELIX 32 AD5 BXT B 198 LEU B 208 1 11
HELIX 33 AD6 SER B 210 PHE B 217 5 8
HELIX 34 AD7 SER B 235 GLY B 251 1 17
HELIX 35 AD8 ASN B 256 ARG B 265 1 10
HELIX 36 AD9 ASP B 268 ALA B 277 1 10
HELIX 37 AE1 MET B 302 LEU B 309 1 8
HELIX 38 AE2 GLY B 326 VAL B 331 1 6
HELIX 39 AE3 THR B 346 PHE B 358 1 13
HELIX 40 AE4 SER B 362 TYR B 373 1 12
HELIX 41 AE5 GLU B 383 PHE B 398 1 16
HELIX 42 AE6 PHE B 398 GLU B 411 1 14
HELIX 43 AE7 PRO B 431 GLY B 435 5 5
HELIX 44 AE8 GLU B 441 PHE B 446 1 6
HELIX 45 AE9 GLY B 447 GLU B 451 5 5
HELIX 46 AF1 THR B 457 GLY B 478 1 22
HELIX 47 AF2 ARG B 515 PHE B 525 1 11
HELIX 48 AF3 PHE B 526 VAL B 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O ILE A 99 N THR A 26
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N TRP A 112 O VAL A 142
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 503 N TYR A 420
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 THR B 8 0
SHEET 2 AA3 3 GLY B 11 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 AA3 3 TRP B 56 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 AA411 MET B 16 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 AA411 TYR B 94 PRO B 100 -1 O LEU B 95 N ILE B 31
SHEET 4 AA411 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ARG B 219 N LEU B 194
SHEET 8 AA411 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA411 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 AA411 LYS B 499 LEU B 503 1 O LEU B 501 N PHE B 418
SHEET 11 AA411 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.04
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.04
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.04
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.03
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.43
LINK C GLU A 197 N BXT A 198 1555 1555 1.33
LINK C BXT A 198 N ALA A 199 1555 1555 1.33
LINK ND2 ASN A 241 C1 NAG A 604 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A 605 1555 1555 1.43
LINK ND2 ASN A 455 C1 NAG A 606 1555 1555 1.45
LINK ND2 ASN A 481 C1 NAG A 607 1555 1555 1.46
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.46
LINK ND2 ASN B 57 C1 NAG B 602 1555 1555 1.43
LINK ND2 ASN B 106 C1 NAG B 603 1555 1555 1.46
LINK C GLU B 197 N BXT B 198 1555 1555 1.33
LINK C BXT B 198 N ALA B 199 1555 1555 1.33
LINK ND2 ASN B 241 C1 NAG B 604 1555 1555 1.45
LINK ND2 ASN B 256 C1 NAG B 605 1555 1555 1.44
LINK ND2 ASN B 341 C1 NAG B 606 1555 1555 1.45
LINK ND2 ASN B 481 C1 NAG B 607 1555 1555 1.46
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.46
CISPEP 1 ALA A 101 PRO A 102 0 2.97
CISPEP 2 TYR A 282 GLY A 283 0 0.17
CISPEP 3 ALA B 101 PRO B 102 0 -0.39
SITE 1 AC1 4 TRP A 82 GLY A 115 GLY A 116 GLU A 197
SITE 1 AC2 1 LYS A 314
SITE 1 AC3 5 LEU B 18 TYR B 61 TRP B 98 ASP B 129
SITE 2 AC3 5 LYS B 131
SITE 1 AC4 7 SER B 425 LYS B 427 LEU B 428 TYR B 440
SITE 2 AC4 7 GLU B 443 TYR B 456 HOH B 711
SITE 1 AC5 5 TRP B 82 GLY B 115 GLY B 116 GLU B 197
SITE 2 AC5 5 BXT B 198
SITE 1 AC6 3 ASP A 3 ILE A 4 ASN A 17
SITE 1 AC7 2 ARG A 14 ASN A 57
SITE 1 AC8 2 ASN A 106 ASN A 188
SITE 1 AC9 2 ASN A 241 ASN A 245
SITE 1 AD1 2 SER A 338 ASN A 341
SITE 1 AD2 2 ARG A 453 ASN A 455
SITE 1 AD3 6 TYR A 477 ASN A 479 ASN A 481 GLU A 482
SITE 2 AD3 6 LEU B 88 GLN B 270
SITE 1 AD4 3 ILE B 4 ASN B 17 THR B 24
SITE 1 AD5 3 TRP B 52 ILE B 55 ASN B 57
SITE 1 AD6 3 ASN B 106 ASN B 188 LYS B 190
SITE 1 AD7 2 ASN B 241 ASN B 245
SITE 1 AD8 2 ASN B 256 GLU B 411
SITE 1 AD9 2 SER B 338 ASN B 341
SITE 1 AE1 2 TYR B 477 ASN B 481
SITE 1 AE2 22 TRP B 112 ILE B 113 GLY B 115 GLY B 116
SITE 2 AE2 22 GLY B 117 GLY B 196 ALA B 199 GLY B 200
SITE 3 AE2 22 ALA B 201 ALA B 202 GLN B 223 SER B 224
SITE 4 AE2 22 GLY B 225 TRP B 231 PHE B 398 HIS B 438
SITE 5 AE2 22 GLY B 439 GLU B 441 ILE B 442 GOL B 610
SITE 6 AE2 22 HOH B 735 HOH B 747
SITE 1 AE3 15 GLY B 116 GLY B 117 PHE B 118 GLU B 197
SITE 2 AE3 15 GLY B 200 ALA B 201 ALA B 202 SER B 203
SITE 3 AE3 15 GLN B 223 SER B 224 GLY B 225 TRP B 231
SITE 4 AE3 15 PHE B 398 HIS B 438 GOL B 610
CRYST1 76.010 79.940 231.490 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 0.013156 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004320 0.00000
TER 4107 VAL A 529
TER 8173 VAL B 529
MASTER 502 0 22 48 28 0 33 6 8517 2 284 82
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