| content |
HEADER HYDROLASE 25-SEP-15 5DYT
TITLE CRYSTAL STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH N-
TITLE 2 ((1-BENZYLPIPERIDIN-3-YL)METHYL)-N-METHYLNAPHTHALENE-2-SULFONAMIDE
CAVEAT 5DYT NAG A 606 HAS WRONG CHIRALITY AT ATOM C1 NAG A 607 HAS WRONG
CAVEAT 2 5DYT CHIRALITY AT ATOM C1 NAG A 608 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 5DYT C1 FUC A 609 HAS WRONG CHIRALITY AT ATOM C1 NAG A 610 HAS
CAVEAT 4 5DYT WRONG CHIRALITY AT ATOM C1 NAG A 614 HAS WRONG CHIRALITY AT
CAVEAT 5 5DYT ATOM C1 FUC A 615 HAS WRONG CHIRALITY AT ATOM C1 FUC B 610
CAVEAT 6 5DYT HAS WRONG CHIRALITY AT ATOM C1 NAG B 611 HAS WRONG
CAVEAT 7 5DYT CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RSIDUES 28-557;
COMPND 5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 6 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 7 EC: 3.1.1.8;
COMPND 8 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 HUMAN BUTYRYLCHOLINESTERASE, AD, ALZHEIMER DISEASE, SULFONAMIDE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,B.BRUS,J.P.COLLETIER
REVDAT 1 05-OCT-16 5DYT 0
JRNL AUTH U.KOSAK,B.BRUS,D.KNEZ,M.GOBEC,R.SINK,M.ZIVIN,K.SALAT,
JRNL AUTH 2 A.PODKOWA,B.FILIPEK,A.WIECKOWSKA,B.MALAWSKA,J.STOJAN,
JRNL AUTH 3 N.COQUELLE,J.P.COLLETIER,S.GOBEC
JRNL TITL DEVELOPMENT OF A NEW SULFONAMIDE INHIBITOR OF
JRNL TITL 2 BUTYRYLCHOLINESTERASE WITH IN VIVO ANTI-ALZHEIMER ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 47137
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1414
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 46.1278 - 5.4912 0.99 4793 146 0.1739 0.2230
REMARK 3 2 5.4912 - 4.3596 1.00 4657 150 0.1460 0.1856
REMARK 3 3 4.3596 - 3.8088 1.00 4576 138 0.1449 0.1962
REMARK 3 4 3.8088 - 3.4607 1.00 4571 140 0.1767 0.2328
REMARK 3 5 3.4607 - 3.2127 0.99 4522 143 0.1959 0.2637
REMARK 3 6 3.2127 - 3.0234 0.99 4539 145 0.2086 0.2575
REMARK 3 7 3.0234 - 2.8720 1.00 4520 135 0.2249 0.2892
REMARK 3 8 2.8720 - 2.7470 1.00 4519 135 0.2331 0.3402
REMARK 3 9 2.7470 - 2.6412 1.00 4501 136 0.2367 0.3010
REMARK 3 10 2.6412 - 2.5501 1.00 4525 146 0.2572 0.3065
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.009 9100
REMARK 3 ANGLE : 1.000 12318
REMARK 3 CHIRALITY : 0.056 1354
REMARK 3 PLANARITY : 0.006 1540
REMARK 3 DIHEDRAL : 20.644 3333
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5DYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000214050.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93903
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47153
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.08070
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.73190
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 1POM
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: 0.2 M AMMONIUM ACETATE, 12%
REMARK 280 POLYETHYLENE GLYCOL 4000., PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 38.23500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.64000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.64000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.23500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.11500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 99.0 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 THR A 0
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 THR B 0
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 GLN B 484
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 GLN A 380 CG CD OE1 NE2
REMARK 470 ARG A 453 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 506 CD OE1 OE2
REMARK 470 SER B 53 CB OG
REMARK 470 LYS B 248 CG CD CE NZ
REMARK 470 ASN B 485 CB CG OD1 ND2
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 470 GLU B 506 CG CD OE1 OE2
REMARK 470 SER B 507 CB OG
REMARK 470 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 UNK UNX A 621 UNK UNX A 623 1.26
REMARK 500 UNK UNX B 618 UNK UNX B 620 1.36
REMARK 500 UNK UNX A 622 UNK UNX A 623 1.54
REMARK 500 O6 NAG B 604 C1 FUL B 606 1.55
REMARK 500 ND2 ASN B 57 O5 NAG B 602 1.85
REMARK 500 UNK UNX B 619 UNK UNX B 620 2.00
REMARK 500 UNK UNX A 621 UNK UNX A 622 2.02
REMARK 500 ND2 ASN A 57 O5 NAG A 602 2.03
REMARK 500 ND2 ASN A 17 O5 NAG A 601 2.04
REMARK 500 O HOH B 778 O HOH B 811 2.05
REMARK 500 O PHE B 217 NZ LYS B 313 2.06
REMARK 500 O4 NAG A 611 O5 NAG A 612 2.06
REMARK 500 O6 NAG A 602 O5 FUC A 604 2.07
REMARK 500 ND2 ASN A 241 O5 NAG A 607 2.11
REMARK 500 ND2 ASN B 241 O5 NAG B 604 2.12
REMARK 500 O HOH A 772 O HOH A 800 2.13
REMARK 500 O4 NAG A 602 C2 NAG A 603 2.14
REMARK 500 CG ASN B 106 O5 NAG B 603 2.15
REMARK 500 O HOH B 804 O HOH B 812 2.15
REMARK 500 O6 NAG B 608 O HOH B 701 2.16
REMARK 500 O4 NAG A 613 O5 NAG A 614 2.16
REMARK 500 O6 NAG B 604 C2 FUL B 606 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 237 O ARG B 453 1545 2.12
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 -111.76 -89.77
REMARK 500 ASP A 54 -170.81 -64.72
REMARK 500 GLN A 67 142.97 -171.89
REMARK 500 ASN A 106 47.81 -160.96
REMARK 500 PHE A 118 12.45 56.90
REMARK 500 ALA A 162 72.24 -159.19
REMARK 500 SER A 198 -124.11 64.33
REMARK 500 ASP A 297 -71.79 -135.24
REMARK 500 ASP A 375 68.80 -68.58
REMARK 500 GLN A 380 110.46 -170.16
REMARK 500 ARG A 381 70.92 49.46
REMARK 500 PHE A 398 -55.84 -124.30
REMARK 500 ARG A 453 6.15 -67.80
REMARK 500 GLU A 482 -73.78 -102.37
REMARK 500 LYS B 9 -8.09 -59.90
REMARK 500 PHE B 43 -1.95 79.92
REMARK 500 ASP B 54 -162.86 -62.01
REMARK 500 SER B 89 144.13 -177.09
REMARK 500 ASN B 106 54.72 -158.28
REMARK 500 PHE B 118 -1.00 62.34
REMARK 500 PRO B 160 -7.06 -59.71
REMARK 500 ALA B 162 74.03 -155.83
REMARK 500 SER B 198 -120.22 65.18
REMARK 500 THR B 218 -62.21 -108.32
REMARK 500 TYR B 282 72.36 -119.81
REMARK 500 PRO B 285 -8.84 -59.81
REMARK 500 ASP B 297 -73.37 -142.45
REMARK 500 ASP B 379 22.76 -75.72
REMARK 500 PHE B 398 -66.18 -131.30
REMARK 500 ASN B 455 33.66 -71.99
REMARK 500 GLU B 506 -83.48 -61.01
REMARK 500 PHE B 525 -52.38 -126.67
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 ALA A 155 LEU A 156 149.08
REMARK 500
REMARK 500 REMARK: NULL
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 FUL B 606
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HB A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HB B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
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: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through FUC A 604 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through NAG A 606 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through FUC A 609 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 610 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 611 through NAG A 612 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 613 through FUC A 615 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
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: AE4
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: AE5
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: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 604 through NAG B 605 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 607 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 609 through FUC B 610 bound to ASN B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 611 bound
REMARK 800 to ASN B 481
DBREF 5DYT A 0 529 UNP P06276 CHLE_HUMAN 28 557
DBREF 5DYT B 0 529 UNP P06276 CHLE_HUMAN 28 557
SEQRES 1 A 530 THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS
SEQRES 2 A 530 VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL
SEQRES 3 A 530 THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU
SEQRES 4 A 530 GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS
SEQRES 5 A 530 TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER
SEQRES 6 A 530 CYS CSO GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS
SEQRES 7 A 530 GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU
SEQRES 8 A 530 ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS
SEQRES 9 A 530 PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 A 530 GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP
SEQRES 11 A 530 GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL
SEQRES 12 A 530 SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA
SEQRES 13 A 530 LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU
SEQRES 14 A 530 PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN
SEQRES 15 A 530 ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU
SEQRES 16 A 530 PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS
SEQRES 17 A 530 LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA
SEQRES 18 A 530 ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL
SEQRES 19 A 530 THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU
SEQRES 20 A 530 ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU
SEQRES 21 A 530 ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE
SEQRES 22 A 530 LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO
SEQRES 23 A 530 LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE
SEQRES 24 A 530 LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN
SEQRES 25 A 530 PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP
SEQRES 26 A 530 GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE
SEQRES 27 A 530 SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE
SEQRES 28 A 530 GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU
SEQRES 29 A 530 PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP
SEQRES 30 A 530 VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU
SEQRES 31 A 530 GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA
SEQRES 32 A 530 LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN
SEQRES 33 A 530 ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU
SEQRES 34 A 530 PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU
SEQRES 35 A 530 ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP
SEQRES 36 A 530 ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE
SEQRES 37 A 530 VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO
SEQRES 38 A 530 ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE
SEQRES 39 A 530 LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU
SEQRES 40 A 530 SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS
SEQRES 41 A 530 ARG PHE TRP THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 530 THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS
SEQRES 2 B 530 VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL
SEQRES 3 B 530 THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU
SEQRES 4 B 530 GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS
SEQRES 5 B 530 TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER
SEQRES 6 B 530 CYS CSO GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS
SEQRES 7 B 530 GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU
SEQRES 8 B 530 ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS
SEQRES 9 B 530 PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 B 530 GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP
SEQRES 11 B 530 GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL
SEQRES 12 B 530 SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA
SEQRES 13 B 530 LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU
SEQRES 14 B 530 PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN
SEQRES 15 B 530 ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU
SEQRES 16 B 530 PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS
SEQRES 17 B 530 LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA
SEQRES 18 B 530 ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL
SEQRES 19 B 530 THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU
SEQRES 20 B 530 ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU
SEQRES 21 B 530 ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE
SEQRES 22 B 530 LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO
SEQRES 23 B 530 LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE
SEQRES 24 B 530 LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN
SEQRES 25 B 530 PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP
SEQRES 26 B 530 GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE
SEQRES 27 B 530 SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE
SEQRES 28 B 530 GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU
SEQRES 29 B 530 PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP
SEQRES 30 B 530 VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU
SEQRES 31 B 530 GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA
SEQRES 32 B 530 LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN
SEQRES 33 B 530 ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU
SEQRES 34 B 530 PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU
SEQRES 35 B 530 ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP
SEQRES 36 B 530 ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE
SEQRES 37 B 530 VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO
SEQRES 38 B 530 ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE
SEQRES 39 B 530 LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU
SEQRES 40 B 530 SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS
SEQRES 41 B 530 ARG PHE TRP THR SER PHE PHE PRO LYS VAL
MODRES 5DYT CSO A 66 CYS MODIFIED RESIDUE
MODRES 5DYT CSO B 66 CYS MODIFIED RESIDUE
HET CSO A 66 7
HET CSO B 66 7
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET FUC A 604 10
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET FUC A 609 10
HET NAG A 610 14
HET NAG A 611 14
HET NAG A 612 14
HET NAG A 613 14
HET NAG A 614 14
HET FUC A 615 10
HET 5HB A 616 29
HET GOL A 617 6
HET GOL A 618 6
HET GOL A 619 6
HET EDO A 620 4
HET UNX A 621 1
HET UNX A 622 1
HET UNX A 623 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 FUL B 606 10
HET NAG B 607 14
HET NAG B 608 14
HET NAG B 609 14
HET FUC B 610 10
HET NAG B 611 14
HET 5HB B 612 29
HET GOL B 613 6
HET GOL B 614 6
HET EDO B 615 4
HET EDO B 616 4
HET EDO B 617 4
HET UNX B 618 1
HET UNX B 619 1
HET UNX B 620 1
HET PEG B 621 7
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM 5HB N-{[(3R)-1-BENZYLPIPERIDIN-3-YL]METHYL}-N-
HETNAM 2 5HB METHYLNAPHTHALENE-2-SULFONAMIDE
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM FUL BETA-L-FUCOSE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 3 NAG 21(C8 H15 N O6)
FORMUL 4 FUC 4(C6 H12 O5)
FORMUL 10 5HB 2(C24 H28 N2 O2 S)
FORMUL 11 GOL 5(C3 H8 O3)
FORMUL 14 EDO 4(C2 H6 O2)
FORMUL 15 UNX 6(X)
FORMUL 22 FUL C6 H12 O5
FORMUL 36 PEG C4 H10 O3
FORMUL 37 HOH *232(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 VAL A 148 LEU A 154 1 7
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 SER A 198 SER A 210 1 13
HELIX 9 AA9 PRO A 211 PHE A 217 5 7
HELIX 10 AB1 SER A 235 THR A 250 1 16
HELIX 11 AB2 ASN A 256 LYS A 267 1 12
HELIX 12 AB3 ASP A 268 LEU A 274 1 7
HELIX 13 AB4 ASN A 275 VAL A 280 5 6
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 VAL A 331 1 6
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 TYR A 373 1 12
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 GLU A 411 1 14
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 PHE A 446 1 6
HELIX 22 AC4 GLY A 447 ASN A 455 5 9
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 PHE A 525 1 11
HELIX 25 AC7 PHE A 526 VAL A 529 5 4
HELIX 26 AC8 LEU B 38 ARG B 42 5 5
HELIX 27 AC9 PHE B 76 MET B 81 1 6
HELIX 28 AD1 LEU B 125 ASP B 129 5 5
HELIX 29 AD2 GLY B 130 ARG B 138 1 9
HELIX 30 AD3 GLY B 149 LEU B 154 1 6
HELIX 31 AD4 ASN B 165 ILE B 182 1 18
HELIX 32 AD5 ALA B 183 PHE B 185 5 3
HELIX 33 AD6 SER B 198 SER B 210 1 13
HELIX 34 AD7 PRO B 211 PHE B 217 5 7
HELIX 35 AD8 SER B 235 THR B 250 1 16
HELIX 36 AD9 ASN B 256 ARG B 265 1 10
HELIX 37 AE1 ASP B 268 LEU B 274 1 7
HELIX 38 AE2 ASN B 275 VAL B 279 5 5
HELIX 39 AE3 MET B 302 LEU B 309 1 8
HELIX 40 AE4 GLY B 326 VAL B 331 1 6
HELIX 41 AE5 THR B 346 PHE B 358 1 13
HELIX 42 AE6 SER B 362 TYR B 373 1 12
HELIX 43 AE7 GLU B 383 PHE B 398 1 16
HELIX 44 AE8 PHE B 398 GLU B 411 1 14
HELIX 45 AE9 PRO B 431 GLY B 435 5 5
HELIX 46 AF1 GLU B 441 PHE B 446 1 6
HELIX 47 AF2 GLY B 447 GLU B 451 5 5
HELIX 48 AF3 THR B 457 GLY B 478 1 22
HELIX 49 AF4 ARG B 515 PHE B 525 1 11
HELIX 50 AF5 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 LEU A 95 N ILE A 31
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 LEU A 110 O ILE A 140
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 GLY B 11 N THR B 8
SHEET 3 AA3 3 ILE B 55 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 VAL B 97 N PHE B 28
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 PHE B 195 N ILE B 111
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ILE B 221 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 2.05
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.05
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.05
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.05
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.05
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.05
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.52
LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.45
LINK C CYS A 65 N CSO A 66 1555 1555 1.33
LINK C CSO A 66 N GLN A 67 1555 1555 1.32
LINK ND2 ASN A 106 C1 NAG A 605 1555 1555 1.40
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.48
LINK ND2 ASN A 341 C1 NAG A 610 1555 1555 1.50
LINK ND2 ASN A 481 C1 NAG A 611 1555 1555 1.45
LINK ND2 ASN A 486 C1 NAG A 613 1555 1555 1.45
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.47
LINK ND2 ASN B 57 C1 NAG B 602 1555 1555 1.47
LINK C CYS B 65 N CSO B 66 1555 1555 1.33
LINK C CSO B 66 N GLN B 67 1555 1555 1.33
LINK ND2 ASN B 106 C1 NAG B 603 1555 1555 1.52
LINK ND2 ASN B 106 O5 NAG B 603 1555 1555 1.31
LINK ND2 ASN B 241 C1 NAG B 604 1555 1555 1.49
LINK ND2 ASN B 256 C1 NAG B 607 1555 1555 1.45
LINK ND2 ASN B 341 C1 NAG B 608 1555 1555 1.51
LINK ND2 ASN B 455 C1 NAG B 609 1555 1555 1.46
LINK ND2 ASN B 481 C1 NAG B 611 1555 1555 1.48
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.46
LINK O6 NAG A 602 C1 FUC A 604 1555 1555 1.39
LINK O4 NAG A 605 C1 NAG A 606 1555 1555 1.54
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.46
LINK O6 NAG A 607 C1 FUC A 609 1555 1555 1.50
LINK O4 NAG A 611 C1 NAG A 612 1555 1555 1.50
LINK O4 NAG A 613 C1 NAG A 614 1555 1555 1.41
LINK O6 NAG A 613 C1 FUC A 615 1555 1555 1.46
LINK O4 NAG B 604 C1 NAG B 605 1555 1555 1.49
LINK O6 NAG B 609 C1 FUC B 610 1555 1555 1.48
CISPEP 1 ALA A 101 PRO A 102 0 1.90
CISPEP 2 GLN A 380 ARG A 381 0 -0.04
CISPEP 3 ALA B 101 PRO B 102 0 2.03
SITE 1 AC1 9 GLY A 116 GLY A 117 GLN A 119 THR A 120
SITE 2 AC1 9 SER A 198 SER A 287 TRP A 430 HIS A 438
SITE 3 AC1 9 HOH A 703
SITE 1 AC2 4 LEU A 18 TRP A 98 ASP A 129 LYS A 131
SITE 1 AC3 6 ASN A 228 TYR A 396 PRO A 401 TRP A 522
SITE 2 AC3 6 THR A 523 HOH A 760
SITE 1 AC4 5 TYR A 33 SER A 48 LEU A 49 LEU A 173
SITE 2 AC4 5 TRP A 177
SITE 1 AC5 2 HIS A 77 GLU A 443
SITE 1 AC6 3 PHE B 278 NAG B 604 NAG B 605
SITE 1 AC7 15 GLY B 116 GLY B 117 GLN B 119 THR B 120
SITE 2 AC7 15 SER B 198 TRP B 231 LEU B 286 SER B 287
SITE 3 AC7 15 PHE B 329 TRP B 430 MET B 437 HIS B 438
SITE 4 AC7 15 TYR B 440 HOH B 711 HOH B 812
SITE 1 AC8 5 LEU B 18 TYR B 61 TRP B 98 ASP B 129
SITE 2 AC8 5 LYS B 131
SITE 1 AC9 6 TRP B 231 LEU B 286 SER B 287 VAL B 288
SITE 2 AC9 6 ASN B 397 EDO B 616
SITE 1 AD1 3 ARG B 42 LYS B 267 PRO B 269
SITE 1 AD2 7 PRO B 230 TRP B 231 VAL B 233 THR B 234
SITE 2 AD2 7 GLU B 238 VAL B 288 GOL B 614
SITE 1 AD3 1 ASN B 455
SITE 1 AD4 7 HIS B 77 MET B 81 SER B 425 LYS B 427
SITE 2 AD4 7 LEU B 428 PRO B 429 GLU B 443
SITE 1 AD5 1 ASN A 17
SITE 1 AD6 2 ILE A 55 ASN A 57
SITE 1 AD7 3 ASN A 106 ASN A 188 LYS A 190
SITE 1 AD8 7 ASN A 241 ASN A 245 LYS A 248 PHE A 278
SITE 2 AD8 7 PRO A 281 NAG B 609 FUC B 610
SITE 1 AD9 5 SER A 338 ASN A 341 HOH A 713 HOH A 793
SITE 2 AD9 5 HOH A 798
SITE 1 AE1 10 TYR A 477 ASN A 479 ASN A 481 GLU A 482
SITE 2 AE1 10 THR A 483 GLN A 484 CSO B 66 ASP B 87
SITE 3 AE1 10 LEU B 88 GLN B 270
SITE 1 AE2 4 ASN A 486 SER A 487 THR A 488 THR A 508
SITE 1 AE3 2 ILE B 4 ASN B 17
SITE 1 AE4 1 ASN B 57
SITE 1 AE5 3 ASN B 106 ASN B 188 HOH B 703
SITE 1 AE6 6 TYR B 237 ASN B 241 ASN B 245 TYR B 282
SITE 2 AE6 6 FUL B 606 HOH B 785
SITE 1 AE7 2 ASN B 256 GLU B 411
SITE 1 AE8 5 SER B 338 ASN B 341 HOH B 701 HOH B 716
SITE 2 AE8 5 HOH B 744
SITE 1 AE9 6 TYR A 237 ARG A 240 NAG A 607 LYS B 427
SITE 2 AE9 6 ASP B 454 ASN B 455
SITE 1 AF1 4 TYR B 477 ASN B 481 GLU B 482 HOH B 756
CRYST1 76.470 80.230 231.280 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 0.013077 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004324 0.00000
TER 4211 VAL A 529
TER 8372 VAL B 529
MASTER 479 0 46 50 28 0 46 6 9040 2 500 82
END |