HEADER HYDROLASE 25-FEB-16 5IEF
TITLE MURINE ENDOPLASMIC RETICULUM ALPHA-GLUCOSIDASE II WITH N-BUTYL-1-
TITLE 2 DEOXYNOJIRIMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTRAL ALPHA-GLUCOSIDASE AB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-GLUCOSIDASE 2,GLUCOSIDASE II SUBUNIT ALPHA;
COMPND 5 EC: 3.2.1.84;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THIS CHAIN CONTAINS ALL OF THE RESIDUES FROM THE
COMPND 8 MATURE Q8BHN3 ISOFORM 2 (I.E. NO SIGNAL PEPTIDE AND STARTS AT RESIDUE
COMPND 9 33) BUT HAS BEEN TRYPSINISED SO THAT THERE ARE TWO GAPS IN THE
COMPND 10 SEQUENCE BETWEEN: 186-243 AND 351-369 (INCLUSIVE);
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: GLUCOSIDASE 2 SUBUNIT BETA;
COMPND 13 CHAIN: B;
COMPND 14 SYNONYM: 80K-H PROTEIN,GLUCOSIDASE II SUBUNIT BETA,PROTEIN KINASE C
COMPND 15 SUBSTRATE 60.1 KDA PROTEIN HEAVY CHAIN,PKCSH;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: THIS CHAIN CONTAINS ALL OF THE RESIDUES FROM THE
COMPND 18 MATURE O08795 BUT HAS BEEN TRYPSINISED SO THAT THERE ALL THAT WAS
COMPND 19 CRYSTALLISED ARE RESIDUES: 30-117
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GANAB, G2AN, KIAA0088;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F;
SOURCE 10 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 11 EXPRESSION_SYSTEM_CELL: ENDOTHELIAL;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: POPINGS;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 16 ORGANISM_COMMON: MOUSE;
SOURCE 17 ORGANISM_TAXID: 10090;
SOURCE 18 GENE: PRKCSH;
SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F;
SOURCE 23 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 24 EXPRESSION_SYSTEM_CELL: ENDOTHELIAL;
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: POPING
KEYWDS ENZYME GLYCOSYL HYDROLASE GH31 QUALITY CONTROL EXOGLYCOSIDASE,
KEYWDS 2 HYDROLASE, NB-DNJ
EXPDTA X-RAY DIFFRACTION
AUTHOR A.T.CAPUTO,P.ROVERSI,D.S.ALONZI,J.L.KIAPPES,N.ZITZMANN
REVDAT 5 10-JAN-24 5IEF 1 HETSYN
REVDAT 4 29-JUL-20 5IEF 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 24-AUG-16 5IEF 1 JRNL
REVDAT 2 03-AUG-16 5IEF 1 JRNL
REVDAT 1 27-JUL-16 5IEF 0
JRNL AUTH A.T.CAPUTO,D.S.ALONZI,L.MARTI,I.B.RECA,J.L.KIAPPES,
JRNL AUTH 2 W.B.STRUWE,A.CROSS,S.BASU,E.D.LOWE,B.DARLOT,A.SANTINO,
JRNL AUTH 3 P.ROVERSI,N.ZITZMANN
JRNL TITL STRUCTURES OF MAMMALIAN ER ALPHA-GLUCOSIDASE II CAPTURE THE
JRNL TITL 2 BINDING MODES OF BROAD-SPECTRUM IMINOSUGAR ANTIVIRALS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 E4630 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 27462106
JRNL DOI 10.1073/PNAS.1604463113
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 44118
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2224
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3297
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2212
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3148
REMARK 3 BIN R VALUE (WORKING SET) : 0.2206
REMARK 3 BIN FREE R VALUE : 0.2331
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.52
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02510
REMARK 3 B22 (A**2) : -1.29870
REMARK 3 B33 (A**2) : 1.32380
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.318
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.378
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.223
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.369
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.223
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8056 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11023 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2713 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 189 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1175 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8056 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 986 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9288 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.63
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.94
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218726.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44500
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 103.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.38100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: 5F0E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% V/V ETHYLENE GLYCOL, 11% W/V PEG
REMARK 280 8000 (FROM THE MORPHEUS PRECIPITANT MIX 2), 50 MM MORPHEUS
REMARK 280 CARBOXYLIC ACIDS MIX, 100 MM MORPHEUS BUFFER SYSTEM 1 PH 6.25,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 51.92000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.44500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.92000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.44500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 VAL A 208
REMARK 465 PRO A 209
REMARK 465 GLN A 210
REMARK 465 GLU A 211
REMARK 465 SER A 212
REMARK 465 LYS A 213
REMARK 465 ASP A 214
REMARK 465 PRO A 215
REMARK 465 ALA A 216
REMARK 465 GLU A 217
REMARK 465 GLY A 218
REMARK 465 ASN A 219
REMARK 465 GLY A 220
REMARK 465 ALA A 221
REMARK 465 GLN A 222
REMARK 465 PRO A 223
REMARK 465 GLU A 224
REMARK 465 ALA A 225
REMARK 465 THR A 226
REMARK 465 PRO A 227
REMARK 465 GLY A 228
REMARK 465 ASP A 229
REMARK 465 GLY A 230
REMARK 465 ASP A 231
REMARK 465 LYS A 232
REMARK 465 PRO A 233
REMARK 465 GLU A 234
REMARK 465 GLU A 235
REMARK 465 THR A 236
REMARK 465 GLN A 237
REMARK 465 GLU A 238
REMARK 465 LYS A 239
REMARK 465 ALA A 240
REMARK 465 GLU A 241
REMARK 465 LYS A 242
REMARK 465 ASP A 243
REMARK 465 THR A 351
REMARK 465 ALA A 352
REMARK 465 GLY A 353
REMARK 465 LYS A 354
REMARK 465 THR A 355
REMARK 465 LEU A 356
REMARK 465 PHE A 357
REMARK 465 GLY A 358
REMARK 465 LYS A 359
REMARK 465 MET A 360
REMARK 465 LEU A 361
REMARK 465 ASP A 362
REMARK 465 TYR A 363
REMARK 465 LEU A 364
REMARK 465 GLN A 365
REMARK 465 GLY A 366
REMARK 465 SER A 367
REMARK 465 GLY A 368
REMARK 465 GLU A 369
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 TRP A 525 CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP A 525 CH2
REMARK 470 ALA A 967 O
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 LYS A 96 35.60 71.46
REMARK 500 ALA A 143 -119.20 49.30
REMARK 500 ASP A 163 -109.13 58.18
REMARK 500 TRP A 248 -122.54 -107.38
REMARK 500 LYS A 253 -117.89 54.43
REMARK 500 LYS A 253 -118.61 55.43
REMARK 500 LYS A 259 65.27 39.32
REMARK 500 ILE A 281 52.13 35.21
REMARK 500 LEU A 317 -154.66 -101.56
REMARK 500 ASP A 427 -179.66 -171.24
REMARK 500 PRO A 491 39.37 -88.71
REMARK 500 PHE A 665 74.29 -102.20
REMARK 500 LYS A 675 175.62 71.87
REMARK 500 HIS A 872 -11.33 -157.96
REMARK 500 ASN B 107 56.43 -153.40
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 P6G A 1006
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 50 O
REMARK 620 2 ASP B 53 OD1 86.4
REMARK 620 3 TYR B 55 O 173.5 89.4
REMARK 620 4 ASP B 57 OD2 99.1 99.7 86.5
REMARK 620 5 ASP B 63 OD2 95.8 172.1 87.7 87.5
REMARK 620 6 GLU B 64 OE2 94.8 79.5 79.5 165.9 92.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 91 O
REMARK 620 2 ASP B 94 OD1 85.6
REMARK 620 3 VAL B 96 O 170.6 85.0
REMARK 620 4 ASP B 98 OD2 94.3 96.9 86.4
REMARK 620 5 ASP B 104 OD2 102.5 170.8 86.9 86.9
REMARK 620 6 GLU B 105 OE2 94.2 78.7 84.4 170.1 96.2
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F0E RELATED DB: PDB
REMARK 900 RELATED ID: 5HJO RELATED DB: PDB
REMARK 900 RELATED ID: 5HJR RELATED DB: PDB
REMARK 900 RELATED ID: 5H9O RELATED DB: PDB
REMARK 900 RELATED ID: 5IED RELATED DB: PDB
REMARK 900 RELATED ID: 5IEE RELATED DB: PDB
REMARK 900 RELATED ID: 5IEG RELATED DB: PDB
DBREF 5IEF A 33 966 UNP Q8BHN3 GANAB_MOUSE 33 966
DBREF 5IEF B 30 117 UNP O08795 GLU2B_MOUSE 30 117
SEQADV 5IEF A UNP Q8BHN3 PHE 188 DELETION
SEQADV 5IEF A UNP Q8BHN3 SER 189 DELETION
SEQADV 5IEF A UNP Q8BHN3 ASP 190 DELETION
SEQADV 5IEF A UNP Q8BHN3 LYS 191 DELETION
SEQADV 5IEF A UNP Q8BHN3 VAL 192 DELETION
SEQADV 5IEF A UNP Q8BHN3 SER 193 DELETION
SEQADV 5IEF A UNP Q8BHN3 LEU 194 DELETION
SEQADV 5IEF A UNP Q8BHN3 ALA 195 DELETION
SEQADV 5IEF A UNP Q8BHN3 LEU 196 DELETION
SEQADV 5IEF A UNP Q8BHN3 GLY 197 DELETION
SEQADV 5IEF A UNP Q8BHN3 SER 198 DELETION
SEQADV 5IEF A UNP Q8BHN3 VAL 199 DELETION
SEQADV 5IEF A UNP Q8BHN3 TRP 200 DELETION
SEQADV 5IEF A UNP Q8BHN3 ASP 201 DELETION
SEQADV 5IEF A UNP Q8BHN3 LYS 202 DELETION
SEQADV 5IEF A UNP Q8BHN3 ILE 203 DELETION
SEQADV 5IEF A UNP Q8BHN3 LYS 204 DELETION
SEQADV 5IEF A UNP Q8BHN3 ASN 205 DELETION
SEQADV 5IEF A UNP Q8BHN3 LEU 206 DELETION
SEQADV 5IEF A UNP Q8BHN3 PHE 207 DELETION
SEQADV 5IEF A UNP Q8BHN3 SER 208 DELETION
SEQADV 5IEF A UNP Q8BHN3 ARG 209 DELETION
SEQADV 5IEF ALA A 967 UNP Q8BHN3 EXPRESSION TAG
SEQRES 1 A 913 VAL ASP ARG SER ASN PHE LYS THR CYS ASP GLU SER SER
SEQRES 2 A 913 PHE CYS LYS ARG GLN ARG SER ILE ARG PRO GLY LEU SER
SEQRES 3 A 913 PRO TYR ARG ALA LEU LEU ASP THR LEU GLN LEU GLY PRO
SEQRES 4 A 913 ASP ALA LEU THR VAL HIS LEU ILE HIS GLU VAL THR LYS
SEQRES 5 A 913 VAL LEU LEU VAL LEU GLU LEU GLN GLY LEU GLN LYS ASN
SEQRES 6 A 913 MET THR ARG ILE ARG ILE ASP GLU LEU GLU PRO ARG ARG
SEQRES 7 A 913 PRO ARG TYR ARG VAL PRO ASP VAL LEU VAL ALA ASP PRO
SEQRES 8 A 913 PRO THR ALA ARG LEU SER VAL SER GLY ARG ASP ASP ASN
SEQRES 9 A 913 SER VAL GLU LEU THR VAL ALA GLU GLY PRO TYR LYS ILE
SEQRES 10 A 913 ILE LEU THR ALA GLN PRO PHE ARG LEU ASP LEU LEU GLU
SEQRES 11 A 913 ASP ARG SER LEU LEU LEU SER VAL ASN ALA ARG GLY LEU
SEQRES 12 A 913 MET ALA PHE GLU HIS GLN ARG ALA PRO ARG VAL PRO GLN
SEQRES 13 A 913 GLU SER LYS ASP PRO ALA GLU GLY ASN GLY ALA GLN PRO
SEQRES 14 A 913 GLU ALA THR PRO GLY ASP GLY ASP LYS PRO GLU GLU THR
SEQRES 15 A 913 GLN GLU LYS ALA GLU LYS ASP GLU PRO GLY ALA TRP GLU
SEQRES 16 A 913 GLU THR PHE LYS THR HIS SER ASP SER LYS PRO TYR GLY
SEQRES 17 A 913 PRO THR SER VAL GLY LEU ASP PHE SER LEU PRO GLY MET
SEQRES 18 A 913 GLU HIS VAL TYR GLY ILE PRO GLU HIS ALA ASP SER LEU
SEQRES 19 A 913 ARG LEU LYS VAL THR GLU GLY GLY GLU PRO TYR ARG LEU
SEQRES 20 A 913 TYR ASN LEU ASP VAL PHE GLN TYR GLU LEU ASN ASN PRO
SEQRES 21 A 913 MET ALA LEU TYR GLY SER VAL PRO VAL LEU LEU ALA HIS
SEQRES 22 A 913 SER PHE HIS ARG ASP LEU GLY ILE PHE TRP LEU ASN ALA
SEQRES 23 A 913 ALA GLU THR TRP VAL ASP ILE SER SER ASN THR ALA GLY
SEQRES 24 A 913 LYS THR LEU PHE GLY LYS MET LEU ASP TYR LEU GLN GLY
SEQRES 25 A 913 SER GLY GLU THR PRO GLN THR ASP ILE ARG TRP MET SER
SEQRES 26 A 913 GLU SER GLY ILE ILE ASP VAL PHE LEU MET LEU GLY PRO
SEQRES 27 A 913 SER VAL PHE ASP VAL PHE ARG GLN TYR ALA SER LEU THR
SEQRES 28 A 913 GLY THR GLN ALA LEU PRO PRO LEU PHE SER LEU GLY TYR
SEQRES 29 A 913 HIS GLN SER ARG TRP ASN TYR ARG ASP GLU ALA ASP VAL
SEQRES 30 A 913 LEU GLU VAL ASP GLN GLY PHE ASP ASP HIS ASN MET PRO
SEQRES 31 A 913 CYS ASP VAL ILE TRP LEU ASP ILE GLU HIS ALA ASP GLY
SEQRES 32 A 913 LYS ARG TYR PHE THR TRP ASP PRO THR ARG PHE PRO GLN
SEQRES 33 A 913 PRO LEU ASN MET LEU GLU HIS LEU ALA SER LYS ARG ARG
SEQRES 34 A 913 LYS LEU VAL ALA ILE VAL ASP PRO HIS ILE LYS VAL ASP
SEQRES 35 A 913 SER GLY TYR ARG VAL HIS GLU GLU LEU ARG ASN HIS GLY
SEQRES 36 A 913 LEU TYR VAL LYS THR ARG ASP GLY SER ASP TYR GLU GLY
SEQRES 37 A 913 TRP CYS TRP PRO GLY SER ALA SER TYR PRO ASP PHE THR
SEQRES 38 A 913 ASN PRO ARG MET ARG ALA TRP TRP SER ASN MET PHE SER
SEQRES 39 A 913 PHE ASP ASN TYR GLU GLY SER ALA PRO ASN LEU TYR VAL
SEQRES 40 A 913 TRP ASN ASP MET ASN GLU PRO SER VAL PHE ASN GLY PRO
SEQRES 41 A 913 GLU VAL THR MET LEU LYS ASP ALA VAL HIS TYR GLY GLY
SEQRES 42 A 913 TRP GLU HIS ARG ASP ILE HIS ASN ILE TYR GLY LEU TYR
SEQRES 43 A 913 VAL HIS MET ALA THR ALA ASP GLY LEU ILE GLN ARG SER
SEQRES 44 A 913 GLY GLY ILE GLU ARG PRO PHE VAL LEU SER ARG ALA PHE
SEQRES 45 A 913 PHE SER GLY SER GLN ARG PHE GLY ALA VAL TRP THR GLY
SEQRES 46 A 913 ASP ASN THR ALA GLU TRP ASP HIS LEU LYS ILE SER ILE
SEQRES 47 A 913 PRO MET CYS LEU SER LEU ALA LEU VAL GLY LEU SER PHE
SEQRES 48 A 913 CYS GLY ALA ASP VAL GLY GLY PHE PHE LYS ASN PRO GLU
SEQRES 49 A 913 PRO GLU LEU LEU VAL ARG TRP TYR GLN MET GLY ALA TYR
SEQRES 50 A 913 GLN PRO PHE PHE ARG ALA HIS ALA HIS LEU ASP THR GLY
SEQRES 51 A 913 ARG ARG GLU PRO TRP LEU LEU ALA SER GLN TYR GLN ASP
SEQRES 52 A 913 ALA ILE ARG ASP ALA LEU PHE GLN ARG TYR SER LEU LEU
SEQRES 53 A 913 PRO PHE TRP TYR THR LEU PHE TYR GLN ALA HIS LYS GLU
SEQRES 54 A 913 GLY PHE PRO VAL MET ARG PRO LEU TRP VAL GLN TYR PRO
SEQRES 55 A 913 GLU ASP MET SER THR PHE SER ILE GLU ASP GLN PHE MET
SEQRES 56 A 913 LEU GLY ASP ALA LEU LEU ILE HIS PRO VAL SER ASP ALA
SEQRES 57 A 913 GLY ALA HIS GLY VAL GLN VAL TYR LEU PRO GLY GLN GLU
SEQRES 58 A 913 GLU VAL TRP TYR ASP ILE GLN SER TYR GLN LYS HIS HIS
SEQRES 59 A 913 GLY PRO GLN THR LEU TYR LEU PRO VAL THR LEU SER SER
SEQRES 60 A 913 ILE PRO VAL PHE GLN ARG GLY GLY THR ILE VAL PRO ARG
SEQRES 61 A 913 TRP MET ARG VAL ARG ARG SER SER ASP CYS MET LYS ASP
SEQRES 62 A 913 ASP PRO ILE THR LEU PHE VAL ALA LEU SER PRO GLN GLY
SEQRES 63 A 913 THR ALA GLN GLY GLU LEU PHE LEU ASP ASP GLY HIS THR
SEQRES 64 A 913 PHE ASN TYR GLN THR ARG HIS GLU PHE LEU LEU ARG ARG
SEQRES 65 A 913 PHE SER PHE SER GLY SER THR LEU VAL SER SER SER ALA
SEQRES 66 A 913 ASP PRO LYS GLY HIS LEU GLU THR PRO ILE TRP ILE GLU
SEQRES 67 A 913 ARG VAL VAL ILE MET GLY ALA GLY LYS PRO ALA ALA VAL
SEQRES 68 A 913 VAL LEU GLN THR LYS GLY SER PRO GLU SER ARG LEU SER
SEQRES 69 A 913 PHE GLN HIS ASP PRO GLU THR SER VAL LEU ILE LEU ARG
SEQRES 70 A 913 LYS PRO GLY VAL SER VAL ALA SER ASP TRP SER ILE HIS
SEQRES 71 A 913 LEU ARG ALA
SEQRES 1 B 88 PHE TYR GLU GLU SER LYS PRO PHE THR CYS LEU ASP GLY
SEQRES 2 B 88 THR ALA THR ILE PRO PHE ASP GLN VAL ASN ASP ASP TYR
SEQRES 3 B 88 CYS ASP CYS LYS ASP GLY SER ASP GLU PRO GLY THR ALA
SEQRES 4 B 88 ALA CYS PRO ASN GLY SER PHE HIS CYS THR ASN THR GLY
SEQRES 5 B 88 TYR LYS PRO LEU TYR ILE LEU SER SER ARG VAL ASN ASP
SEQRES 6 B 88 GLY VAL CYS ASP CYS CYS ASP GLY THR ASP GLU TYR ASN
SEQRES 7 B 88 SER GLY THR VAL CYS GLU ASN THR CYS ARG
HET NAG C 1 14
HET NAG C 2 14
HET FMT A1003 5
HET ACT A1004 7
HET NBV A1005 35
HET P6G A1006 30
HET P6G A1007 45
HET CA B 201 1
HET CA B 202 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FMT FORMIC ACID
HETNAM ACT ACETATE ION
HETNAM NBV (2R,3R,4R,5S)-1-BUTYL-2-(HYDROXYMETHYL)PIPERIDINE-3,4,
HETNAM 2 NBV 5-TRIOL
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 FMT C H2 O2
FORMUL 5 ACT C2 H3 O2 1-
FORMUL 6 NBV C10 H21 N O4
FORMUL 7 P6G 2(C12 H26 O7)
FORMUL 9 CA 2(CA 2+)
FORMUL 11 HOH *290(H2 O)
HELIX 1 AA1 ASP A 34 PHE A 38 5 5
HELIX 2 AA2 THR A 40 GLU A 43 5 4
HELIX 3 AA3 SER A 44 SER A 52 1 9
HELIX 4 AA4 SER A 393 GLY A 406 1 14
HELIX 5 AA5 PRO A 412 LEU A 416 5 5
HELIX 6 AA6 ASP A 427 HIS A 441 1 15
HELIX 7 AA7 ASP A 451 ALA A 455 5 5
HELIX 8 AA8 GLN A 470 LYS A 481 1 12
HELIX 9 AA9 TYR A 499 HIS A 508 1 10
HELIX 10 AB1 ASN A 536 PHE A 547 1 12
HELIX 11 AB2 GLY A 573 THR A 577 5 5
HELIX 12 AB3 HIS A 584 TRP A 588 5 5
HELIX 13 AB4 GLU A 589 HIS A 594 1 6
HELIX 14 AB5 ILE A 596 ARG A 612 1 17
HELIX 15 AB6 GLY A 629 GLY A 634 5 6
HELIX 16 AB7 GLU A 644 VAL A 661 1 18
HELIX 17 AB8 GLU A 678 TYR A 691 1 14
HELIX 18 AB9 GLU A 707 LEU A 711 5 5
HELIX 19 AC1 ALA A 712 LEU A 729 1 18
HELIX 20 AC2 LEU A 729 GLY A 744 1 16
HELIX 21 AC3 PRO A 750 TYR A 755 1 6
HELIX 22 AC4 ASP A 758 PHE A 762 5 5
HELIX 23 AC5 SER A 841 LYS A 846 1 6
HELIX 24 AC6 PHE A 874 ARG A 879 1 6
HELIX 25 AC7 PRO B 47 VAL B 51 5 5
HELIX 26 AC8 SER B 90 VAL B 92 5 3
SHEET 1 AA1 4 TYR A 60 LEU A 69 0
SHEET 2 AA1 4 LEU A 74 HIS A 80 -1 O THR A 75 N GLN A 68
SHEET 3 AA1 4 LEU A 86 LEU A 94 -1 O LEU A 89 N VAL A 76
SHEET 4 AA1 4 THR A 125 ALA A 126 -1 O ALA A 126 N GLY A 93
SHEET 1 AA2 8 TYR A 60 LEU A 69 0
SHEET 2 AA2 8 LEU A 74 HIS A 80 -1 O THR A 75 N GLN A 68
SHEET 3 AA2 8 LEU A 86 LEU A 94 -1 O LEU A 89 N VAL A 76
SHEET 4 AA2 8 MET A 98 GLU A 105 -1 O ARG A 102 N GLU A 90
SHEET 5 AA2 8 ILE A 384 MET A 389 -1 O LEU A 388 N THR A 99
SHEET 6 AA2 8 ASP A 332 TRP A 337 -1 N GLY A 334 O MET A 389
SHEET 7 AA2 8 VAL A 323 HIS A 327 -1 N ALA A 326 O LEU A 333
SHEET 8 AA2 8 HIS A 277 GLY A 280 -1 N TYR A 279 O LEU A 325
SHEET 1 AA3 7 LEU A 128 ARG A 133 0
SHEET 2 AA3 7 SER A 137 VAL A 142 -1 O GLU A 139 N GLY A 132
SHEET 3 AA3 7 TYR A 147 THR A 152 -1 O ILE A 149 N LEU A 140
SHEET 4 AA3 7 ARG A 157 GLU A 162 -1 O LEU A 161 N LYS A 148
SHEET 5 AA3 7 SER A 165 VAL A 170 -1 O LEU A 168 N LEU A 160
SHEET 6 AA3 7 VAL A 266 PRO A 273 -1 O SER A 271 N SER A 169
SHEET 7 AA3 7 ALA A 177 PHE A 178 -1 N ALA A 177 O GLY A 267
SHEET 1 AA4 9 LEU A 128 ARG A 133 0
SHEET 2 AA4 9 SER A 137 VAL A 142 -1 O GLU A 139 N GLY A 132
SHEET 3 AA4 9 TYR A 147 THR A 152 -1 O ILE A 149 N LEU A 140
SHEET 4 AA4 9 ARG A 157 GLU A 162 -1 O LEU A 161 N LYS A 148
SHEET 5 AA4 9 SER A 165 VAL A 170 -1 O LEU A 168 N LEU A 160
SHEET 6 AA4 9 VAL A 266 PRO A 273 -1 O SER A 271 N SER A 169
SHEET 7 AA4 9 GLN A 372 SER A 379 -1 O SER A 379 N VAL A 266
SHEET 8 AA4 9 THR A 343 ASN A 350 -1 N SER A 348 O ASP A 374
SHEET 9 AA4 9 TYR A 299 LEU A 301 -1 N LEU A 301 O THR A 343
SHEET 1 AA5 2 GLU A 250 PHE A 252 0
SHEET 2 AA5 2 HIS A 255 ASP A 257 -1 O ASP A 257 N GLU A 250
SHEET 1 AA6 8 CYS A 666 GLY A 667 0
SHEET 2 AA6 8 ALA A 635 TRP A 637 1 N VAL A 636 O GLY A 667
SHEET 3 AA6 8 VAL A 621 SER A 623 1 N VAL A 621 O ALA A 635
SHEET 4 AA6 8 LEU A 559 ASN A 563 1 N ASN A 563 O LEU A 622
SHEET 5 AA6 8 LYS A 484 ILE A 488 1 N LEU A 485 O TYR A 560
SHEET 6 AA6 8 VAL A 447 LEU A 450 1 N LEU A 450 O VAL A 486
SHEET 7 AA6 8 TYR A 418 GLN A 420 1 N GLN A 420 O VAL A 447
SHEET 8 AA6 8 PHE A 695 ALA A 697 1 O PHE A 695 N HIS A 419
SHEET 1 AA7 3 ILE A 493 LYS A 494 0
SHEET 2 AA7 3 GLY A 527 SER A 530 -1 O SER A 530 N ILE A 493
SHEET 3 AA7 3 GLY A 522 CYS A 524 -1 N CYS A 524 O GLY A 527
SHEET 1 AA8 6 MET A 748 ARG A 749 0
SHEET 2 AA8 6 PHE A 768 LEU A 770 -1 O MET A 769 N ARG A 749
SHEET 3 AA8 6 LEU A 774 ILE A 776 -1 O ILE A 776 N PHE A 768
SHEET 4 AA8 6 VAL A 824 ARG A 827 -1 O PHE A 825 N LEU A 775
SHEET 5 AA8 6 VAL A 797 ASP A 800 -1 N TYR A 799 O GLN A 826
SHEET 6 AA8 6 LYS A 806 HIS A 808 -1 O HIS A 807 N TRP A 798
SHEET 1 AA9 2 GLY A 786 LEU A 791 0
SHEET 2 AA9 2 GLN A 811 PRO A 816 -1 O LEU A 813 N VAL A 789
SHEET 1 AB1 5 THR A 830 ARG A 834 0
SHEET 2 AB1 5 ILE A 850 ALA A 855 -1 O ALA A 855 N THR A 830
SHEET 3 AB1 5 TRP A 910 MET A 917 1 O MET A 917 N VAL A 854
SHEET 4 AB1 5 VAL A 947 SER A 956 -1 O LEU A 948 N ILE A 916
SHEET 5 AB1 5 PHE A 939 ASP A 942 -1 N GLN A 940 O ILE A 949
SHEET 1 AB2 6 ALA A 862 LEU A 868 0
SHEET 2 AB2 6 LEU A 883 SER A 890 -1 O PHE A 889 N ALA A 862
SHEET 3 AB2 6 THR A 893 SER A 898 -1 O SER A 897 N ARG A 886
SHEET 4 AB2 6 TRP A 961 ARG A 966 -1 O ILE A 963 N LEU A 894
SHEET 5 AB2 6 ALA A 924 GLN A 928 -1 N ALA A 924 O ARG A 966
SHEET 6 AB2 6 SER A 935 ARG A 936 -1 O SER A 935 N LEU A 927
SHEET 1 AB3 2 PHE B 37 THR B 38 0
SHEET 2 AB3 2 THR B 45 ILE B 46 -1 O ILE B 46 N PHE B 37
SHEET 1 AB4 2 SER B 74 CYS B 77 0
SHEET 2 AB4 2 LEU B 85 LEU B 88 -1 O LEU B 85 N CYS B 77
SSBOND 1 CYS A 41 CYS A 47 1555 1555 2.04
SSBOND 2 CYS A 655 CYS A 666 1555 1555 2.05
SSBOND 3 CYS B 39 CYS B 58 1555 1555 2.05
SSBOND 4 CYS B 56 CYS B 70 1555 1555 2.07
SSBOND 5 CYS B 77 CYS B 99 1555 1555 2.01
SSBOND 6 CYS B 97 CYS B 112 1555 1555 2.04
SSBOND 7 CYS B 100 CYS B 116 1555 1555 2.05
LINK ND2 ASN A 97 C1 NAG C 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O GLN B 50 CA CA B 201 1555 1555 2.25
LINK OD1 ASP B 53 CA CA B 201 1555 1555 2.17
LINK O TYR B 55 CA CA B 201 1555 1555 2.29
LINK OD2 ASP B 57 CA CA B 201 1555 1555 2.38
LINK OD2 ASP B 63 CA CA B 201 1555 1555 2.21
LINK OE2 GLU B 64 CA CA B 201 1555 1555 2.35
LINK O ARG B 91 CA CA B 202 1555 1555 2.28
LINK OD1 ASP B 94 CA CA B 202 1555 1555 2.43
LINK O VAL B 96 CA CA B 202 1555 1555 2.29
LINK OD2 ASP B 98 CA CA B 202 1555 1555 2.33
LINK OD2 ASP B 104 CA CA B 202 1555 1555 2.27
LINK OE2 GLU B 105 CA CA B 202 1555 1555 2.17
CISPEP 1 GLY A 145 PRO A 146 0 6.51
CISPEP 2 GLN A 154 PRO A 155 0 -9.97
CISPEP 3 PRO A 282 GLU A 283 0 9.51
CISPEP 4 GLY A 391 PRO A 392 0 12.14
CISPEP 5 TRP A 423 ASN A 424 0 0.51
CISPEP 6 GLU A 567 PRO A 568 0 2.53
CISPEP 7 GLY A 809 PRO A 810 0 -7.99
CRYST1 103.840 172.890 62.770 90.00 90.00 90.00 P 21 21 2 4
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 0.009630 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005784 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015931 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
