HEADER HYDROLASE 12-MAR-09 2WCG
TITLE X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH N-OCTYL(CYCLIC
TITLE 2 GUANIDINE)-NOJIRIMYCIN IN THE ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 40-536;
COMPND 5 EC: 3.2.1.45;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: DAUCUS CAROTA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4039
KEYWDS LIPID METABOLISM, GLUCOCEREBROSIDASE, MEMBRANE, LYSOSOME, HYDROLASE,
KEYWDS 2 GLUCOSIDASE, GLYCOPROTEIN, GAUCHER DISEASE, SPHINGOLIPID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BRUMSHTEIN,M.AGUILAR,M.I.GARCIA-MORENO,C.O.MELLET,J.M.GARCIA-
AUTHOR 2 FERNANDEZ,I.SILMAN,Y.SHAALTIEL,D.AVIEZER,J.L.SUSSMAN,A.H.FUTERMAN
REVDAT 4 13-DEC-23 2WCG 1 HETSYN
REVDAT 3 29-JUL-20 2WCG 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 15-NOV-17 2WCG 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 FORMUL LINK SITE ATOM
REVDAT 1 24-NOV-09 2WCG 0
JRNL AUTH B.BRUMSHTEIN,M.AGUILAR-MONCAYO,M.I.GARCIA-MORENO,
JRNL AUTH 2 C.ORTIZ MELLET,J.M.GARCIA FERNANDEZ,I.SILMAN,Y.SHAALTIEL,
JRNL AUTH 3 D.AVIEZER,J.L.SUSSMAN,A.H.FUTERMAN
JRNL TITL 6-AMINO-6-DEOXY-5,6-DI-N-(N'-OCTYLIMINOMETHYLIDENE)
JRNL TITL 2 NOJIRIMYCIN: SYNTHESIS, BIOLOGICAL EVALUATION, AND CRYSTAL
JRNL TITL 3 STRUCTURE IN COMPLEX WITH ACID BETA-GLUCOSIDASE.
JRNL REF CHEMBIOCHEM V. 10 1480 2009
JRNL REFN ISSN 1439-4227
JRNL PMID 19437524
JRNL DOI 10.1002/CBIC.200900142
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 44184
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) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2346
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3158
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.1660
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7743
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 188
REMARK 3 SOLVENT ATOMS : 741
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.303
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.201
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.402
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8158 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11142 ; 1.732 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 984 ; 6.982 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 346 ;36.894 ;23.353
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1218 ;14.364 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;22.291 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1231 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6168 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4933 ; 0.845 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7956 ; 1.599 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3225 ; 2.714 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3186 ; 4.272 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1509 A 1509 1
REMARK 3 1 B 1508 B 1508 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 14 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 14 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 14 ; 0.27 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 14 ; 0.27 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 58 3
REMARK 3 1 B 1 B 58 3
REMARK 3 2 A 64 A 311 3
REMARK 3 2 B 64 B 311 3
REMARK 3 3 A 320 A 344 3
REMARK 3 3 B 320 B 344 3
REMARK 3 4 A 351 A 395 3
REMARK 3 4 B 351 B 395 3
REMARK 3 5 A 400 A 497 3
REMARK 3 5 B 400 B 497 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 1872 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 1872 ; 0.06 ; 0.05
REMARK 3 LOOSE POSITIONAL 2 A (A): 1759 ; 0.10 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 B (A): 1759 ; 0.10 ; 5.00
REMARK 3 TIGHT THERMAL 2 A (A**2): 1872 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 1872 ; 0.19 ; 0.50
REMARK 3 LOOSE THERMAL 2 A (A**2): 1759 ; 0.22 ; 10.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 1759 ; 0.22 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1499 A 1502 1
REMARK 3 1 B 1498 B 1501 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 49 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 B (A): 49 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 3 A (A**2): 49 ; 0.14 ; 0.50
REMARK 3 TIGHT THERMAL 3 B (A**2): 49 ; 0.14 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. ALIPHATIC TAIL OF THE INHIBITOR WAS NOT MODELED INTO
REMARK 3 THE STRUCTURE. FLEXIBLE REGIONS THAT SHOW NO CLEAR ELECTRON
REMARK 3 DENSITY WERE NOT MODELED INTO THE STRUCTURE.
REMARK 4
REMARK 4 2WCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1290038927.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.8726
REMARK 200 MONOCHROMATOR : SILICON 111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52146
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.410
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2V3F
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M TRIS PH 6.5,
REMARK 280 25%(W/V) PEG3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 48.41350
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 ASP A 27
REMARK 465 PRO A 28
REMARK 465 PRO A 29
REMARK 465 THR A 30
REMARK 465 PHE A 31
REMARK 465 LEU A 499
REMARK 465 VAL A 500
REMARK 465 ASP A 501
REMARK 465 THR A 502
REMARK 465 MET A 503
REMARK 465 GLU B -1
REMARK 465 THR B 30
REMARK 465 PHE B 31
REMARK 465 PRO B 32
REMARK 465 LEU B 498
REMARK 465 LEU B 499
REMARK 465 VAL B 500
REMARK 465 ASP B 501
REMARK 465 THR B 502
REMARK 465 MET B 503
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 LEU A 34 CG CD1 CD2
REMARK 470 GLU A 72 CG CD OE1 OE2
REMARK 470 GLU A 111 CD OE1 OE2
REMARK 470 GLU A 112 CG CD OE1 OE2
REMARK 470 LYS A 155 CE NZ
REMARK 470 ARG A 163 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 224 CE NZ
REMARK 470 GLU A 300 CD OE1 OE2
REMARK 470 LYS A 441 CD CE NZ
REMARK 470 LYS A 466 CE NZ
REMARK 470 PHE B 0 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 2 CZ NH1 NH2
REMARK 470 LEU B 34 CG CD1 CD2
REMARK 470 ASN B 59 CG OD1 ND2
REMARK 470 GLU B 111 CD OE1 OE2
REMARK 470 LYS B 155 CD CE NZ
REMARK 470 GLN B 169 CG CD OE1 NE2
REMARK 470 LYS B 303 NZ
REMARK 470 GLU B 388 CG CD OE1 OE2
REMARK 470 LYS B 466 CG CD CE NZ
REMARK 470 GLN B 497 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN B 19 C1 NAG D 1 1.80
REMARK 500 O4 NAG D 2 O5 BMA D 3 1.84
REMARK 500 O4 NAG C 2 O5 BMA C 3 1.88
REMARK 500 O HOH A 2284 O HOH A 2319 2.05
REMARK 500 O4 NAG C 1 O5 NAG C 2 2.06
REMARK 500 O HOH A 2045 O HOH A 2277 2.08
REMARK 500 O4 NAG D 1 O5 NAG D 2 2.09
REMARK 500 O3 NAG D 1 C1 FUC B 1501 2.10
REMARK 500 O HOH A 2112 O HOH B 2238 2.13
REMARK 500 O HOH A 2027 O HOH A 2029 2.17
REMARK 500 O HOH A 2003 O HOH A 2110 2.19
REMARK 500 O HOH A 2243 O HOH A 2283 2.19
REMARK 500 O HOH B 2069 O HOH B 2314 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE B 26 CB PHE B 26 CG -0.104
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 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 433 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 353 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 433 NE - CZ - NH2 ANGL. DEV. = 4.6 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 ALA A 33 -151.25 -65.85
REMARK 500 MET A 49 49.03 38.80
REMARK 500 PHE A 75 -136.77 -117.83
REMARK 500 ALA A 124 -152.10 74.83
REMARK 500 LEU A 156 -71.04 -108.46
REMARK 500 ASN A 192 -168.83 -119.18
REMARK 500 GLU A 233 140.33 -179.72
REMARK 500 GLU A 235 64.84 38.62
REMARK 500 LEU A 249 107.06 -164.52
REMARK 500 LEU A 281 -82.25 75.94
REMARK 500 THR A 323 -73.42 -117.27
REMARK 500 HIS A 374 8.66 84.76
REMARK 500 TRP A 381 -138.25 -86.76
REMARK 500 TYR A 487 -12.93 71.47
REMARK 500 ASN B 19 -155.27 -148.98
REMARK 500 PHE B 75 -132.02 -114.43
REMARK 500 ALA B 124 -154.07 64.48
REMARK 500 LEU B 156 -67.17 -109.63
REMARK 500 ASN B 192 -167.26 -121.16
REMARK 500 GLU B 233 138.59 177.11
REMARK 500 LEU B 249 113.37 -161.61
REMARK 500 ASP B 263 -63.59 -123.93
REMARK 500 LEU B 281 -82.76 74.73
REMARK 500 THR B 323 -70.83 -115.83
REMARK 500 TRP B 381 -134.69 -85.67
REMARK 500 ASN B 392 117.16 -165.21
REMARK 500 ALA B 476 10.10 59.32
REMARK 500 TYR B 487 -14.13 75.22
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 LEU A 34 GLY A 35 -47.44
REMARK 500 LEU B 34 GLY B 35 -149.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2044 DISTANCE = 5.88 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 N'-OCTYL(CYCLIC GUANIDINE)-NOJIRIMYCIN (MT5): ALIPHATIC
REMARK 600 TAIL IS INVISIBLE IN ELECTRON DENSITY AND, THEREFORE, IS
REMARK 600 ABSENT FROM THE STRUCTURE
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 NAG D 1
REMARK 610 FUC A 1502
REMARK 610 MT5 A 1509
REMARK 610 FUC B 1501
REMARK 610 MT5 B 1508
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC", "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 TWO ADDITIONAL AMINO ACIDS AT THE N-TERMINAL (EF) AND SIX
REMARK 999 AMINO ACIDS AT THE C-TERMINAL (LLVDTM)
DBREF 2WCG A -1 0 PDB 2WCG 2WCG -1 0
DBREF 2WCG A 1 497 UNP B2R6A7 B2R6A7_HUMAN 40 536
DBREF 2WCG A 498 503 PDB 2WCG 2WCG 498 503
DBREF 2WCG B -1 0 PDB 2WCG 2WCG -1 0
DBREF 2WCG B 1 497 UNP B2R6A7 B2R6A7_HUMAN 40 536
DBREF 2WCG B 498 503 PDB 2WCG 2WCG 498 503
SEQRES 1 A 505 GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR
SEQRES 2 A 505 SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP
SEQRES 3 A 505 SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE
SEQRES 4 A 505 SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU
SEQRES 5 A 505 LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR
SEQRES 6 A 505 GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN
SEQRES 7 A 505 LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA
SEQRES 8 A 505 ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN
SEQRES 9 A 505 LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY
SEQRES 10 A 505 TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE
SEQRES 11 A 505 SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP
SEQRES 12 A 505 PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR
SEQRES 13 A 505 LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU
SEQRES 14 A 505 ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR
SEQRES 15 A 505 SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY
SEQRES 16 A 505 LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS
SEQRES 17 A 505 GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA
SEQRES 18 A 505 TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA
SEQRES 19 A 505 GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO
SEQRES 20 A 505 PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP
SEQRES 21 A 505 PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER
SEQRES 22 A 505 THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN
SEQRES 23 A 505 ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR
SEQRES 24 A 505 ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL
SEQRES 25 A 505 HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR
SEQRES 26 A 505 LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU
SEQRES 27 A 505 PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU
SEQRES 28 A 505 GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN
SEQRES 29 A 505 TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL
SEQRES 30 A 505 VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU
SEQRES 31 A 505 GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO
SEQRES 32 A 505 ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN
SEQRES 33 A 505 PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE
SEQRES 34 A 505 PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN
SEQRES 35 A 505 LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP
SEQRES 36 A 505 GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS
SEQRES 37 A 505 ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE
SEQRES 38 A 505 LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR
SEQRES 39 A 505 LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET
SEQRES 1 B 505 GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR
SEQRES 2 B 505 SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP
SEQRES 3 B 505 SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE
SEQRES 4 B 505 SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU
SEQRES 5 B 505 LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR
SEQRES 6 B 505 GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN
SEQRES 7 B 505 LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA
SEQRES 8 B 505 ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN
SEQRES 9 B 505 LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY
SEQRES 10 B 505 TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE
SEQRES 11 B 505 SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP
SEQRES 12 B 505 PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR
SEQRES 13 B 505 LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU
SEQRES 14 B 505 ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR
SEQRES 15 B 505 SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY
SEQRES 16 B 505 LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS
SEQRES 17 B 505 GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA
SEQRES 18 B 505 TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA
SEQRES 19 B 505 GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO
SEQRES 20 B 505 PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP
SEQRES 21 B 505 PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER
SEQRES 22 B 505 THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN
SEQRES 23 B 505 ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR
SEQRES 24 B 505 ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL
SEQRES 25 B 505 HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR
SEQRES 26 B 505 LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU
SEQRES 27 B 505 PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU
SEQRES 28 B 505 GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN
SEQRES 29 B 505 TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL
SEQRES 30 B 505 VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU
SEQRES 31 B 505 GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO
SEQRES 32 B 505 ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN
SEQRES 33 B 505 PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE
SEQRES 34 B 505 PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN
SEQRES 35 B 505 LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP
SEQRES 36 B 505 GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS
SEQRES 37 B 505 ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE
SEQRES 38 B 505 LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR
SEQRES 39 B 505 LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET
MODRES 2WCG ASN A 19 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET FUC A1502 10
HET SO4 A1503 5
HET SO4 A1504 5
HET SO4 A1505 5
HET SO4 A1506 5
HET SO4 A1507 5
HET SO4 A1508 5
HET MT5 A1509 14
HET CL A1510 1
HET FUC B1501 10
HET SO4 B1502 5
HET SO4 B1503 5
HET SO4 B1504 5
HET SO4 B1505 5
HET SO4 B1506 5
HET SO4 B1507 5
HET MT5 B1508 14
HET CL B1509 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM MT5 N-[(3E,5R,6R,7S,8R,8AR)-5,6,7,8-
HETNAM 2 MT5 TETRAHYDROXYHEXAHYDROIMIDAZO[1,5-A]PYRIDIN-3(2H)-
HETNAM 3 MT5 YLIDENE]OCTAN-1-AMINIUM
HETNAM CL CHLORIDE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
FORMUL 5 FUC 2(C6 H12 O5)
FORMUL 6 SO4 12(O4 S 2-)
FORMUL 12 MT5 2(C15 H30 N3 O4 1+)
FORMUL 13 CL 2(CL 1-)
FORMUL 23 HOH *741(H2 O)
HELIX 1 1 THR A 86 LEU A 94 1 9
HELIX 2 2 SER A 97 SER A 110 1 14
HELIX 3 3 PRO A 150 LYS A 155 1 6
HELIX 4 4 LEU A 156 ALA A 168 1 13
HELIX 5 5 PRO A 182 LEU A 185 5 4
HELIX 6 6 ASP A 203 GLU A 222 1 20
HELIX 7 7 SER A 237 LEU A 241 5 5
HELIX 8 8 THR A 252 ASP A 263 1 12
HELIX 9 9 ASP A 263 ASN A 270 1 8
HELIX 10 10 LEU A 286 LEU A 288 5 3
HELIX 11 11 PRO A 289 THR A 297 1 9
HELIX 12 12 ASP A 298 LYS A 303 1 6
HELIX 13 13 LEU A 314 ALA A 318 5 5
HELIX 14 14 PRO A 319 PHE A 331 1 13
HELIX 15 15 SER A 356 TYR A 373 1 18
HELIX 16 16 ILE A 406 ASP A 409 5 4
HELIX 17 17 GLN A 414 LYS A 425 1 12
HELIX 18 18 THR B 86 LEU B 94 1 9
HELIX 19 19 SER B 97 SER B 110 1 14
HELIX 20 20 PRO B 150 LYS B 155 1 6
HELIX 21 21 LEU B 156 ALA B 168 1 13
HELIX 22 22 PRO B 182 LEU B 185 5 4
HELIX 23 23 ASP B 203 GLU B 222 1 20
HELIX 24 24 SER B 237 LEU B 241 5 5
HELIX 25 25 THR B 252 ASP B 263 1 12
HELIX 26 26 ASP B 263 ASN B 270 1 8
HELIX 27 27 LEU B 286 LEU B 288 5 3
HELIX 28 28 PRO B 289 THR B 297 1 9
HELIX 29 29 ASP B 298 LYS B 303 1 6
HELIX 30 30 LEU B 314 ALA B 318 5 5
HELIX 31 31 PRO B 319 PHE B 331 1 13
HELIX 32 32 SER B 356 TYR B 373 1 18
HELIX 33 33 ILE B 406 ASP B 409 5 4
HELIX 34 34 GLN B 414 LYS B 425 1 12
SHEET 1 AA 4 PRO A 6 LYS A 7 0
SHEET 2 AA 4 VAL A 15 CYS A 18 -1 O VAL A 15 N LYS A 7
SHEET 3 AA 4 THR A 410 LYS A 413 -1 O PHE A 411 N CYS A 18
SHEET 4 AA 4 ILE A 402 ASP A 405 -1 O ILE A 403 N TYR A 412
SHEET 1 AB 9 GLU A 50 PRO A 55 0
SHEET 2 AB 9 THR A 36 SER A 42 -1 O PHE A 37 N GLY A 54
SHEET 3 AB 9 ILE A 489 TRP A 494 -1 O ILE A 489 N SER A 42
SHEET 4 AB 9 ALA A 456 ASN A 462 -1 O ALA A 456 N TRP A 494
SHEET 5 AB 9 LEU A 444 MET A 450 -1 O ASP A 445 N LEU A 461
SHEET 6 AB 9 GLN A 432 ALA A 438 -1 O GLN A 432 N MET A 450
SHEET 7 AB 9 LEU A 65 LYS A 77 -1 O THR A 68 N VAL A 437
SHEET 8 AB 9 VAL A 468 ASP A 474 1 O PRO A 469 N LEU A 65
SHEET 9 AB 9 GLY A 478 SER A 484 -1 O GLY A 478 N ASP A 474
SHEET 1 AC 9 GLY A 80 ALA A 84 0
SHEET 2 AC 9 VAL A 375 ASN A 382 1 O TRP A 378 N GLY A 82
SHEET 3 AC 9 MET A 335 GLU A 340 1 O LEU A 336 N VAL A 376
SHEET 4 AC 9 GLY A 307 HIS A 311 1 O ILE A 308 N PHE A 337
SHEET 5 AC 9 ARG A 277 GLN A 284 1 O MET A 280 N ALA A 309
SHEET 6 AC 9 ALA A 229 THR A 231 1 O VAL A 230 N LEU A 279
SHEET 7 AC 9 SER A 173 PRO A 178 1 O ALA A 176 N THR A 231
SHEET 8 AC 9 ILE A 118 MET A 123 1 O ILE A 119 N LEU A 175
SHEET 9 AC 9 GLY A 80 ALA A 84 1 O GLY A 83 N ARG A 120
SHEET 1 BA 4 PRO B 6 LYS B 7 0
SHEET 2 BA 4 VAL B 15 CYS B 18 -1 O VAL B 15 N LYS B 7
SHEET 3 BA 4 THR B 410 LYS B 413 -1 O PHE B 411 N CYS B 18
SHEET 4 BA 4 ILE B 402 ASP B 405 -1 O ILE B 403 N TYR B 412
SHEET 1 BB 9 GLU B 50 PRO B 55 0
SHEET 2 BB 9 THR B 36 SER B 42 -1 O PHE B 37 N GLY B 54
SHEET 3 BB 9 ILE B 489 TRP B 494 -1 O ILE B 489 N SER B 42
SHEET 4 BB 9 ALA B 456 ASN B 462 -1 O ALA B 456 N TRP B 494
SHEET 5 BB 9 LEU B 444 MET B 450 -1 O ASP B 445 N LEU B 461
SHEET 6 BB 9 GLN B 432 ALA B 438 -1 O GLN B 432 N MET B 450
SHEET 7 BB 9 LEU B 66 LYS B 77 -1 O THR B 68 N VAL B 437
SHEET 8 BB 9 VAL B 468 ASP B 474 1 O THR B 471 N LEU B 67
SHEET 9 BB 9 GLY B 478 SER B 484 -1 O GLY B 478 N ASP B 474
SHEET 1 BC 9 GLY B 80 ALA B 84 0
SHEET 2 BC 9 VAL B 375 ASN B 382 1 O TRP B 378 N GLY B 82
SHEET 3 BC 9 MET B 335 GLU B 340 1 O LEU B 336 N VAL B 376
SHEET 4 BC 9 GLY B 307 HIS B 311 1 O ILE B 308 N PHE B 337
SHEET 5 BC 9 ARG B 277 GLN B 284 1 O MET B 280 N ALA B 309
SHEET 6 BC 9 ALA B 229 THR B 231 1 O VAL B 230 N LEU B 279
SHEET 7 BC 9 SER B 173 PRO B 178 1 O ALA B 176 N THR B 231
SHEET 8 BC 9 ILE B 118 MET B 123 1 O ILE B 119 N LEU B 175
SHEET 9 BC 9 GLY B 80 ALA B 84 1 O GLY B 83 N ARG B 120
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.10
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.20
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.12
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.22
LINK ND2 ASN A 19 C1 NAG C 1 1555 1555 1.79
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.08
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.38
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.06
CISPEP 1 LEU A 288 PRO A 289 0 5.98
CISPEP 2 GLY A 390 PRO A 391 0 -2.49
CISPEP 3 LEU B 288 PRO B 289 0 5.33
CISPEP 4 GLY B 390 PRO B 391 0 1.62
CRYST1 68.311 96.827 83.234 90.00 104.34 90.00 P 1 21 1 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 0.014639 0.000000 0.003742 0.00000
SCALE2 0.000000 0.010328 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END