HEADER HYDROLASE 02-APR-09 3GXF
TITLE CRYSTAL STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH ISOFAGOMINE AT NEUTRAL
TITLE 2 PH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL-
COMPND 5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;
COMPND 6 EC: 3.2.1.45;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GBA, GC, GLUC;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER
KEYWDS HYDROLASE, ALTERNATIVE INITIATION, DISEASE MUTATION, DISULFIDE BOND,
KEYWDS 2 GAUCHER DISEASE, GLYCOPROTEIN, GLYCOSIDASE, ICHTHYOSIS, LIPID
KEYWDS 3 METABOLISM, LYSOSOME, MEMBRANE, SPHINGOLIPID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.L.LIEBERMAN
REVDAT 3 13-JUL-11 3GXF 1 VERSN
REVDAT 2 16-JUN-09 3GXF 1 JRNL
REVDAT 1 05-MAY-09 3GXF 0
JRNL AUTH R.L.LIEBERMAN,J.A.D'AQUINO,D.RINGE,G.A.PETSKO
JRNL TITL EFFECTS OF PH AND IMINOSUGAR PHARMACOLOGICAL CHAPERONES ON
JRNL TITL 2 LYSOSOMAL GLYCOSIDASE STRUCTURE AND STABILITY.
JRNL REF BIOCHEMISTRY V. 48 4816 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19374450
JRNL DOI 10.1021/BI9002265
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 103572
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5209
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5942
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 327
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15720
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 426
REMARK 3 SOLVENT ATOMS : 905
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.20000
REMARK 3 B22 (A**2) : -0.18000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.336
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.178
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.687
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16573 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22635 ; 1.957 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1984 ; 8.265 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 720 ;37.898 ;23.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2516 ;17.889 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;20.705 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2418 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12532 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8179 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10812 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1107 ; 0.335 ; 0.200
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): 67 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.184 ; 0.200
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): 10183 ; 0.978 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.659 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7325 ; 2.398 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6563 ; 3.684 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 497 4
REMARK 3 1 C 1 C 497 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3930 ; 0.270 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3930 ; 0.750 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 497 4
REMARK 3 1 D 1 D 497 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 3930 ; 0.250 ; 0.500
REMARK 3 MEDIUM THERMAL 2 B (A**2): 3930 ; 0.770 ; 2.000
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
REMARK 4
REMARK 4 3GXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103572
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 32.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY '2NSX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M NAH2PO4, 0.8 M KH2PO4, 0.1 M
REMARK 280 HEPES PH 7.5, SOAK WITH 500UM ISOFAGOMINE FOR 10 MIN, GLYCEROL IN
REMARK 280 CRYO, VAPOR DIFFUSION, TEMPERATURE 298K
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 46.00650
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -349.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -341.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 92.01300
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 OE1 GLN D 226 O1 PO4 D 501 1.98
REMARK 500 NE2 GLN B 207 OD1 ASP B 263 2.03
REMARK 500 NE2 GLN A 207 OD1 ASP A 263 2.05
REMARK 500 O4 PO4 B 499 O HOH B 522 2.06
REMARK 500 OG SER B 12 O1 PO4 B 498 2.09
REMARK 500 CD ARG A 44 O2 PO4 A 501 2.13
REMARK 500 O PHE C 31 O HOH C 592 2.14
REMARK 500 N ASN B 333 O2 PO4 B 506 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 243 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 LEU A 317 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 GLY B 62 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 LEU B 286 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 LEU B 317 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG C 2 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LEU C 286 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG D 39 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG D 39 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG D 47 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 VAL D 343 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 GLY D 344 N - CA - C ANGL. DEV. = -15.7 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 ASN A 19 -159.49 -148.66
REMARK 500 ALA A 33 161.99 -49.93
REMARK 500 MET A 49 55.24 31.77
REMARK 500 PHE A 75 -138.66 -117.87
REMARK 500 ALA A 124 -162.17 65.56
REMARK 500 ALA A 136 63.95 -152.69
REMARK 500 PRO A 150 -157.27 -73.63
REMARK 500 LEU A 156 -67.12 -99.87
REMARK 500 ASN A 192 -161.31 -117.92
REMARK 500 ASP A 203 -172.52 -69.74
REMARK 500 GLU A 233 132.16 151.29
REMARK 500 SER A 242 -113.30 60.00
REMARK 500 ASP A 263 -60.95 -125.04
REMARK 500 LEU A 281 -89.47 63.67
REMARK 500 TRP A 312 -62.70 -105.56
REMARK 500 TYR A 313 60.88 31.97
REMARK 500 LEU A 314 -13.02 136.67
REMARK 500 PHE A 316 -133.10 154.62
REMARK 500 LEU A 317 162.98 -36.33
REMARK 500 ALA A 318 159.86 -39.55
REMARK 500 THR A 323 -72.43 -102.45
REMARK 500 LYS A 346 63.05 144.65
REMARK 500 TRP A 381 -139.27 -83.15
REMARK 500 ARG A 395 140.95 -179.47
REMARK 500 PHE A 397 -2.80 -145.97
REMARK 500 VAL A 477 -46.33 -133.85
REMARK 500 SER B 12 -13.85 -49.76
REMARK 500 MET B 49 60.72 30.54
REMARK 500 THR B 63 -33.62 94.90
REMARK 500 GLN B 70 78.09 -118.09
REMARK 500 PHE B 75 -138.53 -124.89
REMARK 500 ALA B 124 -149.98 67.37
REMARK 500 CYS B 126 -156.52 -132.64
REMARK 500 TYR B 133 148.50 177.51
REMARK 500 LEU B 156 -71.80 -107.65
REMARK 500 ASN B 192 -167.93 -116.87
REMARK 500 PRO B 201 134.53 -38.81
REMARK 500 GLU B 233 133.84 166.86
REMARK 500 GLU B 235 67.06 39.02
REMARK 500 PHE B 246 -167.74 -125.44
REMARK 500 LEU B 281 -89.54 70.31
REMARK 500 LEU B 287 -4.31 -56.96
REMARK 500 THR B 323 -73.71 -102.84
REMARK 500 TRP B 348 -80.35 76.65
REMARK 500 SER B 351 -67.67 -93.48
REMARK 500 HIS B 374 -3.38 87.89
REMARK 500 TRP B 381 -139.97 -84.93
REMARK 500 ASP B 409 38.26 39.83
REMARK 500 PHE B 423 -60.33 -107.69
REMARK 500 LEU B 436 97.49 -162.76
REMARK 500
REMARK 500 THIS ENTRY HAS 98 RAMACHANDRAN OUTLIERS.
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 241 SER A 242 149.15
REMARK 500 ASP A 315 PHE A 316 -42.76
REMARK 500 TYR C 313 LEU C 314 -34.91
REMARK 500 LEU C 314 ASP C 315 147.63
REMARK 500 PHE C 316 LEU C 317 -45.40
REMARK 500 GLY C 344 SER C 345 147.51
REMARK 500 CYS D 342 VAL D 343 101.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE A 246 24.3 L L OUTSIDE RANGE
REMARK 500 ASP A 315 20.3 L L OUTSIDE RANGE
REMARK 500 PHE A 316 19.6 L L OUTSIDE RANGE
REMARK 500 LEU A 317 19.1 L L OUTSIDE RANGE
REMARK 500 VAL A 398 24.2 L L OUTSIDE RANGE
REMARK 500 THR A 410 24.6 L L OUTSIDE RANGE
REMARK 500 THR B 63 21.6 L L OUTSIDE RANGE
REMARK 500 PHE B 347 20.8 L L OUTSIDE RANGE
REMARK 500 ILE D 93 22.0 L L OUTSIDE RANGE
REMARK 500 TYR D 313 24.6 L L OUTSIDE RANGE
REMARK 500 VAL D 343 21.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFM B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFM D 512
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GXM RELATED DB: PDB
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 4.5
REMARK 900 RELATED ID: 3GXI RELATED DB: PDB
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 5.5
DBREF 3GXF A 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 3GXF B 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 3GXF C 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 3GXF D 1 497 UNP P04062 GLCM_HUMAN 40 536
SEQADV 3GXF HIS A 495 UNP P04062 ARG 534 VARIANT
SEQADV 3GXF HIS B 495 UNP P04062 ARG 534 VARIANT
SEQADV 3GXF HIS C 495 UNP P04062 ARG 534 VARIANT
SEQADV 3GXF HIS D 495 UNP P04062 ARG 534 VARIANT
SEQRES 1 A 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 A 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 A 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 A 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 A 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 A 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 A 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 A 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 A 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 A 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 A 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 A 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 A 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 A 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 A 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 A 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 A 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 A 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 A 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 A 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 A 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 A 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 A 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 A 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 A 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 A 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 A 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 A 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 A 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 A 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 A 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 A 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 A 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 A 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 A 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 A 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 A 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 A 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 A 497 HIS ARG GLN
SEQRES 1 B 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 B 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 B 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 B 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 B 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 B 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 B 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 B 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 B 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 B 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 B 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 B 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 B 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 B 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 B 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 B 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 B 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 B 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 B 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 B 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 B 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 B 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 B 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 B 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 B 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 B 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 B 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 B 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 B 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 B 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 B 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 B 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 B 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 B 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 B 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 B 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 B 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 B 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 B 497 HIS ARG GLN
SEQRES 1 C 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 C 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 C 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 C 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 C 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 C 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 C 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 C 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 C 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 C 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 C 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 C 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 C 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 C 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 C 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 C 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 C 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 C 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 C 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 C 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 C 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 C 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 C 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 C 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 C 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 C 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 C 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 C 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 C 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 C 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 C 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 C 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 C 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 C 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 C 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 C 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 C 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 C 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 C 497 HIS ARG GLN
SEQRES 1 D 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 D 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 D 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 D 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 D 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 D 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 D 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 D 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 D 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 D 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 D 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 D 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 D 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 D 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 D 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 D 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 D 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 D 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 D 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 D 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 D 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 D 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 D 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 D 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 D 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 D 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 D 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 D 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 D 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 D 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 D 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 D 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 D 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 D 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 D 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 D 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 D 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 D 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 D 497 HIS ARG GLN
MODRES 3GXF ASN A 19 ASN GLYCOSYLATION SITE
MODRES 3GXF ASN B 19 ASN GLYCOSYLATION SITE
MODRES 3GXF ASN C 19 ASN GLYCOSYLATION SITE
MODRES 3GXF ASN D 19 ASN GLYCOSYLATION SITE
HET PO4 A 498 5
HET PO4 A 499 5
HET PO4 A 500 5
HET PO4 A 501 5
HET PO4 A 502 5
HET PO4 A 503 5
HET PO4 A 504 5
HET PO4 A 505 5
HET PO4 A 506 5
HET PO4 A 507 5
HET PO4 A 508 5
HET PO4 A 509 5
HET PO4 A 510 5
HET PO4 A 511 5
HET PO4 A 512 5
HET PO4 A 513 5
HET PO4 A 514 5
HET PO4 A 515 5
HET NAG A 516 14
HET GOL A 517 6
HET GOL A 518 6
HET PO4 B 498 5
HET PO4 B 499 5
HET PO4 B 500 5
HET PO4 B 501 5
HET PO4 B 502 5
HET PO4 B 503 5
HET PO4 B 504 5
HET PO4 B 505 5
HET PO4 B 506 5
HET PO4 B 507 5
HET PO4 B 508 5
HET PO4 B 509 5
HET PO4 B 510 5
HET PO4 B 511 5
HET PO4 B 512 5
HET PO4 B 513 5
HET PO4 B 514 5
HET PO4 B 515 5
HET NAG B 516 14
HET IFM B 517 10
HET GOL B 518 6
HET GOL B 519 6
HET PO4 C 498 5
HET PO4 C 499 5
HET PO4 C 500 5
HET PO4 C 501 5
HET PO4 C 502 5
HET PO4 C 503 5
HET PO4 C 504 5
HET PO4 C 505 5
HET PO4 C 506 5
HET PO4 C 507 5
HET PO4 C 508 5
HET PO4 C 509 5
HET PO4 C 510 5
HET PO4 C 511 5
HET PO4 C 512 5
HET NAG C 513 14
HET GOL C 514 6
HET PO4 D 498 5
HET PO4 D 499 5
HET PO4 D 500 5
HET PO4 D 501 5
HET PO4 D 502 5
HET PO4 D 503 5
HET PO4 D 504 5
HET PO4 D 505 5
HET PO4 D 506 5
HET PO4 D 507 5
HET PO4 D 508 5
HET PO4 D 509 5
HET PO4 D 510 5
HET NAG D 511 14
HET IFM D 512 10
HETNAM PO4 PHOSPHATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GOL GLYCEROL
HETNAM IFM 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN IFM (3R,4R,5R)-5-(HYDROXYMETHYL)PIPERIDINE-3,4-DIOL
FORMUL 5 PO4 64(O4 P 3-)
FORMUL 23 NAG 4(C8 H15 N O6)
FORMUL 24 GOL 5(C3 H8 O3)
FORMUL 45 IFM 2(C6 H13 N O3)
FORMUL 80 HOH *905(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 LEU A 156 1 7
HELIX 4 4 LEU A 156 ALA A 168 1 13
HELIX 5 5 PRO A 182 LYS A 186 5 5
HELIX 6 6 ASP A 203 HIS A 223 1 21
HELIX 7 7 GLU A 235 LEU A 241 5 7
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 SER A 271 VAL A 276 5 6
HELIX 11 11 LEU A 286 LEU A 288 5 3
HELIX 12 12 PRO A 289 THR A 297 1 9
HELIX 13 13 ASP A 298 LYS A 303 1 6
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 LYS B 186 5 5
HELIX 23 23 ASP B 203 HIS B 223 1 21
HELIX 24 24 GLU B 235 LEU B 241 5 7
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
HELIX 35 35 THR C 86 ALA C 95 1 10
HELIX 36 36 SER C 97 SER C 110 1 14
HELIX 37 37 PRO C 150 LYS C 155 1 6
HELIX 38 38 LEU C 156 ALA C 168 1 13
HELIX 39 39 PRO C 182 LYS C 186 5 5
HELIX 40 40 ASP C 203 HIS C 223 1 21
HELIX 41 41 GLU C 235 LEU C 241 5 7
HELIX 42 42 THR C 252 ASP C 263 1 12
HELIX 43 43 ASP C 263 ASN C 270 1 8
HELIX 44 44 LEU C 286 LEU C 288 5 3
HELIX 45 45 PRO C 289 THR C 297 1 9
HELIX 46 46 ASP C 298 LYS C 303 1 6
HELIX 47 47 PRO C 319 PHE C 331 1 13
HELIX 48 48 SER C 356 TYR C 373 1 18
HELIX 49 49 ILE C 406 ASP C 409 5 4
HELIX 50 50 GLN C 414 LYS C 425 1 12
HELIX 51 51 THR D 86 ALA D 95 1 10
HELIX 52 52 SER D 97 SER D 110 1 14
HELIX 53 53 PRO D 150 LYS D 155 1 6
HELIX 54 54 LEU D 156 ALA D 168 1 13
HELIX 55 55 PRO D 182 LYS D 186 5 5
HELIX 56 56 ASP D 203 HIS D 223 1 21
HELIX 57 57 GLU D 235 LEU D 241 5 7
HELIX 58 58 THR D 252 ASP D 263 1 12
HELIX 59 59 ASP D 263 ASN D 270 1 8
HELIX 60 60 LEU D 286 LEU D 288 5 3
HELIX 61 61 PRO D 289 THR D 297 1 9
HELIX 62 62 ASP D 298 LYS D 303 1 6
HELIX 63 63 LEU D 314 ALA D 318 5 5
HELIX 64 64 THR D 323 PHE D 331 1 9
HELIX 65 65 SER D 356 TYR D 373 1 18
HELIX 66 66 ILE D 406 ASP D 409 5 4
HELIX 67 67 GLN D 414 LYS D 425 1 12
SHEET 1 A 4 PRO A 6 LYS A 7 0
SHEET 2 A 4 VAL A 15 CYS A 18 -1 O VAL A 15 N LYS A 7
SHEET 3 A 4 THR A 410 LYS A 413 -1 O PHE A 411 N CYS A 18
SHEET 4 A 4 ILE A 402 ASP A 405 -1 N ILE A 403 O TYR A 412
SHEET 1 B 9 GLU A 50 PRO A 55 0
SHEET 2 B 9 THR A 36 THR A 43 -1 N ARG A 39 O SER A 52
SHEET 3 B 9 SER A 488 TRP A 494 -1 O LEU A 493 N SER A 38
SHEET 4 B 9 ALA A 456 ASN A 462 -1 N ALA A 456 O TRP A 494
SHEET 5 B 9 ASP A 445 MET A 450 -1 N LEU A 449 O VAL A 457
SHEET 6 B 9 GLN A 432 ALA A 438 -1 N GLN A 432 O MET A 450
SHEET 7 B 9 LEU A 65 LYS A 77 -1 N PHE A 75 O ARG A 433
SHEET 8 B 9 VAL A 468 ASP A 474 1 O LYS A 473 N LEU A 69
SHEET 9 B 9 GLY A 478 SER A 484 -1 O SER A 484 N VAL A 468
SHEET 1 C 9 GLY A 80 ALA A 84 0
SHEET 2 C 9 ILE A 118 MET A 123 1 O ARG A 120 N GLY A 83
SHEET 3 C 9 SER A 173 PRO A 178 1 O LEU A 175 N VAL A 121
SHEET 4 C 9 ALA A 229 THR A 231 1 O THR A 231 N ALA A 176
SHEET 5 C 9 ARG A 277 GLN A 284 1 O ARG A 277 N VAL A 230
SHEET 6 C 9 GLY A 307 HIS A 311 1 O ALA A 309 N MET A 280
SHEET 7 C 9 MET A 335 ALA A 341 1 O PHE A 337 N VAL A 310
SHEET 8 C 9 VAL A 375 ASN A 382 1 O VAL A 376 N LEU A 336
SHEET 9 C 9 GLY A 80 ALA A 84 1 N GLY A 82 O ASP A 380
SHEET 1 D 4 PRO B 6 LYS B 7 0
SHEET 2 D 4 VAL B 15 CYS B 18 -1 O VAL B 15 N LYS B 7
SHEET 3 D 4 THR B 410 LYS B 413 -1 O PHE B 411 N CYS B 18
SHEET 4 D 4 ILE B 402 ASP B 405 -1 N ASP B 405 O THR B 410
SHEET 1 E 9 GLU B 50 PRO B 55 0
SHEET 2 E 9 THR B 36 THR B 43 -1 N ARG B 39 O SER B 52
SHEET 3 E 9 SER B 488 TRP B 494 -1 O LEU B 493 N SER B 38
SHEET 4 E 9 ALA B 456 ASN B 462 -1 N ASN B 462 O SER B 488
SHEET 5 E 9 LEU B 444 MET B 450 -1 N ASP B 445 O LEU B 461
SHEET 6 E 9 GLN B 432 ALA B 438 -1 N GLN B 432 O MET B 450
SHEET 7 E 9 LEU B 65 LYS B 77 -1 N THR B 68 O VAL B 437
SHEET 8 E 9 VAL B 468 ASP B 474 1 O LYS B 473 N LEU B 69
SHEET 9 E 9 GLY B 478 SER B 484 -1 O SER B 484 N VAL B 468
SHEET 1 F 9 GLY B 80 ALA B 84 0
SHEET 2 F 9 ILE B 118 MET B 123 1 O ARG B 120 N GLY B 83
SHEET 3 F 9 SER B 173 PRO B 178 1 O LEU B 175 N VAL B 121
SHEET 4 F 9 ALA B 229 THR B 231 1 O THR B 231 N ALA B 176
SHEET 5 F 9 ARG B 277 GLN B 284 1 O ARG B 277 N VAL B 230
SHEET 6 F 9 GLY B 307 HIS B 311 1 O ALA B 309 N MET B 280
SHEET 7 F 9 MET B 335 GLU B 340 1 O MET B 335 N ILE B 308
SHEET 8 F 9 VAL B 375 ASN B 382 1 O VAL B 376 N LEU B 336
SHEET 9 F 9 GLY B 80 ALA B 84 1 N GLY B 82 O ASP B 380
SHEET 1 G 5 PRO C 6 LYS C 7 0
SHEET 2 G 5 VAL C 15 CYS C 18 -1 O VAL C 15 N LYS C 7
SHEET 3 G 5 THR C 410 LYS C 413 -1 O PHE C 411 N CYS C 18
SHEET 4 G 5 ILE C 402 ASP C 405 -1 N ASP C 405 O THR C 410
SHEET 5 G 5 ALA C 384 LEU C 385 1 N LEU C 385 O VAL C 404
SHEET 1 H 9 GLU C 50 PRO C 55 0
SHEET 2 H 9 THR C 36 THR C 43 -1 N ARG C 39 O SER C 52
SHEET 3 H 9 SER C 488 TRP C 494 -1 O LEU C 493 N SER C 38
SHEET 4 H 9 ALA C 456 ASN C 462 -1 N ALA C 456 O TRP C 494
SHEET 5 H 9 ASP C 445 MET C 450 -1 N ASP C 445 O LEU C 461
SHEET 6 H 9 GLN C 432 ALA C 438 -1 N GLN C 432 O MET C 450
SHEET 7 H 9 LEU C 65 LYS C 77 -1 N PHE C 75 O ARG C 433
SHEET 8 H 9 VAL C 468 ASP C 474 1 O LYS C 473 N LEU C 69
SHEET 9 H 9 GLY C 478 SER C 484 -1 O SER C 484 N VAL C 468
SHEET 1 I 9 GLY C 80 ALA C 84 0
SHEET 2 I 9 ILE C 118 MET C 123 1 O ARG C 120 N GLY C 83
SHEET 3 I 9 SER C 173 PRO C 178 1 O LEU C 175 N VAL C 121
SHEET 4 I 9 ALA C 229 THR C 231 1 O THR C 231 N ALA C 176
SHEET 5 I 9 ARG C 277 GLN C 284 1 O LEU C 279 N VAL C 230
SHEET 6 I 9 GLY C 307 TRP C 312 1 O ALA C 309 N MET C 280
SHEET 7 I 9 MET C 335 ALA C 341 1 O PHE C 337 N VAL C 310
SHEET 8 I 9 VAL C 375 ASN C 382 1 O VAL C 376 N LEU C 336
SHEET 9 I 9 GLY C 80 ALA C 84 1 N GLY C 82 O ASP C 380
SHEET 1 J 5 PRO D 6 LYS D 7 0
SHEET 2 J 5 VAL D 15 CYS D 18 -1 O VAL D 15 N LYS D 7
SHEET 3 J 5 THR D 410 LYS D 413 -1 O PHE D 411 N CYS D 18
SHEET 4 J 5 ILE D 402 ASP D 405 -1 N ILE D 403 O TYR D 412
SHEET 5 J 5 ALA D 384 LEU D 385 1 N LEU D 385 O VAL D 404
SHEET 1 K 9 GLU D 50 PRO D 55 0
SHEET 2 K 9 THR D 36 THR D 43 -1 N ARG D 39 O SER D 52
SHEET 3 K 9 SER D 488 TRP D 494 -1 O LEU D 493 N SER D 38
SHEET 4 K 9 ALA D 456 ASN D 462 -1 N ASN D 462 O SER D 488
SHEET 5 K 9 LEU D 444 MET D 450 -1 N ASP D 445 O LEU D 461
SHEET 6 K 9 GLN D 432 ALA D 438 -1 N GLN D 432 O MET D 450
SHEET 7 K 9 LEU D 65 LYS D 77 -1 N THR D 68 O VAL D 437
SHEET 8 K 9 VAL D 468 ASP D 474 1 O LYS D 473 N LEU D 69
SHEET 9 K 9 GLY D 478 SER D 484 -1 O SER D 484 N VAL D 468
SHEET 1 L 9 GLY D 80 ALA D 84 0
SHEET 2 L 9 ILE D 118 MET D 123 1 O ARG D 120 N GLY D 83
SHEET 3 L 9 SER D 173 PRO D 178 1 O LEU D 175 N VAL D 121
SHEET 4 L 9 ALA D 229 THR D 231 1 O THR D 231 N ALA D 176
SHEET 5 L 9 ARG D 277 GLN D 284 1 O LEU D 279 N VAL D 230
SHEET 6 L 9 GLY D 307 HIS D 311 1 O ALA D 309 N MET D 280
SHEET 7 L 9 MET D 335 GLU D 340 1 O MET D 335 N ILE D 308
SHEET 8 L 9 VAL D 375 ASN D 382 1 O VAL D 376 N LEU D 336
SHEET 9 L 9 GLY D 80 ALA D 84 1 N GLY D 82 O ASP D 380
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.05
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.06
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.11
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.11
SSBOND 5 CYS C 4 CYS C 16 1555 1555 2.08
SSBOND 6 CYS C 18 CYS C 23 1555 1555 2.10
SSBOND 7 CYS D 4 CYS D 16 1555 1555 2.13
SSBOND 8 CYS D 18 CYS D 23 1555 1555 2.14
LINK ND2 ASN A 19 C1 NAG A 516 1555 1555 1.43
LINK ND2 ASN B 19 C1 NAG B 516 1555 1555 1.46
LINK ND2 ASN C 19 C1 NAG C 513 1555 1555 1.45
LINK ND2 ASN D 19 C1 NAG D 511 1555 1555 1.46
CISPEP 1 LEU A 288 PRO A 289 0 -3.42
CISPEP 2 TYR A 313 LEU A 314 0 7.06
CISPEP 3 VAL A 343 GLY A 344 0 -1.16
CISPEP 4 GLY A 344 SER A 345 0 -26.41
CISPEP 5 SER A 345 LYS A 346 0 -13.23
CISPEP 6 GLY A 390 PRO A 391 0 3.98
CISPEP 7 GLY B 62 THR B 63 0 -6.88
CISPEP 8 LEU B 288 PRO B 289 0 -0.88
CISPEP 9 PHE B 347 TRP B 348 0 26.73
CISPEP 10 GLY B 390 PRO B 391 0 8.60
CISPEP 11 LEU C 288 PRO C 289 0 3.54
CISPEP 12 VAL C 343 GLY C 344 0 -21.27
CISPEP 13 SER C 345 LYS C 346 0 11.32
CISPEP 14 GLY C 390 PRO C 391 0 1.44
CISPEP 15 LEU D 288 PRO D 289 0 0.44
CISPEP 16 VAL D 343 GLY D 344 0 -27.35
CISPEP 17 GLY D 344 SER D 345 0 17.13
CISPEP 18 GLY D 390 PRO D 391 0 6.57
SITE 1 AC1 6 TYR A 11 SER A 12 ARG A 353 SER A 356
SITE 2 AC1 6 ASP A 358 HOH A 530
SITE 1 AC2 4 THR A 63 GLN A 440 HOH A 878 LYS C 473
SITE 1 AC3 5 LYS A 79 TRP A 228 ARG A 277 HIS A 306
SITE 2 AC3 5 HOH A 696
SITE 1 AC4 4 ARG A 44 SER A 45 HOH A 669 HOH A 886
SITE 1 AC5 2 ARG A 44 TYR A 487
SITE 1 AC6 4 GLN A 226 HIS A 273 VAL A 276 HOH A 688
SITE 1 AC7 4 PHE A 75 HIS A 328 HIS A 374 HOH A 879
SITE 1 AC8 6 LEU A 165 ARG A 170 PRO A 171 VAL A 172
SITE 2 AC8 6 HOH A 596 HOH A 948
SITE 1 AC9 3 HIS A 290 LYS A 293 HOH A 567
SITE 1 BC1 2 GLU D 254 ARG D 257
SITE 1 BC2 3 GLY A 54 PRO A 55 HOH A 584
SITE 1 BC3 3 GLU A 111 ARG A 170 PO4 A 515
SITE 1 BC4 5 ARG A 277 VAL A 305 HIS A 306 HOH A 693
SITE 2 BC4 5 HOH A 713
SITE 1 BC5 4 GLU A 254 ARG A 257 HOH A 638 HOH A 689
SITE 1 BC6 4 ARG A 329 LEU A 330 LYS D 321 ARG D 329
SITE 1 BC7 4 THR A 187 LYS A 198 GLY A 199 HOH A 686
SITE 1 BC8 5 TYR A 11 TRP A 348 GLU A 349 GLN A 350
SITE 2 BC8 5 ARG A 353
SITE 1 BC9 5 ARG A 170 PRO A 428 PO4 A 509 HOH A 665
SITE 2 BC9 5 HOH A 802
SITE 1 CC1 5 ASN A 19 HOH A 526 HOH A 538 HOH A 645
SITE 2 CC1 5 HOH A 761
SITE 1 CC2 8 ASP A 127 PHE A 128 TRP A 179 ASN A 234
SITE 2 CC2 8 GLU A 235 GLU A 340 TRP A 381 PHE A 397
SITE 1 CC3 7 ASP A 24 SER A 25 PHE A 26 ARG A 48
SITE 2 CC3 7 HOH A 587 HOH A 663 HOH A 667
SITE 1 CC4 6 TYR B 11 SER B 12 ARG B 353 SER B 356
SITE 2 CC4 6 TRP B 357 ASP B 358
SITE 1 CC5 6 GLY B 193 LYS B 194 SER B 242 GLY B 243
SITE 2 CC5 6 HOH B 522 HOH B 562
SITE 1 CC6 4 LYS B 79 TRP B 228 ARG B 277 HIS B 306
SITE 1 CC7 4 ARG B 44 SER B 45 HOH B 656 HOH B 939
SITE 1 CC8 8 GLN B 226 THR B 272 HIS B 273 VAL B 276
SITE 2 CC8 8 HOH B 541 HOH B 574 HOH B 699 HOH B 711
SITE 1 CC9 6 THR B 187 LYS B 194 GLY B 195 SER B 196
SITE 2 CC9 6 HOH B 617 HOH B 620
SITE 1 DC1 3 THR B 187 LYS B 198 GLY B 199
SITE 1 DC2 2 HIS B 290 LYS B 293
SITE 1 DC3 5 LEU B 330 PHE B 331 PRO B 332 ASN B 333
SITE 2 DC3 5 THR B 334
SITE 1 DC4 4 ARG B 277 VAL B 305 HIS B 306 HOH B 944
SITE 1 DC5 2 ARG B 262 HOH B 611
SITE 1 DC6 4 PRO B 171 VAL B 172 HOH B 596 HOH B 616
SITE 1 DC7 2 GLN B 207 ARG B 211
SITE 1 DC8 4 GLN B 143 HIS B 145 HOH B 595 HOH B 627
SITE 1 DC9 5 VAL B 214 ASP B 218 SER B 271 THR B 272
SITE 2 DC9 5 HIS B 273
SITE 1 EC1 4 LYS B 321 ARG B 329 ARG C 329 LEU C 330
SITE 1 EC2 3 ARG B 44 SER B 465 TYR B 487
SITE 1 EC3 5 PRO B 159 HIS B 162 HOH B 546 HOH B 599
SITE 2 EC3 5 HOH B 601
SITE 1 EC4 5 ILE B 5 ASN B 19 THR B 21 TYR B 22
SITE 2 EC4 5 HOH B 670
SITE 1 EC5 10 ASP B 127 PHE B 128 TRP B 179 GLU B 235
SITE 2 EC5 10 PHE B 246 TYR B 313 GLU B 340 SER B 345
SITE 3 EC5 10 TRP B 381 ASN B 396
SITE 1 EC6 7 CYS B 4 ASP B 24 ARG B 48 MET B 49
SITE 2 EC6 7 GOL B 519 HOH B 563 HOH B 817
SITE 1 EC7 9 PHE B 26 MET B 49 GLU B 50 LEU B 51
SITE 2 EC7 9 GOL B 518 HOH B 635 HOH B 659 HOH B 664
SITE 3 EC7 9 HOH B 684
SITE 1 EC8 7 TYR C 11 SER C 12 ARG C 353 SER C 356
SITE 2 EC8 7 TRP C 357 ASP C 358 HOH C 619
SITE 1 EC9 5 LYS A 473 THR C 63 GLY C 64 GLN C 440
SITE 2 EC9 5 HOH C 653
SITE 1 FC1 3 ARG C 44 SER C 45 HOH C 601
SITE 1 FC2 4 LYS C 79 TRP C 228 ARG C 277 HIS C 306
SITE 1 FC3 7 GLN C 226 PHE C 227 THR C 272 HIS C 273
SITE 2 FC3 7 HIS C 274 ASN C 275 VAL C 276
SITE 1 FC4 5 TYR C 11 TRP C 348 GLU C 349 GLN C 350
SITE 2 FC4 5 ARG C 353
SITE 1 FC5 2 ARG C 170 PRO C 428
SITE 1 FC6 3 LYS C 466 ASP C 467 HOH C 937
SITE 1 FC7 7 THR C 154 ILE C 158 PRO C 159 HIS C 162
SITE 2 FC7 7 HIS C 223 HOH C 607 HOH C 720
SITE 1 FC8 2 GLU C 254 ARG C 257
SITE 1 FC9 6 ARG C 277 VAL C 305 HIS C 306 HOH C 565
SITE 2 FC9 6 HOH C 623 HOH C 641
SITE 1 GC1 2 ARG C 44 TYR C 487
SITE 1 GC2 6 PHE C 75 HIS C 328 HIS C 374 HOH C 522
SITE 2 GC2 6 HOH C 608 HOH C 783
SITE 1 GC3 5 LEU C 165 ARG C 170 PRO C 171 VAL C 172
SITE 2 GC3 5 HOH C 768
SITE 1 GC4 4 HIS C 290 LYS C 293 HOH C 602 HOH C 622
SITE 1 GC5 5 ASN C 19 TYR C 22 HOH C 524 HOH C 559
SITE 2 GC5 5 HOH C 629
SITE 1 GC6 7 ASP C 127 PHE C 128 TRP C 179 GLU C 235
SITE 2 GC6 7 GLU C 340 TRP C 381 PHE C 397
SITE 1 GC7 7 SER C 242 TYR D 11 SER D 12 ARG D 353
SITE 2 GC7 7 SER D 356 TRP D 357 ASP D 358
SITE 1 GC8 6 GLY D 193 LYS D 194 SER D 242 GLY D 243
SITE 2 GC8 6 HOH D 612 HOH D 626
SITE 1 GC9 6 LYS D 79 TRP D 228 ARG D 277 HIS D 306
SITE 2 GC9 6 HOH D 516 HOH D 910
SITE 1 HC1 6 GLN D 226 THR D 272 HIS D 273 VAL D 276
SITE 2 HC1 6 HOH D 530 HOH D 628
SITE 1 HC2 2 ARG D 44 SER D 45
SITE 1 HC3 5 THR D 154 ILE D 158 PRO D 159 HIS D 162
SITE 2 HC3 5 HOH D 537
SITE 1 HC4 3 HIS D 290 LYS D 293 HOH D 581
SITE 1 HC5 3 LYS D 198 GLY D 199 HOH D 577
SITE 1 HC6 3 GLN D 207 ARG D 211 HOH D 562
SITE 1 HC7 2 ARG D 44 TYR D 487
SITE 1 HC8 4 LEU D 165 PRO D 171 VAL D 172 HOH D 661
SITE 1 HC9 5 ARG D 277 VAL D 305 HIS D 306 HOH D 594
SITE 2 HC9 5 HOH D 900
SITE 1 IC1 4 ALA D 438 ASN D 442 LEU D 444 HOH D 532
SITE 1 IC2 3 ASN D 19 THR D 21 TYR D 22
SITE 1 IC3 9 ASP D 127 PHE D 128 TRP D 179 GLU D 235
SITE 2 IC3 9 PHE D 246 TYR D 313 GLU D 340 TRP D 381
SITE 3 IC3 9 ASN D 396
CRYST1 110.311 92.013 152.362 90.00 111.21 90.00 P 1 21 1 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 0.009065 0.000000 0.003518 0.00000
SCALE2 0.000000 0.010868 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007040 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
