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HEADER HYDROLASE 11-SEP-24 9GRB
TITLE CRYSTAL STRUCTURE OF MOUSE CARBOXYLESTERASE 2B (CES2B)
CAVEAT 9GRB FUC G 2 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: D, A, B, C;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CES2B, BC015286;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL: EXPI293F CELLS
KEYWDS CARBOXYLESTERASE 2B; CES2B; PROTEIN STRUCTURE; LIPID METABOLISM; X-
KEYWDS 2 RAY CRYSTALLOGRAPHY; ALPHA/BETA-HYDROLASE FOLD; BIOCHEMISTRY; LIPID
KEYWDS 3 HYDROLYSIS; NON-ALCOHOLIC FATTY LIVER DISEASE; HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.RAMMER,H.EISNER,T.SAGMEISTER,M.OBERER
REVDAT 1 24-SEP-25 9GRB 0
JRNL AUTH L.RAMMER,H.EISNER,T.SAGMEISTER,L.RIEGLER-BERKET,
JRNL AUTH 2 C.RODRIGUEZ GAMEZ,G.CHALHOUB,L.LIESINGER,
JRNL AUTH 3 R.BIRNER-GRUENBERGER,G.HAEMMERLE,G.SCHOISWOHL,
JRNL AUTH 4 T.PAVKOV-KELLER,M.OBERER
JRNL TITL CRYSTAL STRUCTURE OF MOUSE CARBOXYLESTERASE 2 (CES2B)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430 (REFMACAT 0.4.105)
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 85632
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.215
REMARK 3 FREE R VALUE TEST SET COUNT : 4466
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6046
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 283
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16231
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 571
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06600
REMARK 3 B22 (A**2) : 0.05200
REMARK 3 B33 (A**2) : 0.01200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.494
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.243
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.181
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.221
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16746 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22762 ; 1.805 ; 1.811
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2073 ; 6.616 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ; 7.086 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2731 ;14.098 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2503 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12902 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7198 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11450 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 687 ; 0.153 ; 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): 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): 8307 ; 4.016 ; 4.232
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10375 ; 6.080 ; 7.618
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8439 ; 5.818 ; 4.618
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12387 ; 8.285 ; 8.286
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 : 6
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : D A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 29 D 549 NULL
REMARK 3 1 A 29 A 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : D B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 2 D 29 D 549 NULL
REMARK 3 2 B 29 B 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : D C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 3 D 30 D 549 NULL
REMARK 3 3 C 30 C 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 4 A 29 A 549 NULL
REMARK 3 4 B 29 B 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 5 A 30 A 548 NULL
REMARK 3 5 C 30 C 548 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 6 B 30 B 549 NULL
REMARK 3 6 C 30 C 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 29 D 551
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0583 -74.2218 101.7037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1023 T22: 0.1785
REMARK 3 T33: 0.2780 T12: 0.0255
REMARK 3 T13: -0.0677 T23: 0.1490
REMARK 3 L TENSOR
REMARK 3 L11: 0.9355 L22: 0.8093
REMARK 3 L33: 2.8853 L12: 0.1168
REMARK 3 L13: 0.0005 L23: -0.5613
REMARK 3 S TENSOR
REMARK 3 S11: -0.0671 S12: -0.0110 S13: 0.1865
REMARK 3 S21: 0.0733 S22: -0.1385 S23: -0.2802
REMARK 3 S31: -0.1663 S32: 0.3150 S33: 0.2056
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 29 A 549
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6103 -54.2987 4.1231
REMARK 3 T TENSOR
REMARK 3 T11: 0.0594 T22: 0.1762
REMARK 3 T33: 0.0252 T12: -0.0453
REMARK 3 T13: -0.0130 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.1480 L22: 2.0711
REMARK 3 L33: 1.3361 L12: 0.1864
REMARK 3 L13: -0.0958 L23: -0.8165
REMARK 3 S TENSOR
REMARK 3 S11: 0.1319 S12: 0.1180 S13: 0.0416
REMARK 3 S21: -0.0381 S22: -0.0455 S23: 0.2090
REMARK 3 S31: 0.0900 S32: -0.3516 S33: -0.0864
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 29 B 549
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1531 -69.1680 40.8764
REMARK 3 T TENSOR
REMARK 3 T11: 0.4085 T22: 0.1211
REMARK 3 T33: 0.0494 T12: -0.0850
REMARK 3 T13: -0.0622 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 2.8379 L22: 0.6161
REMARK 3 L33: 0.7262 L12: -0.0839
REMARK 3 L13: 0.6748 L23: 0.0413
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: -0.1906 S13: -0.1791
REMARK 3 S21: 0.0908 S22: 0.0721 S23: -0.0393
REMARK 3 S31: 0.3391 S32: 0.0091 S33: -0.1211
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 30 C 549
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0314 -58.3622 65.6555
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.1179
REMARK 3 T33: 0.1410 T12: 0.0714
REMARK 3 T13: -0.0210 T23: 0.0699
REMARK 3 L TENSOR
REMARK 3 L11: 1.8615 L22: 0.8712
REMARK 3 L33: 2.3160 L12: 0.5295
REMARK 3 L13: 0.8198 L23: -0.1540
REMARK 3 S TENSOR
REMARK 3 S11: -0.1212 S12: 0.2808 S13: 0.1052
REMARK 3 S21: -0.1136 S22: -0.1128 S23: -0.2077
REMARK 3 S31: -0.1980 S32: 0.1224 S33: 0.2340
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 NOT BEEN USED
REMARK 4
REMARK 4 9GRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-24.
REMARK 100 THE DEPOSITION ID IS D_1292141525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033190
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85640
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 46.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.08605
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.79410
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: H2 MORPHEUS II SCREEN (40 MM
REMARK 280 POLYAMINES (0.1 M SPERMINE TETRAHYDROCHLORIDE, 0.1 M SPERMIDINE
REMARK 280 TRIHYDROCHLORIDE, 0.1 M 1,4-DIAMINOBUTANE DIHYDROCHLORIDE, 0.1 M
REMARK 280 DL-ORNITHINE MONOHYDROCHLORIDE), 0.1 M BUFFER SYSTEM 4 AT PH 6.5
REMARK 280 (1 M MOPSO, BIS-TRIS), AND 32.5% V/V PRECIPITANT MIX 6 (25% W/V
REMARK 280 PEG 4000, 40% W/V 1,2,6-HEXANETRIOL)), PH 7.4, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 90.37500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.90050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 90.37500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.90050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 820 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 873 LIES ON A SPECIAL POSITION.
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 D 103
REMARK 465 MET D 104
REMARK 465 LYS D 105
REMARK 465 GLN A 550
REMARK 465 ASP A 551
REMARK 465 VAL B 103
REMARK 465 MET B 104
REMARK 465 LYS B 105
REMARK 465 GLU B 106
REMARK 465 ILE B 107
REMARK 465 GLN B 550
REMARK 465 ASP B 551
REMARK 465 SER C 29
REMARK 465 GLN C 550
REMARK 465 ASP C 551
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 O ASN C 371 N THR C 372 0.75
REMARK 500 O ASN C 371 CA THR C 372 1.25
REMARK 500 OG1 THR B 538 OD2 ASP C 393 1.85
REMARK 500 ND2 ASN A 371 C1 NAG E 1 1.89
REMARK 500 OD2 ASP B 393 OG1 THR C 538 1.89
REMARK 500 O GLN A 305 O HOH A 701 1.99
REMARK 500 ND2 ASN B 371 C1 NAG G 1 2.01
REMARK 500 CA GLY C 102 O HOH C 714 2.08
REMARK 500 OG SER C 426 O HOH C 701 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR D 538 OD2 ASP A 393 3546 2.11
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 LYS D 110 CB - CG - CD ANGL. DEV. = 16.4 DEGREES
REMARK 500 MET D 266 CG - SD - CE ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLU D 409 CB - CA - C ANGL. DEV. = -14.6 DEGREES
REMARK 500 ARG D 446 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 MET D 469 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG D 525 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ARG D 525 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 ARG D 525 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU D 539 CB - CG - CD2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 MET A 377 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU A 385 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG A 446 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 482 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 482 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 525 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLN A 541 CB - CA - C ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG B 446 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASN C 371 CA - C - O ANGL. DEV. = 19.2 DEGREES
REMARK 500 ASN C 371 O - C - N ANGL. DEV. = -88.7 DEGREES
REMARK 500 MET C 469 CG - SD - CE ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG C 483 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LYS C 542 CB - CA - C ANGL. DEV. = 12.3 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 D 189 87.32 -153.12
REMARK 500 SER D 225 -122.09 60.63
REMARK 500 GLU D 314 -66.63 -92.30
REMARK 500 ASP D 341 52.43 -145.81
REMARK 500 TRP D 345 -74.45 -155.77
REMARK 500 PHE D 413 -52.91 -128.03
REMARK 500 LYS D 451 -121.29 -94.19
REMARK 500 ASP D 509 -149.97 -135.06
REMARK 500 LYS D 537 -88.31 -102.43
REMARK 500 SER D 549 47.73 -90.16
REMARK 500 ALA A 55 -5.51 -140.52
REMARK 500 ALA A 189 87.56 -152.44
REMARK 500 SER A 225 -120.56 60.63
REMARK 500 MET A 306 70.00 61.17
REMARK 500 GLU A 314 -66.91 -94.58
REMARK 500 ASP A 341 51.83 -146.69
REMARK 500 TRP A 345 -73.60 -157.38
REMARK 500 PHE A 413 -54.18 -127.76
REMARK 500 LYS A 451 -119.69 -94.21
REMARK 500 ASP A 509 -149.84 -139.25
REMARK 500 ALA B 55 -5.28 -144.04
REMARK 500 ALA B 189 88.14 -151.72
REMARK 500 SER B 225 -120.94 60.36
REMARK 500 TYR B 258 8.19 82.64
REMARK 500 ASP B 281 106.21 -173.29
REMARK 500 MET B 306 69.11 62.77
REMARK 500 GLU B 314 -66.33 -93.11
REMARK 500 ASP B 341 50.93 -145.44
REMARK 500 TRP B 345 -72.25 -156.32
REMARK 500 PHE B 413 -53.67 -127.42
REMARK 500 LYS B 451 -119.01 -93.48
REMARK 500 ASP B 509 -149.74 -135.13
REMARK 500 LYS B 537 -72.92 -110.75
REMARK 500 LYS C 105 -73.95 -73.99
REMARK 500 ALA C 189 86.77 -151.81
REMARK 500 SER C 225 -122.20 60.19
REMARK 500 TYR C 258 7.92 81.80
REMARK 500 GLU C 278 50.65 36.63
REMARK 500 GLU C 314 -66.36 -94.17
REMARK 500 ASP C 341 51.60 -146.98
REMARK 500 TRP C 345 -72.64 -157.17
REMARK 500 PHE C 413 -54.45 -127.96
REMARK 500 LYS C 451 -122.03 -94.20
REMARK 500 ASP C 509 -149.31 -135.73
REMARK 500 LYS C 537 -72.19 -109.57
REMARK 500 GLU C 545 -1.97 -58.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG D 36 0.11 SIDE CHAIN
REMARK 500 ARG D 287 0.09 SIDE CHAIN
REMARK 500 ARG A 482 0.11 SIDE CHAIN
REMARK 500 ARG C 203 0.10 SIDE CHAIN
REMARK 500 ARG C 525 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN C 371 -17.78
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 D 733 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH D 734 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH D 735 DISTANCE = 7.81 ANGSTROMS
REMARK 525 HOH D 736 DISTANCE = 12.80 ANGSTROMS
REMARK 525 HOH D 737 DISTANCE = 16.61 ANGSTROMS
REMARK 525 HOH A 869 DISTANCE = 7.48 ANGSTROMS
REMARK 525 HOH A 870 DISTANCE = 8.11 ANGSTROMS
REMARK 525 HOH A 871 DISTANCE = 9.20 ANGSTROMS
REMARK 525 HOH A 872 DISTANCE = 11.22 ANGSTROMS
REMARK 525 HOH A 873 DISTANCE = 12.33 ANGSTROMS
REMARK 525 HOH A 874 DISTANCE = 12.51 ANGSTROMS
REMARK 525 HOH A 875 DISTANCE = 12.83 ANGSTROMS
REMARK 525 HOH C 820 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C 821 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH C 822 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH C 823 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH C 824 DISTANCE = 10.95 ANGSTROMS
REMARK 525 HOH C 825 DISTANCE = 13.65 ANGSTROMS
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 G 1
REMARK 610 NAG E 1
REMARK 610 NAG C 601
DBREF 9GRB D 29 551 UNP Q6PDB7 Q6PDB7_MOUSE 29 551
DBREF 9GRB A 29 551 UNP Q6PDB7 Q6PDB7_MOUSE 29 551
DBREF 9GRB B 29 551 UNP Q6PDB7 Q6PDB7_MOUSE 29 551
DBREF 9GRB C 29 551 UNP Q6PDB7 Q6PDB7_MOUSE 29 551
SEQRES 1 D 523 SER PRO GLU ALA SER PRO ILE ARG ASN THR HIS THR GLY
SEQRES 2 D 523 GLN VAL ARG GLY SER LEU VAL HIS VAL LYS ASP THR LYS
SEQRES 3 D 523 ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 D 523 PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO GLU ALA
SEQRES 5 D 523 PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR ALA HIS
SEQRES 6 D 523 PRO ALA MET CYS LEU GLN ASN LEU GLY VAL MET LYS GLU
SEQRES 7 D 523 ILE LYS LEU LYS LEU PRO PRO VAL SER THR SER GLU ASP
SEQRES 8 D 523 CYS LEU TYR LEU ASN ILE TYR THR PRO ALA HIS ALA HIS
SEQRES 9 D 523 GLU GLY SER ASN LEU PRO VAL MET VAL TRP ILE HIS GLY
SEQRES 10 D 523 GLY GLY LEU VAL ALA GLY MET ALA SER MET TYR ASP GLY
SEQRES 11 D 523 SER LEU LEU ALA ALA ILE GLU ASP LEU VAL VAL VAL THR
SEQRES 12 D 523 ILE GLN TYR ARG LEU GLY VAL LEU GLY PHE PHE SER THR
SEQRES 13 D 523 GLY ASP GLN HIS ALA ARG GLY ASN TRP GLY PHE LEU ASP
SEQRES 14 D 523 GLN VAL ALA ALA LEU ARG TRP ILE GLN GLN ASN ILE ALA
SEQRES 15 D 523 HIS PHE GLY GLY LYS PRO ASP ARG VAL THR ILE PHE GLY
SEQRES 16 D 523 GLU SER ALA GLY GLY THR SER VAL SER SER HIS VAL VAL
SEQRES 17 D 523 SER PRO MET SER LYS GLY LEU PHE HIS GLY ALA ILE MET
SEQRES 18 D 523 GLU SER GLY VAL ALA LEU LEU PRO TYR LEU ILE THR ASP
SEQRES 19 D 523 THR SER GLU MET VAL SER THR THR VAL ALA LYS LEU SER
SEQRES 20 D 523 GLY CYS GLU ALA MET ASP SER GLU ALA LEU VAL ARG CYS
SEQRES 21 D 523 LEU ARG GLY LYS SER GLU ALA GLU ILE LEU ALA ILE ASN
SEQRES 22 D 523 LYS LEU VAL GLN MET ILE PRO ALA VAL VAL ASP GLY GLU
SEQRES 23 D 523 PHE PHE PRO ARG HIS PRO LYS GLU LEU LEU ALA SER GLU
SEQRES 24 D 523 ASP PHE HIS PRO VAL PRO SER ILE ILE GLY VAL ASN ASN
SEQRES 25 D 523 ASP GLU PHE GLY TRP THR ILE PRO VAL VAL MET GLY SER
SEQRES 26 D 523 ALA GLN THR ILE LYS GLU ILE THR ARG GLU ASN LEU GLN
SEQRES 27 D 523 ALA VAL LEU LYS ASN THR THR ALA GLN LEU MET LEU PRO
SEQRES 28 D 523 PRO GLU CYS SER ASP LEU LEU MET GLU GLU TYR MET GLY
SEQRES 29 D 523 ASP THR GLU ASP ALA GLN THR LEU GLN ILE GLN PHE THR
SEQRES 30 D 523 GLU MET MET GLU ASP PHE MET PHE VAL ILE PRO ALA LEU
SEQRES 31 D 523 GLN VAL ALA TYR PHE GLN ARG SER HIS ALA SER VAL TYR
SEQRES 32 D 523 PHE TYR GLU PHE GLN HIS GLN ILE ALA SER LEU LYS ASP
SEQRES 33 D 523 VAL ARG PRO THR HIS VAL LYS ALA ASP HIS ALA ASP GLU
SEQRES 34 D 523 ILE PRO PHE VAL PHE GLY TYR PHE PHE TRP ASP MET LYS
SEQRES 35 D 523 LEU ASP PHE THR GLU GLY GLU LYS LEU LEU SER ARG ARG
SEQRES 36 D 523 MET MET LYS TYR TRP ALA ASN PHE ALA ARG HIS GLY ASN
SEQRES 37 D 523 PRO ASN SER GLU GLY LEU PRO TYR TRP PRO VAL MET ASP
SEQRES 38 D 523 HIS ASP GLU GLN TYR LEU GLN LEU ASP THR GLN PRO ALA
SEQRES 39 D 523 VAL GLY ARG ALA LEU LYS SER ARG ARG LEU GLN PHE TRP
SEQRES 40 D 523 THR LYS THR LEU SER GLN LYS ILE GLN GLU LEU ARG ALA
SEQRES 41 D 523 SER GLN ASP
SEQRES 1 A 523 SER PRO GLU ALA SER PRO ILE ARG ASN THR HIS THR GLY
SEQRES 2 A 523 GLN VAL ARG GLY SER LEU VAL HIS VAL LYS ASP THR LYS
SEQRES 3 A 523 ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 A 523 PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO GLU ALA
SEQRES 5 A 523 PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR ALA HIS
SEQRES 6 A 523 PRO ALA MET CYS LEU GLN ASN LEU GLY VAL MET LYS GLU
SEQRES 7 A 523 ILE LYS LEU LYS LEU PRO PRO VAL SER THR SER GLU ASP
SEQRES 8 A 523 CYS LEU TYR LEU ASN ILE TYR THR PRO ALA HIS ALA HIS
SEQRES 9 A 523 GLU GLY SER ASN LEU PRO VAL MET VAL TRP ILE HIS GLY
SEQRES 10 A 523 GLY GLY LEU VAL ALA GLY MET ALA SER MET TYR ASP GLY
SEQRES 11 A 523 SER LEU LEU ALA ALA ILE GLU ASP LEU VAL VAL VAL THR
SEQRES 12 A 523 ILE GLN TYR ARG LEU GLY VAL LEU GLY PHE PHE SER THR
SEQRES 13 A 523 GLY ASP GLN HIS ALA ARG GLY ASN TRP GLY PHE LEU ASP
SEQRES 14 A 523 GLN VAL ALA ALA LEU ARG TRP ILE GLN GLN ASN ILE ALA
SEQRES 15 A 523 HIS PHE GLY GLY LYS PRO ASP ARG VAL THR ILE PHE GLY
SEQRES 16 A 523 GLU SER ALA GLY GLY THR SER VAL SER SER HIS VAL VAL
SEQRES 17 A 523 SER PRO MET SER LYS GLY LEU PHE HIS GLY ALA ILE MET
SEQRES 18 A 523 GLU SER GLY VAL ALA LEU LEU PRO TYR LEU ILE THR ASP
SEQRES 19 A 523 THR SER GLU MET VAL SER THR THR VAL ALA LYS LEU SER
SEQRES 20 A 523 GLY CYS GLU ALA MET ASP SER GLU ALA LEU VAL ARG CYS
SEQRES 21 A 523 LEU ARG GLY LYS SER GLU ALA GLU ILE LEU ALA ILE ASN
SEQRES 22 A 523 LYS LEU VAL GLN MET ILE PRO ALA VAL VAL ASP GLY GLU
SEQRES 23 A 523 PHE PHE PRO ARG HIS PRO LYS GLU LEU LEU ALA SER GLU
SEQRES 24 A 523 ASP PHE HIS PRO VAL PRO SER ILE ILE GLY VAL ASN ASN
SEQRES 25 A 523 ASP GLU PHE GLY TRP THR ILE PRO VAL VAL MET GLY SER
SEQRES 26 A 523 ALA GLN THR ILE LYS GLU ILE THR ARG GLU ASN LEU GLN
SEQRES 27 A 523 ALA VAL LEU LYS ASN THR THR ALA GLN LEU MET LEU PRO
SEQRES 28 A 523 PRO GLU CYS SER ASP LEU LEU MET GLU GLU TYR MET GLY
SEQRES 29 A 523 ASP THR GLU ASP ALA GLN THR LEU GLN ILE GLN PHE THR
SEQRES 30 A 523 GLU MET MET GLU ASP PHE MET PHE VAL ILE PRO ALA LEU
SEQRES 31 A 523 GLN VAL ALA TYR PHE GLN ARG SER HIS ALA SER VAL TYR
SEQRES 32 A 523 PHE TYR GLU PHE GLN HIS GLN ILE ALA SER LEU LYS ASP
SEQRES 33 A 523 VAL ARG PRO THR HIS VAL LYS ALA ASP HIS ALA ASP GLU
SEQRES 34 A 523 ILE PRO PHE VAL PHE GLY TYR PHE PHE TRP ASP MET LYS
SEQRES 35 A 523 LEU ASP PHE THR GLU GLY GLU LYS LEU LEU SER ARG ARG
SEQRES 36 A 523 MET MET LYS TYR TRP ALA ASN PHE ALA ARG HIS GLY ASN
SEQRES 37 A 523 PRO ASN SER GLU GLY LEU PRO TYR TRP PRO VAL MET ASP
SEQRES 38 A 523 HIS ASP GLU GLN TYR LEU GLN LEU ASP THR GLN PRO ALA
SEQRES 39 A 523 VAL GLY ARG ALA LEU LYS SER ARG ARG LEU GLN PHE TRP
SEQRES 40 A 523 THR LYS THR LEU SER GLN LYS ILE GLN GLU LEU ARG ALA
SEQRES 41 A 523 SER GLN ASP
SEQRES 1 B 523 SER PRO GLU ALA SER PRO ILE ARG ASN THR HIS THR GLY
SEQRES 2 B 523 GLN VAL ARG GLY SER LEU VAL HIS VAL LYS ASP THR LYS
SEQRES 3 B 523 ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 B 523 PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO GLU ALA
SEQRES 5 B 523 PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR ALA HIS
SEQRES 6 B 523 PRO ALA MET CYS LEU GLN ASN LEU GLY VAL MET LYS GLU
SEQRES 7 B 523 ILE LYS LEU LYS LEU PRO PRO VAL SER THR SER GLU ASP
SEQRES 8 B 523 CYS LEU TYR LEU ASN ILE TYR THR PRO ALA HIS ALA HIS
SEQRES 9 B 523 GLU GLY SER ASN LEU PRO VAL MET VAL TRP ILE HIS GLY
SEQRES 10 B 523 GLY GLY LEU VAL ALA GLY MET ALA SER MET TYR ASP GLY
SEQRES 11 B 523 SER LEU LEU ALA ALA ILE GLU ASP LEU VAL VAL VAL THR
SEQRES 12 B 523 ILE GLN TYR ARG LEU GLY VAL LEU GLY PHE PHE SER THR
SEQRES 13 B 523 GLY ASP GLN HIS ALA ARG GLY ASN TRP GLY PHE LEU ASP
SEQRES 14 B 523 GLN VAL ALA ALA LEU ARG TRP ILE GLN GLN ASN ILE ALA
SEQRES 15 B 523 HIS PHE GLY GLY LYS PRO ASP ARG VAL THR ILE PHE GLY
SEQRES 16 B 523 GLU SER ALA GLY GLY THR SER VAL SER SER HIS VAL VAL
SEQRES 17 B 523 SER PRO MET SER LYS GLY LEU PHE HIS GLY ALA ILE MET
SEQRES 18 B 523 GLU SER GLY VAL ALA LEU LEU PRO TYR LEU ILE THR ASP
SEQRES 19 B 523 THR SER GLU MET VAL SER THR THR VAL ALA LYS LEU SER
SEQRES 20 B 523 GLY CYS GLU ALA MET ASP SER GLU ALA LEU VAL ARG CYS
SEQRES 21 B 523 LEU ARG GLY LYS SER GLU ALA GLU ILE LEU ALA ILE ASN
SEQRES 22 B 523 LYS LEU VAL GLN MET ILE PRO ALA VAL VAL ASP GLY GLU
SEQRES 23 B 523 PHE PHE PRO ARG HIS PRO LYS GLU LEU LEU ALA SER GLU
SEQRES 24 B 523 ASP PHE HIS PRO VAL PRO SER ILE ILE GLY VAL ASN ASN
SEQRES 25 B 523 ASP GLU PHE GLY TRP THR ILE PRO VAL VAL MET GLY SER
SEQRES 26 B 523 ALA GLN THR ILE LYS GLU ILE THR ARG GLU ASN LEU GLN
SEQRES 27 B 523 ALA VAL LEU LYS ASN THR THR ALA GLN LEU MET LEU PRO
SEQRES 28 B 523 PRO GLU CYS SER ASP LEU LEU MET GLU GLU TYR MET GLY
SEQRES 29 B 523 ASP THR GLU ASP ALA GLN THR LEU GLN ILE GLN PHE THR
SEQRES 30 B 523 GLU MET MET GLU ASP PHE MET PHE VAL ILE PRO ALA LEU
SEQRES 31 B 523 GLN VAL ALA TYR PHE GLN ARG SER HIS ALA SER VAL TYR
SEQRES 32 B 523 PHE TYR GLU PHE GLN HIS GLN ILE ALA SER LEU LYS ASP
SEQRES 33 B 523 VAL ARG PRO THR HIS VAL LYS ALA ASP HIS ALA ASP GLU
SEQRES 34 B 523 ILE PRO PHE VAL PHE GLY TYR PHE PHE TRP ASP MET LYS
SEQRES 35 B 523 LEU ASP PHE THR GLU GLY GLU LYS LEU LEU SER ARG ARG
SEQRES 36 B 523 MET MET LYS TYR TRP ALA ASN PHE ALA ARG HIS GLY ASN
SEQRES 37 B 523 PRO ASN SER GLU GLY LEU PRO TYR TRP PRO VAL MET ASP
SEQRES 38 B 523 HIS ASP GLU GLN TYR LEU GLN LEU ASP THR GLN PRO ALA
SEQRES 39 B 523 VAL GLY ARG ALA LEU LYS SER ARG ARG LEU GLN PHE TRP
SEQRES 40 B 523 THR LYS THR LEU SER GLN LYS ILE GLN GLU LEU ARG ALA
SEQRES 41 B 523 SER GLN ASP
SEQRES 1 C 523 SER PRO GLU ALA SER PRO ILE ARG ASN THR HIS THR GLY
SEQRES 2 C 523 GLN VAL ARG GLY SER LEU VAL HIS VAL LYS ASP THR LYS
SEQRES 3 C 523 ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 C 523 PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO GLU ALA
SEQRES 5 C 523 PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR ALA HIS
SEQRES 6 C 523 PRO ALA MET CYS LEU GLN ASN LEU GLY VAL MET LYS GLU
SEQRES 7 C 523 ILE LYS LEU LYS LEU PRO PRO VAL SER THR SER GLU ASP
SEQRES 8 C 523 CYS LEU TYR LEU ASN ILE TYR THR PRO ALA HIS ALA HIS
SEQRES 9 C 523 GLU GLY SER ASN LEU PRO VAL MET VAL TRP ILE HIS GLY
SEQRES 10 C 523 GLY GLY LEU VAL ALA GLY MET ALA SER MET TYR ASP GLY
SEQRES 11 C 523 SER LEU LEU ALA ALA ILE GLU ASP LEU VAL VAL VAL THR
SEQRES 12 C 523 ILE GLN TYR ARG LEU GLY VAL LEU GLY PHE PHE SER THR
SEQRES 13 C 523 GLY ASP GLN HIS ALA ARG GLY ASN TRP GLY PHE LEU ASP
SEQRES 14 C 523 GLN VAL ALA ALA LEU ARG TRP ILE GLN GLN ASN ILE ALA
SEQRES 15 C 523 HIS PHE GLY GLY LYS PRO ASP ARG VAL THR ILE PHE GLY
SEQRES 16 C 523 GLU SER ALA GLY GLY THR SER VAL SER SER HIS VAL VAL
SEQRES 17 C 523 SER PRO MET SER LYS GLY LEU PHE HIS GLY ALA ILE MET
SEQRES 18 C 523 GLU SER GLY VAL ALA LEU LEU PRO TYR LEU ILE THR ASP
SEQRES 19 C 523 THR SER GLU MET VAL SER THR THR VAL ALA LYS LEU SER
SEQRES 20 C 523 GLY CYS GLU ALA MET ASP SER GLU ALA LEU VAL ARG CYS
SEQRES 21 C 523 LEU ARG GLY LYS SER GLU ALA GLU ILE LEU ALA ILE ASN
SEQRES 22 C 523 LYS LEU VAL GLN MET ILE PRO ALA VAL VAL ASP GLY GLU
SEQRES 23 C 523 PHE PHE PRO ARG HIS PRO LYS GLU LEU LEU ALA SER GLU
SEQRES 24 C 523 ASP PHE HIS PRO VAL PRO SER ILE ILE GLY VAL ASN ASN
SEQRES 25 C 523 ASP GLU PHE GLY TRP THR ILE PRO VAL VAL MET GLY SER
SEQRES 26 C 523 ALA GLN THR ILE LYS GLU ILE THR ARG GLU ASN LEU GLN
SEQRES 27 C 523 ALA VAL LEU LYS ASN THR THR ALA GLN LEU MET LEU PRO
SEQRES 28 C 523 PRO GLU CYS SER ASP LEU LEU MET GLU GLU TYR MET GLY
SEQRES 29 C 523 ASP THR GLU ASP ALA GLN THR LEU GLN ILE GLN PHE THR
SEQRES 30 C 523 GLU MET MET GLU ASP PHE MET PHE VAL ILE PRO ALA LEU
SEQRES 31 C 523 GLN VAL ALA TYR PHE GLN ARG SER HIS ALA SER VAL TYR
SEQRES 32 C 523 PHE TYR GLU PHE GLN HIS GLN ILE ALA SER LEU LYS ASP
SEQRES 33 C 523 VAL ARG PRO THR HIS VAL LYS ALA ASP HIS ALA ASP GLU
SEQRES 34 C 523 ILE PRO PHE VAL PHE GLY TYR PHE PHE TRP ASP MET LYS
SEQRES 35 C 523 LEU ASP PHE THR GLU GLY GLU LYS LEU LEU SER ARG ARG
SEQRES 36 C 523 MET MET LYS TYR TRP ALA ASN PHE ALA ARG HIS GLY ASN
SEQRES 37 C 523 PRO ASN SER GLU GLY LEU PRO TYR TRP PRO VAL MET ASP
SEQRES 38 C 523 HIS ASP GLU GLN TYR LEU GLN LEU ASP THR GLN PRO ALA
SEQRES 39 C 523 VAL GLY ARG ALA LEU LYS SER ARG ARG LEU GLN PHE TRP
SEQRES 40 C 523 THR LYS THR LEU SER GLN LYS ILE GLN GLU LEU ARG ALA
SEQRES 41 C 523 SER GLN ASP
HET NAG G 1 14
HET FUC G 2 10
HET NAG E 1 14
HET FUC E 2 10
HET NAG C 601 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 5 NAG 3(C8 H15 N O6)
FORMUL 5 FUC 2(C6 H12 O5)
FORMUL 8 HOH *571(H2 O)
HELIX 1 AA1 VAL D 70 ARG D 74 5 5
HELIX 2 AA2 GLY D 158 ASP D 166 1 9
HELIX 3 AA3 LEU D 176 PHE D 182 1 7
HELIX 4 AA4 ASN D 192 ILE D 209 1 18
HELIX 5 AA5 ALA D 210 PHE D 212 5 3
HELIX 6 AA6 SER D 225 SER D 237 1 13
HELIX 7 AA7 PRO D 238 LYS D 241 5 4
HELIX 8 AA8 SER D 264 GLY D 276 1 13
HELIX 9 AA9 ASP D 281 ARG D 290 1 10
HELIX 10 AB1 SER D 293 VAL D 304 1 12
HELIX 11 AB2 HIS D 319 SER D 326 1 8
HELIX 12 AB3 TRP D 345 MET D 351 1 7
HELIX 13 AB4 SER D 353 GLU D 359 1 7
HELIX 14 AB5 ASN D 364 LEU D 376 1 13
HELIX 15 AB6 GLU D 381 MET D 391 1 11
HELIX 16 AB7 ASP D 396 PHE D 413 1 18
HELIX 17 AB8 PHE D 413 SER D 426 1 14
HELIX 18 AB9 ILE D 439 LYS D 443 5 5
HELIX 19 AC1 GLU D 457 GLY D 463 1 7
HELIX 20 AC2 THR D 474 GLY D 495 1 22
HELIX 21 AC3 LYS D 528 LYS D 537 1 10
HELIX 22 AC4 LYS D 537 SER D 549 1 13
HELIX 23 AC5 VAL A 70 ARG A 74 5 5
HELIX 24 AC6 GLY A 158 ASP A 166 1 9
HELIX 25 AC7 LEU A 176 PHE A 182 1 7
HELIX 26 AC8 ASN A 192 ILE A 209 1 18
HELIX 27 AC9 ALA A 210 PHE A 212 5 3
HELIX 28 AD1 SER A 225 SER A 237 1 13
HELIX 29 AD2 PRO A 238 LYS A 241 5 4
HELIX 30 AD3 SER A 264 GLY A 276 1 13
HELIX 31 AD4 ASP A 281 ARG A 290 1 10
HELIX 32 AD5 SER A 293 VAL A 304 1 12
HELIX 33 AD6 HIS A 319 SER A 326 1 8
HELIX 34 AD7 TRP A 345 MET A 351 1 7
HELIX 35 AD8 SER A 353 GLU A 359 1 7
HELIX 36 AD9 ASN A 364 LEU A 376 1 13
HELIX 37 AE1 PRO A 379 GLU A 381 5 3
HELIX 38 AE2 CYS A 382 MET A 391 1 10
HELIX 39 AE3 ASP A 396 PHE A 413 1 18
HELIX 40 AE4 PHE A 413 SER A 426 1 14
HELIX 41 AE5 ILE A 439 LYS A 443 5 5
HELIX 42 AE6 GLU A 457 GLY A 463 1 7
HELIX 43 AE7 THR A 474 GLY A 495 1 22
HELIX 44 AE8 LYS A 528 LYS A 537 1 10
HELIX 45 AE9 LYS A 537 SER A 549 1 13
HELIX 46 AF1 VAL B 70 ARG B 74 5 5
HELIX 47 AF2 GLY B 158 ASP B 166 1 9
HELIX 48 AF3 LEU B 176 PHE B 182 1 7
HELIX 49 AF4 ASN B 192 ILE B 209 1 18
HELIX 50 AF5 ALA B 210 PHE B 212 5 3
HELIX 51 AF6 SER B 225 SER B 237 1 13
HELIX 52 AF7 PRO B 238 LYS B 241 5 4
HELIX 53 AF8 SER B 264 SER B 275 1 12
HELIX 54 AF9 ASP B 281 ARG B 290 1 10
HELIX 55 AG1 SER B 293 VAL B 304 1 12
HELIX 56 AG2 HIS B 319 SER B 326 1 8
HELIX 57 AG3 TRP B 345 MET B 351 1 7
HELIX 58 AG4 SER B 353 GLU B 359 1 7
HELIX 59 AG5 ASN B 364 LEU B 376 1 13
HELIX 60 AG6 PRO B 379 GLU B 381 5 3
HELIX 61 AG7 CYS B 382 MET B 391 1 10
HELIX 62 AG8 ASP B 396 PHE B 413 1 18
HELIX 63 AG9 PHE B 413 SER B 426 1 14
HELIX 64 AH1 ILE B 439 LYS B 443 5 5
HELIX 65 AH2 GLU B 457 GLY B 463 1 7
HELIX 66 AH3 THR B 474 GLY B 495 1 22
HELIX 67 AH4 LYS B 528 LYS B 537 1 10
HELIX 68 AH5 LYS B 537 SER B 549 1 13
HELIX 69 AH6 VAL C 70 ARG C 74 5 5
HELIX 70 AH7 GLY C 158 ASP C 166 1 9
HELIX 71 AH8 LEU C 176 PHE C 182 1 7
HELIX 72 AH9 ASN C 192 ILE C 209 1 18
HELIX 73 AI1 ALA C 210 PHE C 212 5 3
HELIX 74 AI2 SER C 225 SER C 237 1 13
HELIX 75 AI3 PRO C 238 LYS C 241 5 4
HELIX 76 AI4 SER C 264 GLY C 276 1 13
HELIX 77 AI5 ASP C 281 ARG C 290 1 10
HELIX 78 AI6 SER C 293 VAL C 304 1 12
HELIX 79 AI7 HIS C 319 SER C 326 1 8
HELIX 80 AI8 TRP C 345 MET C 351 1 7
HELIX 81 AI9 SER C 353 GLU C 359 1 7
HELIX 82 AJ1 ASN C 364 ALA C 374 1 11
HELIX 83 AJ2 GLU C 381 MET C 391 1 11
HELIX 84 AJ3 ASP C 396 PHE C 413 1 18
HELIX 85 AJ4 PHE C 413 SER C 426 1 14
HELIX 86 AJ5 ILE C 439 LYS C 443 5 5
HELIX 87 AJ6 GLU C 457 GLY C 463 1 7
HELIX 88 AJ7 THR C 474 GLY C 495 1 22
HELIX 89 AJ8 LYS C 528 LYS C 537 1 10
HELIX 90 AJ9 LYS C 537 ALA C 548 1 12
SHEET 1 AA1 3 ILE D 35 THR D 38 0
SHEET 2 AA1 3 GLY D 41 ARG D 44 -1 O VAL D 43 N ARG D 36
SHEET 3 AA1 3 VAL D 87 ASP D 89 1 O ARG D 88 N GLN D 42
SHEET 1 AA211 SER D 46 HIS D 49 0
SHEET 2 AA211 GLY D 56 PRO D 64 -1 O VAL D 57 N VAL D 48
SHEET 3 AA211 TYR D 122 PRO D 128 -1 O THR D 127 N HIS D 58
SHEET 4 AA211 VAL D 168 ILE D 172 -1 O VAL D 169 N TYR D 126
SHEET 5 AA211 LEU D 137 ILE D 143 1 N TRP D 142 O VAL D 170
SHEET 6 AA211 GLY D 214 GLU D 224 1 O THR D 220 N VAL D 139
SHEET 7 AA211 GLY D 246 GLU D 250 1 O GLU D 250 N GLY D 223
SHEET 8 AA211 SER D 334 ASN D 339 1 O ILE D 335 N MET D 249
SHEET 9 AA211 VAL D 430 PHE D 435 1 O PHE D 435 N VAL D 338
SHEET 10 AA211 GLN D 513 LEU D 517 1 O LEU D 515 N PHE D 432
SHEET 11 AA211 ALA D 522 ARG D 525 -1 O ALA D 522 N GLN D 516
SHEET 1 AA3 2 MET D 96 CYS D 97 0
SHEET 2 AA3 2 THR D 116 SER D 117 1 O SER D 117 N MET D 96
SHEET 1 AA4 3 ILE A 35 THR A 38 0
SHEET 2 AA4 3 GLY A 41 ARG A 44 -1 O VAL A 43 N ARG A 36
SHEET 3 AA4 3 VAL A 87 ASP A 89 1 O ARG A 88 N GLN A 42
SHEET 1 AA511 SER A 46 VAL A 48 0
SHEET 2 AA511 VAL A 57 PRO A 64 -1 O VAL A 57 N VAL A 48
SHEET 3 AA511 TYR A 122 PRO A 128 -1 O THR A 127 N HIS A 58
SHEET 4 AA511 VAL A 168 ILE A 172 -1 O VAL A 169 N TYR A 126
SHEET 5 AA511 LEU A 137 ILE A 143 1 N TRP A 142 O VAL A 170
SHEET 6 AA511 GLY A 214 GLU A 224 1 O THR A 220 N VAL A 139
SHEET 7 AA511 GLY A 246 GLU A 250 1 O GLU A 250 N GLY A 223
SHEET 8 AA511 SER A 334 ASN A 339 1 O ILE A 335 N MET A 249
SHEET 9 AA511 VAL A 430 PHE A 435 1 O PHE A 435 N VAL A 338
SHEET 10 AA511 GLN A 513 LEU A 517 1 O LEU A 515 N PHE A 432
SHEET 11 AA511 ALA A 522 ARG A 525 -1 O ALA A 522 N GLN A 516
SHEET 1 AA6 2 MET A 96 CYS A 97 0
SHEET 2 AA6 2 THR A 116 SER A 117 1 O SER A 117 N MET A 96
SHEET 1 AA7 3 ILE B 35 THR B 38 0
SHEET 2 AA7 3 GLY B 41 ARG B 44 -1 O VAL B 43 N ARG B 36
SHEET 3 AA7 3 VAL B 87 ASP B 89 1 O ARG B 88 N GLN B 42
SHEET 1 AA811 SER B 46 VAL B 48 0
SHEET 2 AA811 VAL B 57 PRO B 64 -1 O VAL B 57 N VAL B 48
SHEET 3 AA811 TYR B 122 PRO B 128 -1 O THR B 127 N HIS B 58
SHEET 4 AA811 VAL B 168 ILE B 172 -1 O VAL B 169 N TYR B 126
SHEET 5 AA811 LEU B 137 ILE B 143 1 N TRP B 142 O VAL B 170
SHEET 6 AA811 GLY B 214 GLU B 224 1 O THR B 220 N VAL B 139
SHEET 7 AA811 GLY B 246 GLU B 250 1 O GLU B 250 N GLY B 223
SHEET 8 AA811 SER B 334 ASN B 339 1 O ILE B 335 N MET B 249
SHEET 9 AA811 VAL B 430 PHE B 435 1 O PHE B 435 N VAL B 338
SHEET 10 AA811 GLN B 513 LEU B 517 1 O LEU B 515 N PHE B 432
SHEET 11 AA811 ALA B 522 ARG B 525 -1 O ALA B 522 N GLN B 516
SHEET 1 AA9 2 MET B 96 CYS B 97 0
SHEET 2 AA9 2 THR B 116 SER B 117 1 O SER B 117 N MET B 96
SHEET 1 AB1 3 ILE C 35 THR C 38 0
SHEET 2 AB1 3 GLY C 41 ARG C 44 -1 O VAL C 43 N ARG C 36
SHEET 3 AB1 3 VAL C 87 ASP C 89 1 O ARG C 88 N GLN C 42
SHEET 1 AB211 SER C 46 HIS C 49 0
SHEET 2 AB211 GLY C 56 PRO C 64 -1 O VAL C 57 N VAL C 48
SHEET 3 AB211 TYR C 122 PRO C 128 -1 O THR C 127 N HIS C 58
SHEET 4 AB211 VAL C 168 ILE C 172 -1 O VAL C 169 N TYR C 126
SHEET 5 AB211 LEU C 137 ILE C 143 1 N TRP C 142 O VAL C 170
SHEET 6 AB211 GLY C 214 GLU C 224 1 O THR C 220 N VAL C 139
SHEET 7 AB211 GLY C 246 GLU C 250 1 O GLU C 250 N GLY C 223
SHEET 8 AB211 SER C 334 ASN C 339 1 O ILE C 335 N MET C 249
SHEET 9 AB211 VAL C 430 PHE C 435 1 O PHE C 435 N VAL C 338
SHEET 10 AB211 GLN C 513 LEU C 517 1 O LEU C 515 N PHE C 432
SHEET 11 AB211 ALA C 522 ARG C 525 -1 O ALA C 522 N GLN C 516
SHEET 1 AB3 2 MET C 96 CYS C 97 0
SHEET 2 AB3 2 THR C 116 SER C 117 1 O SER C 117 N MET C 96
SSBOND 1 CYS D 97 CYS D 120 1555 1555 2.07
SSBOND 2 CYS D 277 CYS D 288 1555 1555 2.04
SSBOND 3 CYS A 97 CYS A 120 1555 1555 2.06
SSBOND 4 CYS A 277 CYS A 288 1555 1555 2.10
SSBOND 5 CYS B 97 CYS B 120 1555 1555 2.04
SSBOND 6 CYS B 277 CYS B 288 1555 1555 2.06
SSBOND 7 CYS C 97 CYS C 120 1555 1555 2.02
SSBOND 8 CYS C 277 CYS C 288 1555 1555 2.05
LINK O6 NAG G 1 C1 FUC G 2 1555 1555 1.55
LINK O6 NAG E 1 C1 FUC E 2 1555 1555 1.57
CRYST1 180.750 109.801 135.435 90.00 92.89 90.00 C 1 2 1 16
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 0.005533 0.000000 0.000279 0.00000
SCALE2 0.000000 0.009107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007393 0.00000
TER 4066 ASP D 551
TER 8138 SER A 549
TER 12169 SER B 549
TER 16245 SER C 549
MASTER 622 0 5 90 64 0 0 616864 4 78 164
END |