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HEADER HYDROLASE 19-JUL-24 9G73
TITLE CRYSTAL STRUCTURE OF MOUSE CARBOXYLESTERASE 2E (CES2E)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRETHROID HYDROLASE CES2E;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBOXYLIC ESTER HYDROLASE,CARBOXYLESTERASE 2E;
COMPND 5 EC: 3.1.1.88,3.1.1.-;
COMPND 6 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: CES2E, CES5;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK
KEYWDS CARBOXYLESTERASE 2E; PROTEIN STRUCTURE; LIPID METABOLISM; X-RAY
KEYWDS 2 CRYSTALLOGRAPHY; ALPHA/BETA-HYDROLASE FOLD; BIOCHEMISTRY; LIPID
KEYWDS 3 HYDROLYSIS; NON-ALCOHOLIC FATTY LIVER DISEASE; HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.EISNER,T.SAGMEISTER,L.RAMMER,M.OBERER
REVDAT 1 13-AUG-25 9G73 0
JRNL AUTH H.EISNER,L.RAMMER,L.RIEGLER-BERKET,C.RODRIGUEZ GAMEZ,
JRNL AUTH 2 T.SAGMEISTER,G.CHALHOUB,L.LIESINGER,R.BIRNER-GRUENBERGER,
JRNL AUTH 3 T.PAVKOV-KELLER,G.HAEMMERLE,G.SCHOISWOHL,M.OBERER
JRNL TITL CRYSTAL STRUCTURE OF MOUSE CES2E
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54111
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) : 0.176
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.023
REMARK 3 FREE R VALUE TEST SET COUNT : 2718
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
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) : 3789
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8154
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 249
REMARK 3 SOLVENT ATOMS : 698
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46100
REMARK 3 B22 (A**2) : -1.11100
REMARK 3 B33 (A**2) : 2.57200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.337
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.997
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8680 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 7983 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11803 ; 1.543 ; 1.665
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18474 ; 1.301 ; 1.597
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1047 ; 7.041 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 421 ;32.213 ;22.922
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1385 ;13.344 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;19.211 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1122 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9636 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1900 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1681 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 121 ; 0.220 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4105 ; 0.160 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 491 ; 0.178 ; 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): 4183 ; 3.018 ; 3.450
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4182 ; 3.007 ; 3.449
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5230 ; 4.875 ; 5.159
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5231 ; 4.875 ; 5.160
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4497 ; 4.134 ; 4.176
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4438 ; 4.130 ; 4.155
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6570 ; 6.499 ; 6.026
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6481 ; 6.504 ; 5.991
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 28 A 550 NULL
REMARK 3 2 B 28 B 550 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
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 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 BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9G73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1292133137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873128
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54113
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 80.646
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07550
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41570
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.190
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 (%): 54.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN STOCK SOLUTION IN 20 MM
REMARK 280 TRIS/HCL, PH 7.4, AND 150 MM NACL; SHOTGUN (SG1) SCREEN: E1 (2.0
REMARK 280 M AMMONIUM SULFATE AND 0.1 M BIS-TRIS BUFFER PH 5.5) WITH
REMARK 280 PROTEIN END CONCENTRATION OF 2.89 MG/ML IN A 0.5 UL DROP, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 74.71600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.71600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 63.46550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.62150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 63.46550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.62150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 74.71600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 63.46550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.62150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.71600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 63.46550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.62150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 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 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 TYR A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 GLY A 8
REMARK 465 TRP A 9
REMARK 465 LEU A 10
REMARK 465 ASN A 11
REMARK 465 ALA A 12
REMARK 465 VAL A 13
REMARK 465 ALA A 14
REMARK 465 CYS A 15
REMARK 465 GLY A 16
REMARK 465 VAL A 17
REMARK 465 LEU A 18
REMARK 465 LEU A 19
REMARK 465 LEU A 20
REMARK 465 VAL A 21
REMARK 465 LEU A 22
REMARK 465 HIS A 23
REMARK 465 VAL A 24
REMARK 465 GLN A 25
REMARK 465 GLY A 26
REMARK 465 GLN A 27
REMARK 465 LEU A 101
REMARK 465 MET A 102
REMARK 465 GLY A 103
REMARK 465 SER A 104
REMARK 465 GLU A 105
REMARK 465 ASP A 106
REMARK 465 SER A 552
REMARK 465 GLN A 553
REMARK 465 GLU A 554
REMARK 465 ARG A 555
REMARK 465 HIS A 556
REMARK 465 LYS A 557
REMARK 465 GLU A 558
REMARK 465 LEU A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 HIS A 562
REMARK 465 HIS A 563
REMARK 465 HIS A 564
REMARK 465 HIS A 565
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 TYR B 4
REMARK 465 LYS B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 GLY B 8
REMARK 465 TRP B 9
REMARK 465 LEU B 10
REMARK 465 ASN B 11
REMARK 465 ALA B 12
REMARK 465 VAL B 13
REMARK 465 ALA B 14
REMARK 465 CYS B 15
REMARK 465 GLY B 16
REMARK 465 VAL B 17
REMARK 465 LEU B 18
REMARK 465 LEU B 19
REMARK 465 LEU B 20
REMARK 465 VAL B 21
REMARK 465 LEU B 22
REMARK 465 HIS B 23
REMARK 465 VAL B 24
REMARK 465 GLN B 25
REMARK 465 GLY B 26
REMARK 465 LEU B 101
REMARK 465 MET B 102
REMARK 465 GLY B 103
REMARK 465 SER B 104
REMARK 465 GLU B 105
REMARK 465 GLU B 554
REMARK 465 ARG B 555
REMARK 465 HIS B 556
REMARK 465 LYS B 557
REMARK 465 GLU B 558
REMARK 465 LEU B 559
REMARK 465 HIS B 560
REMARK 465 HIS B 561
REMARK 465 HIS B 562
REMARK 465 HIS B 563
REMARK 465 HIS B 564
REMARK 465 HIS B 565
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 HOH A 954 O HOH A 1017 2.09
REMARK 500 O HOH A 701 O HOH A 915 2.10
REMARK 500 O HOH A 948 O HOH A 955 2.11
REMARK 500 O HOH B 797 O HOH B 872 2.12
REMARK 500 OD2 ASP A 220 O HOH A 701 2.13
REMARK 500 O HOH A 994 O HOH A 1038 2.13
REMARK 500 ND1 HIS A 425 O HOH A 702 2.16
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 ASP A 50 19.46 52.38
REMARK 500 ALA A 192 82.39 -158.80
REMARK 500 SER A 228 -115.66 58.92
REMARK 500 GLU A 317 -70.49 -128.73
REMARK 500 ASP A 344 59.45 -142.16
REMARK 500 TRP A 348 -64.09 -144.92
REMARK 500 PHE A 416 -52.43 -130.36
REMARK 500 LYS A 454 -130.58 -91.34
REMARK 500 ASN A 471 25.31 47.66
REMARK 500 ASP A 512 -153.31 -126.29
REMARK 500 LYS A 540 -57.01 -128.61
REMARK 500 ASP B 99 38.44 -95.08
REMARK 500 ILE B 113 34.12 -99.00
REMARK 500 ALA B 192 81.16 -157.34
REMARK 500 SER B 228 -117.15 58.45
REMARK 500 GLU B 317 -69.34 -127.04
REMARK 500 TRP B 348 -63.92 -145.86
REMARK 500 PHE B 416 -52.61 -130.23
REMARK 500 LYS B 454 -128.59 -90.69
REMARK 500 ASP B 512 -155.54 -127.52
REMARK 500 LYS B 540 -56.05 -128.03
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 A1068 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B1026 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B1027 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B1028 DISTANCE = 6.92 ANGSTROMS
DBREF 9G73 A 1 559 UNP Q8BK48 EST2E_MOUSE 1 559
DBREF 9G73 B 1 559 UNP Q8BK48 EST2E_MOUSE 1 559
SEQADV 9G73 HIS A 560 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS A 561 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS A 562 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS A 563 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS A 564 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS A 565 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS B 560 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS B 561 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS B 562 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS B 563 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS B 564 UNP Q8BK48 EXPRESSION TAG
SEQADV 9G73 HIS B 565 UNP Q8BK48 EXPRESSION TAG
SEQRES 1 A 565 MET PRO LEU TYR LYS LEU LEU GLY TRP LEU ASN ALA VAL
SEQRES 2 A 565 ALA CYS GLY VAL LEU LEU LEU VAL LEU HIS VAL GLN GLY
SEQRES 3 A 565 GLN ASP SER ALA SER PRO ILE ARG ASN THR HIS THR GLY
SEQRES 4 A 565 GLN VAL ARG GLY SER LEU VAL HIS VAL LYS ASP THR ASP
SEQRES 5 A 565 ILE ALA VAL HIS THR PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 6 A 565 PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO GLU ALA
SEQRES 7 A 565 PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR SER HIS
SEQRES 8 A 565 PRO ASN MET CYS LEU GLN ASN ASP ASN LEU MET GLY SER
SEQRES 9 A 565 GLU ASP LEU LYS MET MET ASN LEU ILE LEU PRO PRO ILE
SEQRES 10 A 565 SER MET SER GLU ASP CYS LEU TYR LEU ASN ILE TYR VAL
SEQRES 11 A 565 PRO ALA HIS ALA HIS GLU GLY SER ASN LEU PRO VAL MET
SEQRES 12 A 565 VAL TRP ILE HIS GLY GLY ALA LEU THR VAL GLY MET ALA
SEQRES 13 A 565 SER MET TYR ASP GLY SER MET LEU ALA ALA THR GLU ASP
SEQRES 14 A 565 VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY VAL LEU
SEQRES 15 A 565 GLY PHE PHE SER THR GLY ASP GLN HIS ALA LYS GLY ASN
SEQRES 16 A 565 TRP GLY TYR LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL
SEQRES 17 A 565 GLN GLN ASN ILE VAL HIS PHE GLY GLY ASN PRO ASP ARG
SEQRES 18 A 565 VAL THR ILE PHE GLY GLU SER ALA GLY GLY THR SER VAL
SEQRES 19 A 565 SER SER HIS VAL VAL SER PRO MET SER GLN GLY LEU PHE
SEQRES 20 A 565 HIS GLY ALA ILE MET GLU SER GLY VAL ALA VAL LEU PRO
SEQRES 21 A 565 ASP LEU ILE SER SER SER SER GLU MET VAL HIS ARG ILE
SEQRES 22 A 565 VAL ALA ASN LEU SER GLY CYS ALA ALA VAL ASN SER GLU
SEQRES 23 A 565 THR LEU MET CYS CYS LEU ARG GLY LYS ASN GLU ALA GLU
SEQRES 24 A 565 MET LEU ALA ILE ASN LYS VAL PHE LYS ILE ILE PRO GLY
SEQRES 25 A 565 VAL VAL ASP GLY GLU PHE LEU PRO LYS HIS PRO GLN GLU
SEQRES 26 A 565 LEU MET ALA SER LYS ASP PHE HIS PRO VAL PRO SER ILE
SEQRES 27 A 565 ILE GLY ILE ASN ASN ASP GLU TYR GLY TRP ILE LEU PRO
SEQRES 28 A 565 THR ILE MET ASP PRO ALA GLN LYS ILE GLU GLU ILE THR
SEQRES 29 A 565 ARG LYS THR LEU PRO ALA VAL LEU LYS SER THR ALA LEU
SEQRES 30 A 565 LYS MET MET LEU PRO PRO GLU CYS GLY ASP LEU LEU MET
SEQRES 31 A 565 GLU GLU TYR MET GLY ASP THR GLU ASP PRO GLU THR LEU
SEQRES 32 A 565 GLN ALA GLN PHE ARG GLU MET LYS GLY ASP PHE MET PHE
SEQRES 33 A 565 VAL ILE PRO ALA LEU GLN VAL ALA HIS PHE GLN ARG SER
SEQRES 34 A 565 HIS ALA PRO VAL TYR PHE TYR GLU PHE GLN HIS ARG PRO
SEQRES 35 A 565 SER PHE PHE LYS ASP PHE ARG PRO PRO TYR VAL LYS ALA
SEQRES 36 A 565 ASP HIS GLY ASP GLU ILE PHE LEU VAL PHE GLY TYR GLN
SEQRES 37 A 565 PHE GLY ASN ILE LYS LEU PRO TYR THR GLU GLU GLU GLU
SEQRES 38 A 565 GLN LEU SER ARG ARG ILE MET LYS TYR TRP ALA ASN PHE
SEQRES 39 A 565 ALA ARG HIS GLY ASN PRO ASN SER GLU GLY LEU PRO TYR
SEQRES 40 A 565 TRP PRO VAL MET ASP HIS ASP GLU GLN TYR LEU GLN LEU
SEQRES 41 A 565 ASP ILE GLN PRO SER VAL GLY ARG ALA LEU LYS ALA ARG
SEQRES 42 A 565 ARG LEU GLN PHE TRP THR LYS THR LEU PRO GLN LYS ILE
SEQRES 43 A 565 GLN GLU LEU LYS GLY SER GLN GLU ARG HIS LYS GLU LEU
SEQRES 44 A 565 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 565 MET PRO LEU TYR LYS LEU LEU GLY TRP LEU ASN ALA VAL
SEQRES 2 B 565 ALA CYS GLY VAL LEU LEU LEU VAL LEU HIS VAL GLN GLY
SEQRES 3 B 565 GLN ASP SER ALA SER PRO ILE ARG ASN THR HIS THR GLY
SEQRES 4 B 565 GLN VAL ARG GLY SER LEU VAL HIS VAL LYS ASP THR ASP
SEQRES 5 B 565 ILE ALA VAL HIS THR PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 6 B 565 PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO GLU ALA
SEQRES 7 B 565 PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR SER HIS
SEQRES 8 B 565 PRO ASN MET CYS LEU GLN ASN ASP ASN LEU MET GLY SER
SEQRES 9 B 565 GLU ASP LEU LYS MET MET ASN LEU ILE LEU PRO PRO ILE
SEQRES 10 B 565 SER MET SER GLU ASP CYS LEU TYR LEU ASN ILE TYR VAL
SEQRES 11 B 565 PRO ALA HIS ALA HIS GLU GLY SER ASN LEU PRO VAL MET
SEQRES 12 B 565 VAL TRP ILE HIS GLY GLY ALA LEU THR VAL GLY MET ALA
SEQRES 13 B 565 SER MET TYR ASP GLY SER MET LEU ALA ALA THR GLU ASP
SEQRES 14 B 565 VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY VAL LEU
SEQRES 15 B 565 GLY PHE PHE SER THR GLY ASP GLN HIS ALA LYS GLY ASN
SEQRES 16 B 565 TRP GLY TYR LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL
SEQRES 17 B 565 GLN GLN ASN ILE VAL HIS PHE GLY GLY ASN PRO ASP ARG
SEQRES 18 B 565 VAL THR ILE PHE GLY GLU SER ALA GLY GLY THR SER VAL
SEQRES 19 B 565 SER SER HIS VAL VAL SER PRO MET SER GLN GLY LEU PHE
SEQRES 20 B 565 HIS GLY ALA ILE MET GLU SER GLY VAL ALA VAL LEU PRO
SEQRES 21 B 565 ASP LEU ILE SER SER SER SER GLU MET VAL HIS ARG ILE
SEQRES 22 B 565 VAL ALA ASN LEU SER GLY CYS ALA ALA VAL ASN SER GLU
SEQRES 23 B 565 THR LEU MET CYS CYS LEU ARG GLY LYS ASN GLU ALA GLU
SEQRES 24 B 565 MET LEU ALA ILE ASN LYS VAL PHE LYS ILE ILE PRO GLY
SEQRES 25 B 565 VAL VAL ASP GLY GLU PHE LEU PRO LYS HIS PRO GLN GLU
SEQRES 26 B 565 LEU MET ALA SER LYS ASP PHE HIS PRO VAL PRO SER ILE
SEQRES 27 B 565 ILE GLY ILE ASN ASN ASP GLU TYR GLY TRP ILE LEU PRO
SEQRES 28 B 565 THR ILE MET ASP PRO ALA GLN LYS ILE GLU GLU ILE THR
SEQRES 29 B 565 ARG LYS THR LEU PRO ALA VAL LEU LYS SER THR ALA LEU
SEQRES 30 B 565 LYS MET MET LEU PRO PRO GLU CYS GLY ASP LEU LEU MET
SEQRES 31 B 565 GLU GLU TYR MET GLY ASP THR GLU ASP PRO GLU THR LEU
SEQRES 32 B 565 GLN ALA GLN PHE ARG GLU MET LYS GLY ASP PHE MET PHE
SEQRES 33 B 565 VAL ILE PRO ALA LEU GLN VAL ALA HIS PHE GLN ARG SER
SEQRES 34 B 565 HIS ALA PRO VAL TYR PHE TYR GLU PHE GLN HIS ARG PRO
SEQRES 35 B 565 SER PHE PHE LYS ASP PHE ARG PRO PRO TYR VAL LYS ALA
SEQRES 36 B 565 ASP HIS GLY ASP GLU ILE PHE LEU VAL PHE GLY TYR GLN
SEQRES 37 B 565 PHE GLY ASN ILE LYS LEU PRO TYR THR GLU GLU GLU GLU
SEQRES 38 B 565 GLN LEU SER ARG ARG ILE MET LYS TYR TRP ALA ASN PHE
SEQRES 39 B 565 ALA ARG HIS GLY ASN PRO ASN SER GLU GLY LEU PRO TYR
SEQRES 40 B 565 TRP PRO VAL MET ASP HIS ASP GLU GLN TYR LEU GLN LEU
SEQRES 41 B 565 ASP ILE GLN PRO SER VAL GLY ARG ALA LEU LYS ALA ARG
SEQRES 42 B 565 ARG LEU GLN PHE TRP THR LYS THR LEU PRO GLN LYS ILE
SEQRES 43 B 565 GLN GLU LEU LYS GLY SER GLN GLU ARG HIS LYS GLU LEU
SEQRES 44 B 565 HIS HIS HIS HIS HIS HIS
HET NAG C 1 27
HET NAG C 2 25
HET BMA C 3 19
HET MAN C 4 18
HET MAN C 5 18
HET FUC C 6 18
HET NAG D 1 27
HET NAG D 2 25
HET BMA D 3 19
HET MAN D 4 19
HET NAG D 5 24
HET MAN D 6 19
HET NAG D 7 24
HET FUC D 8 18
HET SO4 A 601 5
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 606 5
HET SO4 A 607 5
HET CL A 608 1
HET CL A 609 1
HET SO4 B 601 5
HET SO4 B 602 5
HET SO4 B 603 5
HET SO4 B 604 5
HET SO4 B 605 5
HET SO4 B 606 5
HET SO4 B 607 5
HET SO4 B 608 5
HET CL B 609 1
HET CL B 610 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
FORMUL 3 MAN 4(C6 H12 O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 SO4 15(O4 S 2-)
FORMUL 12 CL 4(CL 1-)
FORMUL 24 HOH *698(H2 O)
HELIX 1 AA1 VAL A 68 ARG A 72 5 5
HELIX 2 AA2 LEU A 107 LEU A 114 5 8
HELIX 3 AA3 MET A 155 TYR A 159 5 5
HELIX 4 AA4 GLY A 161 ASP A 169 1 9
HELIX 5 AA5 LEU A 179 PHE A 185 1 7
HELIX 6 AA6 ASN A 195 ILE A 212 1 18
HELIX 7 AA7 VAL A 213 PHE A 215 5 3
HELIX 8 AA8 SER A 228 SER A 240 1 13
HELIX 9 AA9 PRO A 241 GLN A 244 5 4
HELIX 10 AB1 LEU A 259 ASP A 261 5 3
HELIX 11 AB2 SER A 267 SER A 278 1 12
HELIX 12 AB3 ASN A 284 LYS A 295 1 12
HELIX 13 AB4 ASN A 296 LYS A 305 1 10
HELIX 14 AB5 HIS A 322 SER A 329 1 8
HELIX 15 AB6 TRP A 348 ASP A 355 1 8
HELIX 16 AB7 GLN A 358 ILE A 363 5 6
HELIX 17 AB8 THR A 367 MET A 379 1 13
HELIX 18 AB9 PRO A 382 GLU A 384 5 3
HELIX 19 AC1 CYS A 385 MET A 394 1 10
HELIX 20 AC2 ASP A 399 PHE A 416 1 18
HELIX 21 AC3 PHE A 416 SER A 429 1 14
HELIX 22 AC4 PRO A 442 ASP A 447 1 6
HELIX 23 AC5 GLU A 460 PHE A 465 1 6
HELIX 24 AC6 THR A 477 GLY A 498 1 22
HELIX 25 AC7 LYS A 531 LYS A 540 1 10
HELIX 26 AC8 LYS A 540 LYS A 550 1 11
HELIX 27 AC9 VAL B 68 ARG B 72 5 5
HELIX 28 AD1 LEU B 107 ILE B 113 1 7
HELIX 29 AD2 MET B 155 TYR B 159 5 5
HELIX 30 AD3 GLY B 161 ASP B 169 1 9
HELIX 31 AD4 LEU B 179 PHE B 185 1 7
HELIX 32 AD5 ASN B 195 ILE B 212 1 18
HELIX 33 AD6 VAL B 213 PHE B 215 5 3
HELIX 34 AD7 SER B 228 SER B 240 1 13
HELIX 35 AD8 PRO B 241 GLN B 244 5 4
HELIX 36 AD9 LEU B 259 ASP B 261 5 3
HELIX 37 AE1 SER B 267 SER B 278 1 12
HELIX 38 AE2 ASN B 284 LYS B 295 1 12
HELIX 39 AE3 ASN B 296 LYS B 305 1 10
HELIX 40 AE4 HIS B 322 SER B 329 1 8
HELIX 41 AE5 TRP B 348 ASP B 355 1 8
HELIX 42 AE6 GLN B 358 ILE B 363 5 6
HELIX 43 AE7 THR B 367 MET B 379 1 13
HELIX 44 AE8 PRO B 382 GLU B 384 5 3
HELIX 45 AE9 CYS B 385 MET B 394 1 10
HELIX 46 AF1 ASP B 399 PHE B 416 1 18
HELIX 47 AF2 PHE B 416 ARG B 428 1 13
HELIX 48 AF3 PRO B 442 ASP B 447 1 6
HELIX 49 AF4 GLU B 460 PHE B 465 1 6
HELIX 50 AF5 THR B 477 GLY B 498 1 22
HELIX 51 AF6 LYS B 531 LYS B 540 1 10
HELIX 52 AF7 LYS B 540 LYS B 550 1 11
HELIX 53 AF8 GLY B 551 GLN B 553 5 3
SHEET 1 AA1 3 ILE A 33 ARG A 34 0
SHEET 2 AA1 3 GLN A 40 ARG A 42 -1 O VAL A 41 N ARG A 34
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N GLN A 40
SHEET 1 AA211 SER A 44 HIS A 47 0
SHEET 2 AA211 ALA A 54 PRO A 62 -1 O VAL A 55 N VAL A 46
SHEET 3 AA211 TYR A 125 PRO A 131 -1 O VAL A 130 N HIS A 56
SHEET 4 AA211 VAL A 171 ILE A 175 -1 O VAL A 172 N TYR A 129
SHEET 5 AA211 LEU A 140 ILE A 146 1 N MET A 143 O VAL A 171
SHEET 6 AA211 GLY A 217 GLU A 227 1 O THR A 223 N VAL A 144
SHEET 7 AA211 GLY A 249 GLU A 253 1 O GLU A 253 N GLY A 226
SHEET 8 AA211 SER A 337 ASN A 342 1 O ILE A 338 N MET A 252
SHEET 9 AA211 VAL A 433 PHE A 438 1 O PHE A 438 N ILE A 341
SHEET 10 AA211 GLN A 516 LEU A 520 1 O LEU A 518 N GLU A 437
SHEET 11 AA211 SER A 525 ARG A 528 -1 O SER A 525 N GLN A 519
SHEET 1 AA3 2 ILE A 263 SER A 264 0
SHEET 2 AA3 2 GLY A 312 VAL A 313 1 O GLY A 312 N SER A 264
SHEET 1 AA4 2 GLN A 468 PHE A 469 0
SHEET 2 AA4 2 ILE A 472 LYS A 473 -1 O ILE A 472 N PHE A 469
SHEET 1 AA5 3 ILE B 33 ARG B 34 0
SHEET 2 AA5 3 GLN B 40 ARG B 42 -1 O VAL B 41 N ARG B 34
SHEET 3 AA5 3 VAL B 85 ASP B 87 1 O ARG B 86 N GLN B 40
SHEET 1 AA611 SER B 44 HIS B 47 0
SHEET 2 AA611 ALA B 54 PRO B 62 -1 O VAL B 55 N VAL B 46
SHEET 3 AA611 TYR B 125 PRO B 131 -1 O VAL B 130 N HIS B 56
SHEET 4 AA611 VAL B 171 ILE B 175 -1 O ALA B 174 N ASN B 127
SHEET 5 AA611 LEU B 140 ILE B 146 1 N MET B 143 O VAL B 171
SHEET 6 AA611 GLY B 217 GLU B 227 1 O THR B 223 N VAL B 144
SHEET 7 AA611 GLY B 249 GLU B 253 1 O GLU B 253 N GLY B 226
SHEET 8 AA611 SER B 337 ASN B 342 1 O ILE B 338 N MET B 252
SHEET 9 AA611 VAL B 433 PHE B 438 1 O PHE B 438 N ILE B 341
SHEET 10 AA611 GLN B 516 LEU B 520 1 O LEU B 518 N GLU B 437
SHEET 11 AA611 SER B 525 ARG B 528 -1 O SER B 525 N GLN B 519
SHEET 1 AA7 2 ILE B 263 SER B 264 0
SHEET 2 AA7 2 GLY B 312 VAL B 313 1 O GLY B 312 N SER B 264
SHEET 1 AA8 2 GLN B 468 PHE B 469 0
SHEET 2 AA8 2 ILE B 472 LYS B 473 -1 O ILE B 472 N PHE B 469
SSBOND 1 CYS A 95 CYS A 123 1555 1555 1.99
SSBOND 2 CYS A 280 CYS A 291 1555 1555 2.09
SSBOND 3 CYS B 95 CYS B 123 1555 1555 2.02
SSBOND 4 CYS B 280 CYS B 291 1555 1555 2.07
LINK ND2 ASN A 276 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN B 276 C1 NAG D 1 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O6 NAG C 1 C1 FUC C 6 1555 1555 1.45
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.47
LINK O6 BMA C 3 C1 MAN C 5 1555 1555 1.46
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O6 NAG D 1 C1 FUC D 8 1555 1555 1.45
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.47
LINK O6 BMA D 3 C1 MAN D 6 1555 1555 1.45
LINK O2 MAN D 4 C1 NAG D 5 1555 1555 1.48
LINK O2 MAN D 6 C1 NAG D 7 1555 1555 1.48
CRYST1 126.931 145.243 149.432 90.00 90.00 90.00 C 2 2 21 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 0.007878 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006692 0.00000
TER 7992 GLY A 551
TER 16038 GLN B 553
MASTER 433 0 33 53 36 0 0 6 9101 2 385 88
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