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HEADER HYDROLASE 09-DEC-19 6V7N
TITLE CRYSTAL STRUCTURE OF A HUMAN LYSOSOME RESIDENT GLYCOPROTEIN, LYSOSOMAL
TITLE 2 ACID LIPASE, AND ITS IMPLICATIONS IN CHOLESTERYL ESTER STORAGE
TITLE 3 DISEASE (CESD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOSOMAL ACID LIPASE/CHOLESTERYL ESTER HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LAL,CHOLESTERYL ESTERASE,LIPASE A,STEROL ESTERASE;
COMPND 5 EC: 3.1.1.13;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LIPA;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS LYSOSOMAL ACID LIPASE, CHOLESTERYL ESTER STORAGE DISEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HAN
REVDAT 1 17-JUN-20 6V7N 0
JRNL AUTH F.RAJAMOHAN,A.R.REYES,M.TU,N.L.NEDOMA,L.R.HOTH,A.G.SCHWAID,
JRNL AUTH 2 R.G.KURUMBAIL,J.WARD,S.HAN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN LYSOSOMAL ACID LIPASE AND ITS
JRNL TITL 2 IMPLICATIONS IN CHOLESTERYL ESTER STORAGE DISEASE (CESD).
JRNL REF J.LIPID RES. 2020
JRNL REFN ISSN 0022-2275
JRNL PMID 32482718
JRNL DOI 10.1194/JLR.RA120000748
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29950
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1518
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.71
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.17
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2881
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2244
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2738
REMARK 3 BIN R VALUE (WORKING SET) : 0.2224
REMARK 3 BIN FREE R VALUE : 0.2609
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.96
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 143
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5973
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 113
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.59270
REMARK 3 B22 (A**2) : 9.66120
REMARK 3 B33 (A**2) : 4.93150
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.320
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.567
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.263
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.541
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.265
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6276 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8551 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2096 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1048 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6276 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 802 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7012 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.12
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.48
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8963 25.1584 0.8897
REMARK 3 T TENSOR
REMARK 3 T11: -0.0538 T22: -0.1134
REMARK 3 T33: -0.1160 T12: 0.0579
REMARK 3 T13: -0.0027 T23: -0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 1.3905 L22: 1.6206
REMARK 3 L33: 2.1639 L12: -0.5208
REMARK 3 L13: 0.0626 L23: -0.2365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: 0.0852 S13: -0.0426
REMARK 3 S21: -0.0594 S22: -0.1104 S23: 0.2295
REMARK 3 S31: -0.0467 S32: -0.4611 S33: 0.0630
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4547 21.4870 -27.8880
REMARK 3 T TENSOR
REMARK 3 T11: -0.0812 T22: -0.1294
REMARK 3 T33: -0.1013 T12: -0.0797
REMARK 3 T13: 0.0001 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.1671 L22: 2.1048
REMARK 3 L33: 2.1552 L12: 0.2354
REMARK 3 L13: 0.2081 L23: 0.3332
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: -0.0630 S13: 0.0647
REMARK 3 S21: -0.0370 S22: -0.0002 S23: -0.3498
REMARK 3 S31: -0.2333 S32: 0.4357 S33: -0.0160
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6V7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1000245919.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-14
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 : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 500K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30000
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 97.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.36100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: 1HLG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 0.1 M
REMARK 280 CH3COONA, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 48.57250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.74300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.57250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.74300
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 SER A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 LEU A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 VAL A 8
REMARK 465 LYS A 50
REMARK 465 GLN A 51
REMARK 465 HIS A 52
REMARK 465 SER A 53
REMARK 465 ASP A 54
REMARK 465 LYS A 55
REMARK 465 GLY A 56
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 LYS B 4
REMARK 465 LEU B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 VAL B 8
REMARK 465 GLN B 51
REMARK 465 HIS B 52
REMARK 465 SER B 53
REMARK 465 ASP B 54
REMARK 465 LYS B 55
REMARK 465 GLY B 56
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 13 45.04 -102.15
REMARK 500 ALA A 69 -169.88 -116.81
REMARK 500 ASN A 73 -32.20 -39.76
REMARK 500 ASN A 77 -142.54 -93.74
REMARK 500 SER A 105 50.67 -117.11
REMARK 500 SER A 153 -117.58 57.39
REMARK 500 ALA A 183 -76.92 -125.00
REMARK 500 PRO A 191 -8.97 -54.80
REMARK 500 LYS A 210 -123.32 -113.06
REMARK 500 LEU A 213 77.44 -119.79
REMARK 500 HIS A 225 71.38 32.86
REMARK 500 VAL A 226 -18.35 -155.83
REMARK 500 LYS A 233 -27.81 71.43
REMARK 500 LEU A 366 -65.54 -125.95
REMARK 500 ASN B 13 42.41 -102.82
REMARK 500 ARG B 49 -71.88 -82.64
REMARK 500 ALA B 69 -169.95 -115.84
REMARK 500 ASN B 77 -142.93 -94.19
REMARK 500 ARG B 106 41.97 -108.29
REMARK 500 SER B 153 -116.56 56.69
REMARK 500 ALA B 183 -77.12 -124.67
REMARK 500 PRO B 191 -9.74 -54.62
REMARK 500 LYS B 210 -117.41 -112.33
REMARK 500 VAL B 226 -2.09 -157.39
REMARK 500 LYS B 233 -33.26 64.05
REMARK 500 ASN B 341 69.00 -115.52
REMARK 500 LEU B 366 -64.93 -125.95
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 A 577 DISTANCE = 7.41 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound
REMARK 800 to ASN A 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 402 through NAG A 403 bound to ASN A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound
REMARK 800 to ASN B 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound
REMARK 800 to ASN B 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 403 through NAG B 404 bound to ASN B 252
DBREF 6V7N A 1 378 UNP P38571 LICH_HUMAN 22 399
DBREF 6V7N B 1 378 UNP P38571 LICH_HUMAN 22 399
SEQADV 6V7N GLN A 51 UNP P38571 ASN 72 ENGINEERED MUTATION
SEQADV 6V7N GLN A 80 UNP P38571 ASN 101 ENGINEERED MUTATION
SEQADV 6V7N GLN A 300 UNP P38571 ASN 321 ENGINEERED MUTATION
SEQADV 6V7N ALA A 379 UNP P38571 EXPRESSION TAG
SEQADV 6V7N SER A 380 UNP P38571 EXPRESSION TAG
SEQADV 6V7N GLU A 381 UNP P38571 EXPRESSION TAG
SEQADV 6V7N ASN A 382 UNP P38571 EXPRESSION TAG
SEQADV 6V7N ASN A 383 UNP P38571 EXPRESSION TAG
SEQADV 6V7N LEU A 384 UNP P38571 EXPRESSION TAG
SEQADV 6V7N GLN B 51 UNP P38571 ASN 72 ENGINEERED MUTATION
SEQADV 6V7N GLN B 80 UNP P38571 ASN 101 ENGINEERED MUTATION
SEQADV 6V7N GLN B 300 UNP P38571 ASN 321 ENGINEERED MUTATION
SEQADV 6V7N ALA B 379 UNP P38571 EXPRESSION TAG
SEQADV 6V7N SER B 380 UNP P38571 EXPRESSION TAG
SEQADV 6V7N GLU B 381 UNP P38571 EXPRESSION TAG
SEQADV 6V7N ASN B 382 UNP P38571 EXPRESSION TAG
SEQADV 6V7N ASN B 383 UNP P38571 EXPRESSION TAG
SEQADV 6V7N LEU B 384 UNP P38571 EXPRESSION TAG
SEQRES 1 A 384 SER GLY GLY LYS LEU THR ALA VAL ASP PRO GLU THR ASN
SEQRES 2 A 384 MET ASN VAL SER GLU ILE ILE SER TYR TRP GLY PHE PRO
SEQRES 3 A 384 SER GLU GLU TYR LEU VAL GLU THR GLU ASP GLY TYR ILE
SEQRES 4 A 384 LEU CYS LEU ASN ARG ILE PRO HIS GLY ARG LYS GLN HIS
SEQRES 5 A 384 SER ASP LYS GLY PRO LYS PRO VAL VAL PHE LEU GLN HIS
SEQRES 6 A 384 GLY LEU LEU ALA ASP SER SER ASN TRP VAL THR ASN LEU
SEQRES 7 A 384 ALA GLN SER SER LEU GLY PHE ILE LEU ALA ASP ALA GLY
SEQRES 8 A 384 PHE ASP VAL TRP MET GLY ASN SER ARG GLY ASN THR TRP
SEQRES 9 A 384 SER ARG LYS HIS LYS THR LEU SER VAL SER GLN ASP GLU
SEQRES 10 A 384 PHE TRP ALA PHE SER TYR ASP GLU MET ALA LYS TYR ASP
SEQRES 11 A 384 LEU PRO ALA SER ILE ASN PHE ILE LEU ASN LYS THR GLY
SEQRES 12 A 384 GLN GLU GLN VAL TYR TYR VAL GLY HIS SER GLN GLY THR
SEQRES 13 A 384 THR ILE GLY PHE ILE ALA PHE SER GLN ILE PRO GLU LEU
SEQRES 14 A 384 ALA LYS ARG ILE LYS MET PHE PHE ALA LEU GLY PRO VAL
SEQRES 15 A 384 ALA SER VAL ALA PHE CYS THR SER PRO MET ALA LYS LEU
SEQRES 16 A 384 GLY ARG LEU PRO ASP HIS LEU ILE LYS ASP LEU PHE GLY
SEQRES 17 A 384 ASP LYS GLU PHE LEU PRO GLN SER ALA PHE LEU LYS TRP
SEQRES 18 A 384 LEU GLY THR HIS VAL CYS THR HIS VAL ILE LEU LYS GLU
SEQRES 19 A 384 LEU CYS GLY ASN LEU CYS PHE LEU LEU CYS GLY PHE ASN
SEQRES 20 A 384 GLU ARG ASN LEU ASN MET SER ARG VAL ASP VAL TYR THR
SEQRES 21 A 384 THR HIS SER PRO ALA GLY THR SER VAL GLN ASN MET LEU
SEQRES 22 A 384 HIS TRP SER GLN ALA VAL LYS PHE GLN LYS PHE GLN ALA
SEQRES 23 A 384 PHE ASP TRP GLY SER SER ALA LYS ASN TYR PHE HIS TYR
SEQRES 24 A 384 GLN GLN SER TYR PRO PRO THR TYR ASN VAL LYS ASP MET
SEQRES 25 A 384 LEU VAL PRO THR ALA VAL TRP SER GLY GLY HIS ASP TRP
SEQRES 26 A 384 LEU ALA ASP VAL TYR ASP VAL ASN ILE LEU LEU THR GLN
SEQRES 27 A 384 ILE THR ASN LEU VAL PHE HIS GLU SER ILE PRO GLU TRP
SEQRES 28 A 384 GLU HIS LEU ASP PHE ILE TRP GLY LEU ASP ALA PRO TRP
SEQRES 29 A 384 ARG LEU TYR ASN LYS ILE ILE ASN LEU MET ARG LYS TYR
SEQRES 30 A 384 GLN ALA SER GLU ASN ASN LEU
SEQRES 1 B 384 SER GLY GLY LYS LEU THR ALA VAL ASP PRO GLU THR ASN
SEQRES 2 B 384 MET ASN VAL SER GLU ILE ILE SER TYR TRP GLY PHE PRO
SEQRES 3 B 384 SER GLU GLU TYR LEU VAL GLU THR GLU ASP GLY TYR ILE
SEQRES 4 B 384 LEU CYS LEU ASN ARG ILE PRO HIS GLY ARG LYS GLN HIS
SEQRES 5 B 384 SER ASP LYS GLY PRO LYS PRO VAL VAL PHE LEU GLN HIS
SEQRES 6 B 384 GLY LEU LEU ALA ASP SER SER ASN TRP VAL THR ASN LEU
SEQRES 7 B 384 ALA GLN SER SER LEU GLY PHE ILE LEU ALA ASP ALA GLY
SEQRES 8 B 384 PHE ASP VAL TRP MET GLY ASN SER ARG GLY ASN THR TRP
SEQRES 9 B 384 SER ARG LYS HIS LYS THR LEU SER VAL SER GLN ASP GLU
SEQRES 10 B 384 PHE TRP ALA PHE SER TYR ASP GLU MET ALA LYS TYR ASP
SEQRES 11 B 384 LEU PRO ALA SER ILE ASN PHE ILE LEU ASN LYS THR GLY
SEQRES 12 B 384 GLN GLU GLN VAL TYR TYR VAL GLY HIS SER GLN GLY THR
SEQRES 13 B 384 THR ILE GLY PHE ILE ALA PHE SER GLN ILE PRO GLU LEU
SEQRES 14 B 384 ALA LYS ARG ILE LYS MET PHE PHE ALA LEU GLY PRO VAL
SEQRES 15 B 384 ALA SER VAL ALA PHE CYS THR SER PRO MET ALA LYS LEU
SEQRES 16 B 384 GLY ARG LEU PRO ASP HIS LEU ILE LYS ASP LEU PHE GLY
SEQRES 17 B 384 ASP LYS GLU PHE LEU PRO GLN SER ALA PHE LEU LYS TRP
SEQRES 18 B 384 LEU GLY THR HIS VAL CYS THR HIS VAL ILE LEU LYS GLU
SEQRES 19 B 384 LEU CYS GLY ASN LEU CYS PHE LEU LEU CYS GLY PHE ASN
SEQRES 20 B 384 GLU ARG ASN LEU ASN MET SER ARG VAL ASP VAL TYR THR
SEQRES 21 B 384 THR HIS SER PRO ALA GLY THR SER VAL GLN ASN MET LEU
SEQRES 22 B 384 HIS TRP SER GLN ALA VAL LYS PHE GLN LYS PHE GLN ALA
SEQRES 23 B 384 PHE ASP TRP GLY SER SER ALA LYS ASN TYR PHE HIS TYR
SEQRES 24 B 384 GLN GLN SER TYR PRO PRO THR TYR ASN VAL LYS ASP MET
SEQRES 25 B 384 LEU VAL PRO THR ALA VAL TRP SER GLY GLY HIS ASP TRP
SEQRES 26 B 384 LEU ALA ASP VAL TYR ASP VAL ASN ILE LEU LEU THR GLN
SEQRES 27 B 384 ILE THR ASN LEU VAL PHE HIS GLU SER ILE PRO GLU TRP
SEQRES 28 B 384 GLU HIS LEU ASP PHE ILE TRP GLY LEU ASP ALA PRO TRP
SEQRES 29 B 384 ARG LEU TYR ASN LYS ILE ILE ASN LEU MET ARG LYS TYR
SEQRES 30 B 384 GLN ALA SER GLU ASN ASN LEU
HET NAG A 401 14
HET NAG A 402 14
HET NAG A 403 14
HET SO4 A 404 5
HET NAG B 401 14
HET NAG B 402 14
HET NAG B 403 14
HET NAG B 404 14
HET SO4 B 405 5
HET SO4 B 406 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 11 HOH *155(H2 O)
HELIX 1 AA1 ASN A 15 TRP A 23 1 9
HELIX 2 AA2 ASP A 70 VAL A 75 5 6
HELIX 3 AA3 SER A 82 ALA A 90 1 9
HELIX 4 AA4 GLN A 115 ALA A 120 5 6
HELIX 5 AA5 SER A 122 TYR A 129 1 8
HELIX 6 AA6 TYR A 129 GLY A 143 1 15
HELIX 7 AA7 SER A 153 ILE A 166 1 14
HELIX 8 AA8 ILE A 166 LYS A 171 1 6
HELIX 9 AA9 SER A 190 ARG A 197 1 8
HELIX 10 AB1 PRO A 199 GLY A 208 1 10
HELIX 11 AB2 GLN A 215 THR A 224 1 10
HELIX 12 AB3 LYS A 233 GLY A 237 5 5
HELIX 13 AB4 ASN A 238 GLY A 245 1 8
HELIX 14 AB5 ASN A 247 LEU A 251 5 5
HELIX 15 AB6 ARG A 255 SER A 263 1 9
HELIX 16 AB7 SER A 268 GLN A 282 1 15
HELIX 17 AB8 SER A 291 GLN A 300 1 10
HELIX 18 AB9 ASN A 308 MET A 312 5 5
HELIX 19 AC1 ASP A 328 THR A 337 1 10
HELIX 20 AC2 LEU A 354 GLY A 359 1 6
HELIX 21 AC3 ASP A 361 LEU A 366 1 6
HELIX 22 AC4 LEU A 366 ASN A 383 1 18
HELIX 23 AC5 ASN B 15 TRP B 23 1 9
HELIX 24 AC6 ASP B 70 VAL B 75 5 6
HELIX 25 AC7 SER B 82 ALA B 90 1 9
HELIX 26 AC8 GLN B 115 ALA B 120 5 6
HELIX 27 AC9 SER B 122 TYR B 129 1 8
HELIX 28 AD1 TYR B 129 GLY B 143 1 15
HELIX 29 AD2 SER B 153 ILE B 166 1 14
HELIX 30 AD3 ILE B 166 LYS B 171 1 6
HELIX 31 AD4 SER B 190 ARG B 197 1 8
HELIX 32 AD5 PRO B 199 GLY B 208 1 10
HELIX 33 AD6 GLN B 215 GLY B 223 1 9
HELIX 34 AD7 LYS B 233 GLY B 237 5 5
HELIX 35 AD8 ASN B 238 GLY B 245 1 8
HELIX 36 AD9 ASN B 247 LEU B 251 5 5
HELIX 37 AE1 ARG B 255 SER B 263 1 9
HELIX 38 AE2 SER B 268 GLN B 282 1 15
HELIX 39 AE3 SER B 291 GLN B 300 1 10
HELIX 40 AE4 ASN B 308 MET B 312 5 5
HELIX 41 AE5 ASP B 328 THR B 337 1 10
HELIX 42 AE6 LEU B 354 GLY B 359 1 6
HELIX 43 AE7 ASP B 361 LEU B 366 1 6
HELIX 44 AE8 LEU B 366 ASN B 383 1 18
SHEET 1 AA1 3 GLU A 28 GLU A 33 0
SHEET 2 AA1 3 TYR A 38 ILE A 45 -1 O LEU A 42 N TYR A 30
SHEET 3 AA1 3 LYS A 107 HIS A 108 -1 O LYS A 107 N ILE A 39
SHEET 1 AA2 8 GLU A 28 GLU A 33 0
SHEET 2 AA2 8 TYR A 38 ILE A 45 -1 O LEU A 42 N TYR A 30
SHEET 3 AA2 8 ASP A 93 GLY A 97 -1 O MET A 96 N ASN A 43
SHEET 4 AA2 8 VAL A 60 GLN A 64 1 N VAL A 61 O TRP A 95
SHEET 5 AA2 8 VAL A 147 HIS A 152 1 O VAL A 150 N PHE A 62
SHEET 6 AA2 8 ILE A 173 LEU A 179 1 O PHE A 177 N TYR A 149
SHEET 7 AA2 8 THR A 316 GLY A 321 1 O ALA A 317 N ALA A 178
SHEET 8 AA2 8 LEU A 342 ILE A 348 1 O ILE A 348 N SER A 320
SHEET 1 AA3 3 GLU B 28 GLU B 33 0
SHEET 2 AA3 3 TYR B 38 ILE B 45 -1 O LEU B 42 N TYR B 30
SHEET 3 AA3 3 LYS B 107 HIS B 108 -1 O LYS B 107 N ILE B 39
SHEET 1 AA4 8 GLU B 28 GLU B 33 0
SHEET 2 AA4 8 TYR B 38 ILE B 45 -1 O LEU B 42 N TYR B 30
SHEET 3 AA4 8 ASP B 93 GLY B 97 -1 O MET B 96 N ASN B 43
SHEET 4 AA4 8 VAL B 60 GLN B 64 1 N VAL B 61 O TRP B 95
SHEET 5 AA4 8 VAL B 147 HIS B 152 1 O VAL B 150 N PHE B 62
SHEET 6 AA4 8 ILE B 173 LEU B 179 1 O PHE B 177 N TYR B 149
SHEET 7 AA4 8 THR B 316 GLY B 321 1 O ALA B 317 N ALA B 178
SHEET 8 AA4 8 LEU B 342 ILE B 348 1 O ILE B 348 N SER B 320
SSBOND 1 CYS A 227 CYS A 236 1555 1555 2.04
SSBOND 2 CYS B 227 CYS B 236 1555 1555 2.04
LINK ND2 ASN A 15 C1 NAG A 401 1555 1555 1.43
LINK ND2 ASN A 252 C1 NAG A 402 1555 1555 1.43
LINK ND2 ASN B 15 C1 NAG B 401 1555 1555 1.43
LINK ND2 ASN B 140 C1 NAG B 402 1555 1555 1.44
LINK ND2 ASN B 252 C1 NAG B 403 1555 1555 1.43
LINK O4 NAG A 402 C1 NAG A 403 1555 1555 1.43
LINK O4 NAG B 403 C1 NAG B 404 1555 1555 1.43
CISPEP 1 SER A 263 PRO A 264 0 1.05
CISPEP 2 SER B 263 PRO B 264 0 0.36
SITE 1 AC1 4 GLN A 301 PRO A 305 THR A 306 ARG B 172
SITE 1 AC2 5 GLN B 301 TYR B 303 PRO B 304 PRO B 305
SITE 2 AC2 5 THR B 306
SITE 1 AC3 2 SER B 112 VAL B 113
SITE 1 AC4 5 ASN A 15 GLU A 18 GLU A 29 HOH A 513
SITE 2 AC4 5 HOH A 534
SITE 1 AC5 6 ASP A 9 LEU A 78 ASN A 252 ARG A 255
SITE 2 AC5 6 HOH A 510 HOH A 523
SITE 1 AC6 3 ASN B 15 GLU B 18 GLU B 29
SITE 1 AC7 2 ASN B 140 LYS B 141
SITE 1 AC8 4 ASP B 9 LEU B 78 ASN B 252 ARG B 255
CRYST1 97.145 165.486 60.360 90.00 90.00 90.00 P 21 21 2 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 0.010294 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006043 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016567 0.00000
TER 2983 LEU A 384
TER 5975 LEU B 384
MASTER 385 0 10 44 22 0 11 6 6241 2 122 60
END |