| 5txf-pdb | HEADER TRANSFERASE 16-NOV-16 5TXF
TITLE CRYSTAL STRUCTURE OF LECITHIN:CHOLESTEROL ACYLTRANSFERASE (LCAT) IN A
TITLE 2 CLOSED CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLCHOLINE-STEROL ACYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: LECITHIN-CHOLESTEROL ACYLTRANSFERASE,PHOSPHOLIPID-
COMPND 5 CHOLESTEROL ACYLTRANSFERASE;
COMPND 6 EC: 2.3.1.43;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LCAT;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ACYLTRANSFERASE, CHOLESTEROL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.MANTHEI,A.GLUKHOVA,J.J.G.TESMER
REVDAT 1 25-OCT-17 5TXF 0
JRNL AUTH K.A.MANTHEI,J.AHN,A.GLUKHOVA,W.YUAN,C.LARKIN,T.D.MANETT,
JRNL AUTH 2 L.CHANG,J.A.SHAYMAN,M.J.AXLEY,A.SCHWENDEMAN,J.J.G.TESMER
JRNL TITL A RETRACTABLE LID IN LECITHIN:CHOLESTEROL ACYLTRANSFERASE
JRNL TITL 2 PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATION BY
JRNL TITL 3 APOLIPOPROTEIN A-I
JRNL REF J.BIOL.CHEM. 2017
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M117.802736
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 45564
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2365
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3251
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3710
REMARK 3 BIN FREE R VALUE SET COUNT : 170
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12156
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 240
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.93000
REMARK 3 B22 (A**2) : -5.37000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.77000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.440
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.558
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 80.043
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12802 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11810 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17488 ; 1.318 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27158 ; 1.042 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1504 ; 5.921 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 592 ;30.526 ;23.243
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1936 ;13.873 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 80 ;13.030 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1906 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14250 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3090 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6040 ; 2.295 ; 6.740
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6039 ; 2.293 ; 6.740
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7536 ; 4.022 ;10.100
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7537 ; 4.023 ;10.101
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6762 ; 1.986 ; 7.061
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6762 ; 1.985 ; 7.061
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9953 ; 3.549 ;10.494
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 14421 ; 6.504 ;54.280
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 14421 ; 6.504 ;54.281
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 20 399 B 20 399 47298 0.04 0.05
REMARK 3 2 A 20 399 C 20 399 47368 0.04 0.05
REMARK 3 3 A 20 399 D 20 399 47416 0.04 0.05
REMARK 3 4 B 20 399 C 20 399 47222 0.04 0.05
REMARK 3 5 B 20 399 D 20 399 47142 0.04 0.05
REMARK 3 6 C 20 399 D 20 399 47348 0.04 0.05
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 21 B 399
REMARK 3 RESIDUE RANGE : B 501 B 505
REMARK 3 ORIGIN FOR THE GROUP (A): 84.9160 35.2330 31.1970
REMARK 3 T TENSOR
REMARK 3 T11: 0.0778 T22: 0.2416
REMARK 3 T33: 0.0980 T12: -0.0556
REMARK 3 T13: 0.0350 T23: 0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 1.2195 L22: 1.4493
REMARK 3 L33: 1.0811 L12: -0.1631
REMARK 3 L13: -0.4361 L23: 0.1081
REMARK 3 S TENSOR
REMARK 3 S11: 0.1442 S12: -0.1811 S13: -0.0141
REMARK 3 S21: -0.1444 S22: -0.2502 S23: -0.3143
REMARK 3 S31: -0.1289 S32: 0.0255 S33: 0.1060
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 21 A 399
REMARK 3 RESIDUE RANGE : A 501 A 504
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1780 30.9490 41.4610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0937 T22: 0.3227
REMARK 3 T33: 0.0446 T12: 0.0751
REMARK 3 T13: 0.0449 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.7215 L22: 1.3825
REMARK 3 L33: 0.9379 L12: -0.0471
REMARK 3 L13: -0.9927 L23: -0.1430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0981 S12: 0.2195 S13: -0.1169
REMARK 3 S21: 0.2782 S22: -0.0754 S23: 0.1634
REMARK 3 S31: -0.1360 S32: -0.0579 S33: -0.0227
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 21 C 399
REMARK 3 RESIDUE RANGE : C 501 C 505
REMARK 3 ORIGIN FOR THE GROUP (A): 71.9140 -9.9510 44.2340
REMARK 3 T TENSOR
REMARK 3 T11: 0.1254 T22: 0.2260
REMARK 3 T33: 0.0698 T12: -0.0254
REMARK 3 T13: 0.0289 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.1275 L22: 1.1476
REMARK 3 L33: 1.4463 L12: -0.2765
REMARK 3 L13: -0.3680 L23: 0.0199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0360 S12: 0.0461 S13: 0.0092
REMARK 3 S21: 0.3412 S22: -0.1544 S23: 0.0872
REMARK 3 S31: 0.1180 S32: 0.1154 S33: 0.1904
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 21 D 399
REMARK 3 RESIDUE RANGE : D 501 D 504
REMARK 3 ORIGIN FOR THE GROUP (A): 80.3010 -5.4730 0.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.1278 T22: 0.2422
REMARK 3 T33: 0.1014 T12: 0.0170
REMARK 3 T13: 0.1028 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.7509 L22: 1.3113
REMARK 3 L33: 2.5918 L12: 0.3653
REMARK 3 L13: -0.8384 L23: -0.3501
REMARK 3 S TENSOR
REMARK 3 S11: -0.0749 S12: 0.0501 S13: -0.0755
REMARK 3 S21: -0.3746 S22: -0.0281 S23: -0.3470
REMARK 3 S31: 0.0024 S32: -0.2714 S33: 0.1030
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5TXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-14; 24-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 21-ID-D; 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919; 0.984
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; PIXEL
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; DECTRIS
REMARK 200 PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48188
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 48.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 1.26200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON LPLA2 (4X90) GENERATED BY
REMARK 200 MODELLER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FORMATE, 20% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 61.76600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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 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 350
REMARK 350 BIOMOLECULE: 3
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: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
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: 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 PHE A 1
REMARK 465 TRP A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 ASN A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 PHE A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 HIS A 11
REMARK 465 THR A 12
REMARK 465 THR A 13
REMARK 465 PRO A 14
REMARK 465 LYS A 15
REMARK 465 ALA A 16
REMARK 465 GLU A 17
REMARK 465 LEU A 18
REMARK 465 SER A 19
REMARK 465 LYS A 240
REMARK 465 GLU A 241
REMARK 465 GLN A 400
REMARK 465 GLY A 401
REMARK 465 PRO A 402
REMARK 465 PRO A 403
REMARK 465 ALA A 404
REMARK 465 SER A 405
REMARK 465 PRO A 406
REMARK 465 THR A 407
REMARK 465 ALA A 408
REMARK 465 SER A 409
REMARK 465 PRO A 410
REMARK 465 GLU A 411
REMARK 465 PRO A 412
REMARK 465 PRO A 413
REMARK 465 PRO A 414
REMARK 465 PRO A 415
REMARK 465 GLU A 416
REMARK 465 HIS A 417
REMARK 465 HIS A 418
REMARK 465 HIS A 419
REMARK 465 HIS A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 PHE B 1
REMARK 465 TRP B 2
REMARK 465 LEU B 3
REMARK 465 LEU B 4
REMARK 465 ASN B 5
REMARK 465 VAL B 6
REMARK 465 LEU B 7
REMARK 465 PHE B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 HIS B 11
REMARK 465 THR B 12
REMARK 465 THR B 13
REMARK 465 PRO B 14
REMARK 465 LYS B 15
REMARK 465 ALA B 16
REMARK 465 GLU B 17
REMARK 465 LEU B 18
REMARK 465 SER B 19
REMARK 465 LYS B 240
REMARK 465 GLU B 241
REMARK 465 GLN B 400
REMARK 465 GLY B 401
REMARK 465 PRO B 402
REMARK 465 PRO B 403
REMARK 465 ALA B 404
REMARK 465 SER B 405
REMARK 465 PRO B 406
REMARK 465 THR B 407
REMARK 465 ALA B 408
REMARK 465 SER B 409
REMARK 465 PRO B 410
REMARK 465 GLU B 411
REMARK 465 PRO B 412
REMARK 465 PRO B 413
REMARK 465 PRO B 414
REMARK 465 PRO B 415
REMARK 465 GLU B 416
REMARK 465 HIS B 417
REMARK 465 HIS B 418
REMARK 465 HIS B 419
REMARK 465 HIS B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 PHE C 1
REMARK 465 TRP C 2
REMARK 465 LEU C 3
REMARK 465 LEU C 4
REMARK 465 ASN C 5
REMARK 465 VAL C 6
REMARK 465 LEU C 7
REMARK 465 PHE C 8
REMARK 465 PRO C 9
REMARK 465 PRO C 10
REMARK 465 HIS C 11
REMARK 465 THR C 12
REMARK 465 THR C 13
REMARK 465 PRO C 14
REMARK 465 LYS C 15
REMARK 465 ALA C 16
REMARK 465 GLU C 17
REMARK 465 LEU C 18
REMARK 465 SER C 19
REMARK 465 LYS C 240
REMARK 465 GLU C 241
REMARK 465 GLN C 400
REMARK 465 GLY C 401
REMARK 465 PRO C 402
REMARK 465 PRO C 403
REMARK 465 ALA C 404
REMARK 465 SER C 405
REMARK 465 PRO C 406
REMARK 465 THR C 407
REMARK 465 ALA C 408
REMARK 465 SER C 409
REMARK 465 PRO C 410
REMARK 465 GLU C 411
REMARK 465 PRO C 412
REMARK 465 PRO C 413
REMARK 465 PRO C 414
REMARK 465 PRO C 415
REMARK 465 GLU C 416
REMARK 465 HIS C 417
REMARK 465 HIS C 418
REMARK 465 HIS C 419
REMARK 465 HIS C 420
REMARK 465 HIS C 421
REMARK 465 HIS C 422
REMARK 465 PHE D 1
REMARK 465 TRP D 2
REMARK 465 LEU D 3
REMARK 465 LEU D 4
REMARK 465 ASN D 5
REMARK 465 VAL D 6
REMARK 465 LEU D 7
REMARK 465 PHE D 8
REMARK 465 PRO D 9
REMARK 465 PRO D 10
REMARK 465 HIS D 11
REMARK 465 THR D 12
REMARK 465 THR D 13
REMARK 465 PRO D 14
REMARK 465 LYS D 15
REMARK 465 ALA D 16
REMARK 465 GLU D 17
REMARK 465 LEU D 18
REMARK 465 SER D 19
REMARK 465 LYS D 240
REMARK 465 GLU D 241
REMARK 465 GLN D 400
REMARK 465 GLY D 401
REMARK 465 PRO D 402
REMARK 465 PRO D 403
REMARK 465 ALA D 404
REMARK 465 SER D 405
REMARK 465 PRO D 406
REMARK 465 THR D 407
REMARK 465 ALA D 408
REMARK 465 SER D 409
REMARK 465 PRO D 410
REMARK 465 GLU D 411
REMARK 465 PRO D 412
REMARK 465 PRO D 413
REMARK 465 PRO D 414
REMARK 465 PRO D 415
REMARK 465 GLU D 416
REMARK 465 HIS D 417
REMARK 465 HIS D 418
REMARK 465 HIS D 419
REMARK 465 HIS D 420
REMARK 465 HIS D 421
REMARK 465 HIS D 422
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 41 63.02 -151.45
REMARK 500 PRO A 94 114.07 -39.05
REMARK 500 TYR A 120 -75.29 -113.39
REMARK 500 GLU A 137 -90.64 -140.11
REMARK 500 TRP A 146 -7.40 -55.32
REMARK 500 SER A 181 -104.69 45.60
REMARK 500 SER A 225 -67.90 -98.33
REMARK 500 ILE A 231 -65.23 -93.05
REMARK 500 PHE A 287 50.75 -144.16
REMARK 500 LEU A 304 68.72 19.40
REMARK 500 ASP A 346 2.90 81.10
REMARK 500 THR A 347 -64.06 -138.34
REMARK 500 GLN A 360 108.66 -53.45
REMARK 500 TYR A 398 44.14 -99.68
REMARK 500 LEU B 32 42.40 38.61
REMARK 500 ASP B 41 63.21 -152.20
REMARK 500 PRO B 94 114.22 -38.77
REMARK 500 TYR B 120 -75.06 -112.45
REMARK 500 GLU B 137 -90.25 -140.45
REMARK 500 TRP B 146 -8.00 -55.19
REMARK 500 SER B 181 -104.49 45.77
REMARK 500 SER B 225 -67.68 -97.22
REMARK 500 ILE B 231 -63.70 -93.44
REMARK 500 PHE B 287 51.05 -143.86
REMARK 500 LEU B 304 69.64 18.91
REMARK 500 ASP B 346 2.66 80.72
REMARK 500 THR B 347 -63.66 -138.22
REMARK 500 GLN B 360 109.89 -53.72
REMARK 500 TYR B 398 44.00 -100.09
REMARK 500 LEU C 32 41.07 39.73
REMARK 500 ASP C 41 63.03 -151.93
REMARK 500 PRO C 94 114.31 -38.87
REMARK 500 TYR C 120 -74.91 -112.65
REMARK 500 GLU C 137 -90.52 -140.26
REMARK 500 TRP C 146 -8.21 -55.01
REMARK 500 SER C 181 -106.20 45.86
REMARK 500 SER C 225 -67.85 -97.00
REMARK 500 ILE C 231 -63.77 -93.79
REMARK 500 PHE C 287 51.03 -143.88
REMARK 500 LEU C 304 69.11 19.40
REMARK 500 ASP C 346 2.80 80.55
REMARK 500 THR C 347 -63.81 -137.83
REMARK 500 GLN C 360 109.23 -53.91
REMARK 500 TYR C 398 43.99 -99.85
REMARK 500 ASP D 41 62.88 -151.46
REMARK 500 PRO D 94 114.16 -39.29
REMARK 500 TYR D 120 -75.52 -113.30
REMARK 500 GLU D 137 -91.53 -141.91
REMARK 500 TRP D 146 -7.27 -55.61
REMARK 500 SER D 181 -105.49 45.38
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 502 through BMA A 504 bound to ASN A 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 501 through NAG B 502 bound to ASN B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 503 through BMA B 505 bound to ASN B 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 501 through NAG C 502 bound to ASN C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 503 through BMA C 505 bound to ASN C 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 501 bound
REMARK 800 to ASN D 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 502 through BMA D 504 bound to ASN D 384
DBREF 5TXF A 1 416 UNP P04180 LCAT_HUMAN 25 440
DBREF 5TXF B 1 416 UNP P04180 LCAT_HUMAN 25 440
DBREF 5TXF C 1 416 UNP P04180 LCAT_HUMAN 25 440
DBREF 5TXF D 1 416 UNP P04180 LCAT_HUMAN 25 440
SEQADV 5TXF HIS A 417 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS A 418 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS A 419 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS A 420 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS A 421 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS A 422 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS B 417 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS B 418 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS B 419 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS B 420 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS B 421 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS B 422 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS C 417 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS C 418 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS C 419 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS C 420 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS C 421 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS C 422 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS D 417 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS D 418 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS D 419 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS D 420 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS D 421 UNP P04180 EXPRESSION TAG
SEQADV 5TXF HIS D 422 UNP P04180 EXPRESSION TAG
SEQRES 1 A 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 A 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 A 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 A 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 A 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 A 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 A 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 A 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 A 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 A 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 A 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 A 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 A 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 A 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 A 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 A 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 A 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 A 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 A 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 A 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 A 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 A 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 A 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 A 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 A 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 A 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 A 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 A 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 A 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 A 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 A 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 A 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 A 422 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 B 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 B 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 B 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 B 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 B 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 B 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 B 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 B 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 B 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 B 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 B 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 B 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 B 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 B 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 B 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 B 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 B 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 B 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 B 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 B 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 B 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 B 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 B 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 B 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 B 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 B 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 B 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 B 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 B 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 B 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 B 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 B 422 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 C 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 C 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 C 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 C 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 C 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 C 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 C 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 C 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 C 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 C 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 C 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 C 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 C 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 C 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 C 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 C 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 C 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 C 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 C 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 C 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 C 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 C 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 C 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 C 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 C 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 C 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 C 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 C 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 C 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 C 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 C 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 C 422 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 D 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 D 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 D 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 D 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 D 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 D 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 D 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 D 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 D 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 D 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 D 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 D 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 D 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 D 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 D 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 D 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 D 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 D 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 D 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 D 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 D 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 D 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 D 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 D 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 D 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 D 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 D 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 D 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 D 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 D 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 D 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 D 422 HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET NAG A 502 14
HET NAG A 503 14
HET BMA A 504 11
HET NAG B 501 14
HET NAG B 502 14
HET NAG B 503 14
HET NAG B 504 14
HET BMA B 505 11
HET NAG C 501 14
HET NAG C 502 14
HET NAG C 503 14
HET NAG C 504 14
HET BMA C 505 11
HET NAG D 501 14
HET NAG D 502 14
HET NAG D 503 14
HET BMA D 504 11
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 5 NAG 14(C8 H15 N O6)
FORMUL 6 BMA 4(C6 H12 O6)
FORMUL 13 HOH *14(H2 O)
HELIX 1 AA1 ASP A 63 LEU A 68 5 6
HELIX 2 AA2 LEU A 70 ARG A 80 1 11
HELIX 3 AA3 THR A 106 TYR A 111 1 6
HELIX 4 AA4 LEU A 121 ASN A 131 1 11
HELIX 5 AA5 GLU A 149 GLN A 152 5 4
HELIX 6 AA6 GLN A 153 GLY A 172 1 20
HELIX 7 AA7 SER A 181 GLN A 194 1 14
HELIX 8 AA8 PRO A 195 PHE A 202 1 8
HELIX 9 AA9 ILE A 217 SER A 225 1 9
HELIX 10 AB1 SER A 249 PHE A 253 5 5
HELIX 11 AB2 ASP A 277 LEU A 285 1 9
HELIX 12 AB3 PHE A 287 ARG A 298 1 12
HELIX 13 AB4 ALA A 349 GLU A 354 1 6
HELIX 14 AB5 LEU A 355 GLN A 360 5 6
HELIX 15 AB6 SER A 383 LEU A 395 1 13
HELIX 16 AB7 ASP B 63 LEU B 68 5 6
HELIX 17 AB8 LEU B 70 ARG B 80 1 11
HELIX 18 AB9 THR B 106 TYR B 111 1 6
HELIX 19 AC1 LEU B 121 ASN B 131 1 11
HELIX 20 AC2 GLU B 149 GLN B 152 5 4
HELIX 21 AC3 GLN B 153 GLY B 172 1 20
HELIX 22 AC4 SER B 181 GLN B 194 1 14
HELIX 23 AC5 PRO B 195 PHE B 202 1 8
HELIX 24 AC6 ILE B 217 SER B 225 1 9
HELIX 25 AC7 SER B 249 PHE B 253 5 5
HELIX 26 AC8 ASP B 277 LEU B 285 1 9
HELIX 27 AC9 PHE B 287 ARG B 298 1 12
HELIX 28 AD1 ALA B 349 GLU B 354 1 6
HELIX 29 AD2 LEU B 355 GLN B 360 5 6
HELIX 30 AD3 SER B 383 LEU B 395 1 13
HELIX 31 AD4 ASP C 63 LEU C 68 5 6
HELIX 32 AD5 LEU C 70 ARG C 80 1 11
HELIX 33 AD6 THR C 106 TYR C 111 1 6
HELIX 34 AD7 LEU C 121 ASN C 131 1 11
HELIX 35 AD8 GLU C 149 GLN C 152 5 4
HELIX 36 AD9 GLN C 153 GLY C 172 1 20
HELIX 37 AE1 SER C 181 GLN C 194 1 14
HELIX 38 AE2 PRO C 195 PHE C 202 1 8
HELIX 39 AE3 ILE C 217 SER C 225 1 9
HELIX 40 AE4 SER C 249 PHE C 253 5 5
HELIX 41 AE5 ASP C 277 LEU C 285 1 9
HELIX 42 AE6 PHE C 287 ARG C 298 1 12
HELIX 43 AE7 ALA C 349 GLU C 354 1 6
HELIX 44 AE8 LEU C 355 GLN C 360 5 6
HELIX 45 AE9 SER C 383 LEU C 395 1 13
HELIX 46 AF1 ASP D 63 LEU D 68 5 6
HELIX 47 AF2 LEU D 70 ARG D 80 1 11
HELIX 48 AF3 THR D 106 TYR D 111 1 6
HELIX 49 AF4 LEU D 121 ASN D 131 1 11
HELIX 50 AF5 GLU D 149 GLN D 152 5 4
HELIX 51 AF6 GLN D 153 GLY D 172 1 20
HELIX 52 AF7 SER D 181 GLN D 194 1 14
HELIX 53 AF8 PRO D 195 PHE D 202 1 8
HELIX 54 AF9 ILE D 217 SER D 225 1 9
HELIX 55 AG1 SER D 249 PHE D 253 5 5
HELIX 56 AG2 ASP D 277 LEU D 285 1 9
HELIX 57 AG3 PHE D 287 ARG D 298 1 12
HELIX 58 AG4 ALA D 349 GLU D 354 1 6
HELIX 59 AG5 LEU D 355 GLN D 360 5 6
HELIX 60 AG6 SER D 383 LEU D 395 1 13
SHEET 1 AA1 6 VAL A 139 ALA A 141 0
SHEET 2 AA1 6 VAL A 25 VAL A 28 1 N VAL A 25 O ARG A 140
SHEET 3 AA1 6 VAL A 175 HIS A 180 1 O PHE A 176 N ILE A 26
SHEET 4 AA1 6 ILE A 203 LEU A 209 1 O ILE A 207 N LEU A 177
SHEET 5 AA1 6 VAL A 311 VAL A 317 1 O TYR A 312 N SER A 208
SHEET 6 AA1 6 VAL A 367 HIS A 373 1 O HIS A 368 N CYS A 313
SHEET 1 AA2 3 PHE A 58 TRP A 61 0
SHEET 2 AA2 3 LEU A 36 LEU A 40 -1 N ALA A 38 O PHE A 58
SHEET 3 AA2 3 VAL A 96 ARG A 99 -1 O GLN A 97 N LYS A 39
SHEET 1 AA3 2 VAL A 81 ASN A 84 0
SHEET 2 AA3 2 LEU A 89 ASN A 92 -1 O SER A 91 N VAL A 82
SHEET 1 AA4 4 ASN A 272 THR A 274 0
SHEET 2 AA4 4 VAL A 264 SER A 267 -1 N PHE A 265 O TYR A 273
SHEET 3 AA4 4 LEU A 319 ILE A 326 1 O TYR A 325 N SER A 267
SHEET 4 AA4 4 GLY A 338 GLY A 344 -1 O GLU A 342 N THR A 321
SHEET 1 AA5 6 VAL B 139 ALA B 141 0
SHEET 2 AA5 6 VAL B 25 VAL B 28 1 N VAL B 25 O ARG B 140
SHEET 3 AA5 6 VAL B 175 HIS B 180 1 O PHE B 176 N ILE B 26
SHEET 4 AA5 6 ILE B 203 LEU B 209 1 O ILE B 207 N LEU B 177
SHEET 5 AA5 6 VAL B 311 VAL B 317 1 O TYR B 312 N SER B 208
SHEET 6 AA5 6 VAL B 367 HIS B 373 1 O HIS B 368 N CYS B 313
SHEET 1 AA6 3 PHE B 58 TRP B 61 0
SHEET 2 AA6 3 LEU B 36 LEU B 40 -1 N ALA B 38 O PHE B 58
SHEET 3 AA6 3 VAL B 96 ARG B 99 -1 O GLN B 97 N LYS B 39
SHEET 1 AA7 2 VAL B 81 ASN B 84 0
SHEET 2 AA7 2 LEU B 89 ASN B 92 -1 O SER B 91 N VAL B 82
SHEET 1 AA8 4 ASN B 272 THR B 274 0
SHEET 2 AA8 4 VAL B 264 SER B 267 -1 N PHE B 265 O TYR B 273
SHEET 3 AA8 4 LEU B 319 ILE B 326 1 O TYR B 325 N SER B 267
SHEET 4 AA8 4 GLY B 338 GLY B 344 -1 O GLU B 342 N THR B 321
SHEET 1 AA9 6 VAL C 139 ALA C 141 0
SHEET 2 AA9 6 VAL C 25 VAL C 28 1 N VAL C 25 O ARG C 140
SHEET 3 AA9 6 VAL C 175 HIS C 180 1 O PHE C 176 N ILE C 26
SHEET 4 AA9 6 ILE C 203 LEU C 209 1 O ILE C 207 N LEU C 177
SHEET 5 AA9 6 VAL C 311 VAL C 317 1 O TYR C 312 N SER C 208
SHEET 6 AA9 6 VAL C 367 HIS C 373 1 O HIS C 368 N CYS C 313
SHEET 1 AB1 3 PHE C 58 TRP C 61 0
SHEET 2 AB1 3 LEU C 36 LEU C 40 -1 N ALA C 38 O PHE C 58
SHEET 3 AB1 3 VAL C 96 ARG C 99 -1 O GLN C 97 N LYS C 39
SHEET 1 AB2 2 VAL C 81 ASN C 84 0
SHEET 2 AB2 2 LEU C 89 ASN C 92 -1 O SER C 91 N VAL C 82
SHEET 1 AB3 4 ASN C 272 THR C 274 0
SHEET 2 AB3 4 VAL C 264 SER C 267 -1 N PHE C 265 O TYR C 273
SHEET 3 AB3 4 LEU C 319 ILE C 326 1 O TYR C 325 N SER C 267
SHEET 4 AB3 4 GLY C 338 GLY C 344 -1 O GLU C 342 N THR C 321
SHEET 1 AB4 6 VAL D 139 ALA D 141 0
SHEET 2 AB4 6 VAL D 25 VAL D 28 1 N VAL D 25 O ARG D 140
SHEET 3 AB4 6 VAL D 175 HIS D 180 1 O PHE D 176 N ILE D 26
SHEET 4 AB4 6 ILE D 203 LEU D 209 1 O ILE D 207 N LEU D 177
SHEET 5 AB4 6 VAL D 311 VAL D 317 1 O TYR D 312 N SER D 208
SHEET 6 AB4 6 VAL D 367 HIS D 373 1 O HIS D 368 N CYS D 313
SHEET 1 AB5 3 PHE D 58 TRP D 61 0
SHEET 2 AB5 3 LEU D 36 LEU D 40 -1 N ALA D 38 O PHE D 58
SHEET 3 AB5 3 VAL D 96 ARG D 99 -1 O GLN D 97 N LYS D 39
SHEET 1 AB6 2 VAL D 81 ASN D 84 0
SHEET 2 AB6 2 LEU D 89 ASN D 92 -1 O SER D 91 N VAL D 82
SHEET 1 AB7 4 ASN D 272 THR D 274 0
SHEET 2 AB7 4 VAL D 264 SER D 267 -1 N PHE D 265 O TYR D 273
SHEET 3 AB7 4 LEU D 319 ILE D 326 1 O TYR D 325 N SER D 267
SHEET 4 AB7 4 GLY D 338 GLY D 344 -1 O GLU D 342 N THR D 321
SSBOND 1 CYS A 50 CYS A 74 1555 1555 2.04
SSBOND 2 CYS A 313 CYS A 356 1555 1555 2.06
SSBOND 3 CYS B 50 CYS B 74 1555 1555 2.03
SSBOND 4 CYS B 313 CYS B 356 1555 1555 2.06
SSBOND 5 CYS C 50 CYS C 74 1555 1555 2.03
SSBOND 6 CYS C 313 CYS C 356 1555 1555 2.06
SSBOND 7 CYS D 50 CYS D 74 1555 1555 2.04
SSBOND 8 CYS D 313 CYS D 356 1555 1555 2.07
LINK ND2 ASN A 272 C1 NAG A 501 1555 1555 1.48
LINK ND2 ASN A 384 C1 NAG A 502 1555 1555 1.47
LINK ND2 ASN B 272 C1 NAG B 501 1555 1555 1.46
LINK ND2 ASN B 384 C1 NAG B 503 1555 1555 1.49
LINK ND2 ASN C 272 C1 NAG C 501 1555 1555 1.47
LINK ND2 ASN C 384 C1 NAG C 503 1555 1555 1.49
LINK ND2 ASN D 272 C1 NAG D 501 1555 1555 1.46
LINK ND2 ASN D 384 C1 NAG D 502 1555 1555 1.47
LINK O4 NAG A 502 C1 NAG A 503 1555 1555 1.44
LINK O4 NAG A 503 C1 BMA A 504 1555 1555 1.45
LINK O4 NAG B 501 C1 NAG B 502 1555 1555 1.44
LINK O4 NAG B 503 C1 NAG B 504 1555 1555 1.44
LINK O4 NAG B 504 C1 BMA B 505 1555 1555 1.44
LINK O4 NAG C 501 C1 NAG C 502 1555 1555 1.45
LINK O4 NAG C 503 C1 NAG C 504 1555 1555 1.45
LINK O4 NAG C 504 C1 BMA C 505 1555 1555 1.45
LINK O4 NAG D 502 C1 NAG D 503 1555 1555 1.44
LINK O4 NAG D 503 C1 BMA D 504 1555 1555 1.43
CISPEP 1 TRP A 61 LEU A 62 0 7.80
CISPEP 2 ILE A 231 PRO A 232 0 -4.82
CISPEP 3 PHE A 331 PRO A 332 0 1.97
CISPEP 4 TRP B 61 LEU B 62 0 7.75
CISPEP 5 ILE B 231 PRO B 232 0 -5.55
CISPEP 6 PHE B 331 PRO B 332 0 1.78
CISPEP 7 TRP C 61 LEU C 62 0 7.45
CISPEP 8 ILE C 231 PRO C 232 0 -5.54
CISPEP 9 PHE C 331 PRO C 332 0 1.37
CISPEP 10 TRP D 61 LEU D 62 0 8.12
CISPEP 11 ILE D 231 PRO D 232 0 -4.65
CISPEP 12 PHE D 331 PRO D 332 0 1.79
SITE 1 AC1 2 PRO A 269 ASN A 272
SITE 1 AC2 1 ASN A 384
SITE 1 AC3 3 PRO B 269 SER B 270 ASN B 272
SITE 1 AC4 1 ASN B 384
SITE 1 AC5 2 PRO C 269 ASN C 272
SITE 1 AC6 1 ASN C 384
SITE 1 AC7 2 PRO D 269 ASN D 272
SITE 1 AC8 1 ASN D 384
CRYST1 95.887 123.532 114.778 90.00 96.19 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010429 0.000000 0.001131 0.00000
SCALE2 0.000000 0.008095 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008764 0.00000
TER 3040 ARG A 399
TER 6080 ARG B 399
TER 9120 ARG C 399
TER 12160 ARG D 399
MASTER 633 0 18 60 60 0 8 612410 4 264 132
END
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