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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 25-OCT-18 6MVD
TITLE CRYSTAL STRUCTURE OF LECITHIN:CHOLESTEROL ACYLTRANSFERASE (LCAT) IN
TITLE 2 COMPLEX WITH ISOPROPYL DODEC-11-ENYLFLUOROPHOSPHONATE (IDFP) AND A
TITLE 3 SMALL MOLECULE ACTIVATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLCHOLINE-STEROL ACYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
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_TAXID: 9606
KEYWDS LCAT, ACYLTRANSFERASE, CHOLESTEROL, ACTIVATOR, TRANSFERASE,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.MANTHEI,L.CHANG,J.J.G.TESMER
REVDAT 1 05-DEC-18 6MVD 0
SPRSDE 05-DEC-18 6MVD 6DTJ
JRNL AUTH K.A.MANTHEI,S.-M.YANG,B.BALJINNYAM,L.CHANG,A.GLUKHOVA,
JRNL AUTH 2 W.YUAN,L.A.FREEMAN,D.J.MALONEY,A.SCHWENDEMAN,A.T.REMALEY,
JRNL AUTH 3 A.JADHAV,J.J.G.TESMER
JRNL TITL MOLECULAR BASIS FOR ACTIVATION OF LECITHIN:CHOLESTEROL
JRNL TITL 2 ACYLTRANSFERASE BY A COMPOUND THAT INCREASES HDL CHOLESTEROL
JRNL REF ELIFE 2018
JRNL REFN ESSN 2050-084X
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3
REMARK 3 NUMBER OF REFLECTIONS : 20413
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1145
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) : 944
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.4230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5978
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 183
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : 1.10000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.23000
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): 0.435
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.341
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.267
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6358 ; 0.008 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 5501 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8705 ; 1.331 ; 1.692
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12869 ; 0.822 ; 1.649
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 740 ; 7.215 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 329 ;33.735 ;21.763
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 948 ;16.686 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;15.087 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 786 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7046 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1252 ; 0.002 ; 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): 2972 ; 2.246 ; 5.895
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2971 ; 2.246 ; 5.895
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3708 ; 3.784 ; 8.835
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3709 ; 3.783 ; 8.835
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3386 ; 2.137 ; 6.146
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3376 ; 2.131 ; 6.136
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4979 ; 3.664 ; 9.121
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7334 ; 6.294 ;70.926
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7333 ; 6.292 ;70.939
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 21 A 505
REMARK 3 ORIGIN FOR THE GROUP (A): 112.5353 -2.4908 114.6773
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.1959
REMARK 3 T33: 0.0543 T12: -0.0157
REMARK 3 T13: 0.0487 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.7527 L22: 0.3426
REMARK 3 L33: 0.4707 L12: -0.2195
REMARK 3 L13: -0.1483 L23: 0.3824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0256 S12: -0.0269 S13: -0.0697
REMARK 3 S21: -0.0026 S22: -0.0722 S23: 0.0540
REMARK 3 S31: -0.0221 S32: -0.0227 S33: 0.0466
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 21 B 501
REMARK 3 ORIGIN FOR THE GROUP (A): 77.9617 21.1487 121.3825
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.2007
REMARK 3 T33: 0.0142 T12: 0.0472
REMARK 3 T13: 0.0193 T23: 0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 2.2058 L22: 0.6833
REMARK 3 L33: 0.4656 L12: -1.0640
REMARK 3 L13: 0.8758 L23: -0.5083
REMARK 3 S TENSOR
REMARK 3 S11: 0.1802 S12: 0.0592 S13: -0.0109
REMARK 3 S21: -0.0476 S22: -0.1340 S23: 0.0031
REMARK 3 S31: 0.0056 S32: -0.0329 S33: -0.0462
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 6MVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237662.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24440
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1000
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) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.270
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5TXF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M LITHIUM SULFATE, 0.1 M TRIS PH
REMARK 280 8.5, AND 16% PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.34850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.18850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.34850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 53.18850
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 LEU A 239
REMARK 465 LYS A 240
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 HIS A 401
REMARK 465 HIS A 402
REMARK 465 HIS A 403
REMARK 465 SER B 236
REMARK 465 ILE B 237
REMARK 465 LYS B 238
REMARK 465 LEU B 239
REMARK 465 LYS B 240
REMARK 465 GLU B 241
REMARK 465 GLU B 242
REMARK 465 GLY B 396
REMARK 465 ALA B 397
REMARK 465 HIS B 398
REMARK 465 HIS B 399
REMARK 465 HIS B 400
REMARK 465 HIS B 401
REMARK 465 HIS B 402
REMARK 465 HIS B 403
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 65.22 -162.93
REMARK 500 ASP A 44 131.89 -172.60
REMARK 500 LEU A 70 -2.05 77.57
REMARK 500 TYR A 120 -77.65 -125.92
REMARK 500 GLU A 137 -81.99 -132.37
REMARK 500 ALA A 170 -71.86 -42.54
REMARK 500 SER A 181 -135.37 60.23
REMARK 500 GLN A 229 55.45 38.06
REMARK 500 PRO A 260 137.22 -39.75
REMARK 500 PHE A 287 58.08 -146.61
REMARK 500 LEU A 304 70.28 50.03
REMARK 500 ASP A 328 -154.16 -78.18
REMARK 500 ASP A 346 -26.14 92.80
REMARK 500 ASP B 41 60.85 -162.20
REMARK 500 ASP B 44 -166.34 -123.50
REMARK 500 ASP B 56 -159.25 -146.04
REMARK 500 THR B 59 98.67 -59.03
REMARK 500 ALA B 118 79.41 -66.38
REMARK 500 TYR B 120 -71.46 -108.12
REMARK 500 ASP B 136 -12.64 73.43
REMARK 500 GLU B 137 -95.18 -97.38
REMARK 500 GLN B 153 44.67 -85.61
REMARK 500 SER B 181 -117.19 58.97
REMARK 500 TRP B 251 5.19 -153.28
REMARK 500 GLU B 261 -35.50 -36.61
REMARK 500 ASP B 277 33.69 -99.82
REMARK 500 PHE B 287 55.79 -158.82
REMARK 500 ASP B 299 75.44 -105.80
REMARK 500 LEU B 300 -52.90 -144.17
REMARK 500 ASP B 328 -158.52 -83.97
REMARK 500 ASP B 346 -45.37 95.27
REMARK 500 LEU B 370 57.67 -140.62
REMARK 500 SER B 383 132.92 -37.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 193 0.12 SIDE CHAIN
REMARK 500 ARG A 351 0.13 SIDE CHAIN
REMARK 500 ARG B 280 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 510 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 368 NE2
REMARK 620 2 HIS A 398 ND1 98.6
REMARK 620 3 HIS A 21 N 126.7 53.9
REMARK 620 4 HIS A 21 ND1 130.3 59.4 5.9
REMARK 620 5 HOH A 613 O 90.2 80.1 121.5 123.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H9A A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H94 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H94 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound
REMARK 800 to ASN A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 503 bound
REMARK 800 to ASN A 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 502 bound
REMARK 800 to ASN B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide H9A B 503 and SER B
REMARK 800 181
DBREF 6MVD A 21 397 UNP P04180 LCAT_HUMAN 45 421
DBREF 6MVD B 21 397 UNP P04180 LCAT_HUMAN 45 421
SEQADV 6MVD HIS A 398 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS A 399 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS A 400 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS A 401 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS A 402 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS A 403 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS B 398 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS B 399 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS B 400 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS B 401 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS B 402 UNP P04180 EXPRESSION TAG
SEQADV 6MVD HIS B 403 UNP P04180 EXPRESSION TAG
SEQRES 1 A 383 HIS THR ARG PRO VAL ILE LEU VAL PRO GLY CYS LEU GLY
SEQRES 2 A 383 ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO ASP VAL VAL
SEQRES 3 A 383 ASN TRP MET CYS TYR ARG LYS THR GLU ASP PHE PHE THR
SEQRES 4 A 383 ILE TRP LEU ASP LEU ASN MET PHE LEU PRO LEU GLY VAL
SEQRES 5 A 383 ASP CYS TRP ILE ASP ASN THR ARG VAL VAL TYR ASN ARG
SEQRES 6 A 383 SER SER GLY LEU VAL SER ASN ALA PRO GLY VAL GLN ILE
SEQRES 7 A 383 ARG VAL PRO GLY PHE GLY LYS THR TYR SER VAL GLU TYR
SEQRES 8 A 383 LEU ASP SER SER LYS LEU ALA GLY TYR LEU HIS THR LEU
SEQRES 9 A 383 VAL GLN ASN LEU VAL ASN ASN GLY TYR VAL ARG ASP GLU
SEQRES 10 A 383 THR VAL ARG ALA ALA PRO TYR ASP TRP ARG LEU GLU PRO
SEQRES 11 A 383 GLY GLN GLN GLU GLU TYR TYR ARG LYS LEU ALA GLY LEU
SEQRES 12 A 383 VAL GLU GLU MET HIS ALA ALA TYR GLY LYS PRO VAL PHE
SEQRES 13 A 383 LEU ILE GLY HIS SER LEU GLY CYS LEU HIS LEU LEU TYR
SEQRES 14 A 383 PHE LEU LEU ARG GLN PRO GLN ALA TRP LYS ASP ARG PHE
SEQRES 15 A 383 ILE ASP GLY PHE ILE SER LEU GLY ALA PRO TRP GLY GLY
SEQRES 16 A 383 SER ILE LYS PRO MET LEU VAL LEU ALA SER GLY ASP ASN
SEQRES 17 A 383 GLN GLY ILE PRO ILE MET SER SER ILE LYS LEU LYS GLU
SEQRES 18 A 383 GLU GLN ARG ILE THR THR THR SER PRO TRP MET PHE PRO
SEQRES 19 A 383 SER ARG MET ALA TRP PRO GLU ASP HIS VAL PHE ILE SER
SEQRES 20 A 383 THR PRO SER PHE ASN TYR THR GLY ARG ASP PHE GLN ARG
SEQRES 21 A 383 PHE PHE ALA ASP LEU HIS PHE GLU GLU GLY TRP TYR MET
SEQRES 22 A 383 TRP LEU GLN SER ARG ASP LEU LEU ALA GLY LEU PRO ALA
SEQRES 23 A 383 PRO GLY VAL GLU VAL TYR CYS LEU TYR GLY VAL GLY LEU
SEQRES 24 A 383 PRO THR PRO ARG THR TYR ILE TYR ASP HIS GLY PHE PRO
SEQRES 25 A 383 TYR THR ASP PRO VAL GLY VAL LEU TYR GLU ASP GLY ASP
SEQRES 26 A 383 ASP THR VAL ALA THR ARG SER THR GLU LEU CYS GLY LEU
SEQRES 27 A 383 TRP GLN GLY ARG GLN PRO GLN PRO VAL HIS LEU LEU PRO
SEQRES 28 A 383 LEU HIS GLY ILE GLN HIS LEU ASN MET VAL PHE SER ASN
SEQRES 29 A 383 LEU THR LEU GLU HIS ILE ASN ALA ILE LEU LEU GLY ALA
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 383 HIS THR ARG PRO VAL ILE LEU VAL PRO GLY CYS LEU GLY
SEQRES 2 B 383 ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO ASP VAL VAL
SEQRES 3 B 383 ASN TRP MET CYS TYR ARG LYS THR GLU ASP PHE PHE THR
SEQRES 4 B 383 ILE TRP LEU ASP LEU ASN MET PHE LEU PRO LEU GLY VAL
SEQRES 5 B 383 ASP CYS TRP ILE ASP ASN THR ARG VAL VAL TYR ASN ARG
SEQRES 6 B 383 SER SER GLY LEU VAL SER ASN ALA PRO GLY VAL GLN ILE
SEQRES 7 B 383 ARG VAL PRO GLY PHE GLY LYS THR TYR SER VAL GLU TYR
SEQRES 8 B 383 LEU ASP SER SER LYS LEU ALA GLY TYR LEU HIS THR LEU
SEQRES 9 B 383 VAL GLN ASN LEU VAL ASN ASN GLY TYR VAL ARG ASP GLU
SEQRES 10 B 383 THR VAL ARG ALA ALA PRO TYR ASP TRP ARG LEU GLU PRO
SEQRES 11 B 383 GLY GLN GLN GLU GLU TYR TYR ARG LYS LEU ALA GLY LEU
SEQRES 12 B 383 VAL GLU GLU MET HIS ALA ALA TYR GLY LYS PRO VAL PHE
SEQRES 13 B 383 LEU ILE GLY HIS SER LEU GLY CYS LEU HIS LEU LEU TYR
SEQRES 14 B 383 PHE LEU LEU ARG GLN PRO GLN ALA TRP LYS ASP ARG PHE
SEQRES 15 B 383 ILE ASP GLY PHE ILE SER LEU GLY ALA PRO TRP GLY GLY
SEQRES 16 B 383 SER ILE LYS PRO MET LEU VAL LEU ALA SER GLY ASP ASN
SEQRES 17 B 383 GLN GLY ILE PRO ILE MET SER SER ILE LYS LEU LYS GLU
SEQRES 18 B 383 GLU GLN ARG ILE THR THR THR SER PRO TRP MET PHE PRO
SEQRES 19 B 383 SER ARG MET ALA TRP PRO GLU ASP HIS VAL PHE ILE SER
SEQRES 20 B 383 THR PRO SER PHE ASN TYR THR GLY ARG ASP PHE GLN ARG
SEQRES 21 B 383 PHE PHE ALA ASP LEU HIS PHE GLU GLU GLY TRP TYR MET
SEQRES 22 B 383 TRP LEU GLN SER ARG ASP LEU LEU ALA GLY LEU PRO ALA
SEQRES 23 B 383 PRO GLY VAL GLU VAL TYR CYS LEU TYR GLY VAL GLY LEU
SEQRES 24 B 383 PRO THR PRO ARG THR TYR ILE TYR ASP HIS GLY PHE PRO
SEQRES 25 B 383 TYR THR ASP PRO VAL GLY VAL LEU TYR GLU ASP GLY ASP
SEQRES 26 B 383 ASP THR VAL ALA THR ARG SER THR GLU LEU CYS GLY LEU
SEQRES 27 B 383 TRP GLN GLY ARG GLN PRO GLN PRO VAL HIS LEU LEU PRO
SEQRES 28 B 383 LEU HIS GLY ILE GLN HIS LEU ASN MET VAL PHE SER ASN
SEQRES 29 B 383 LEU THR LEU GLU HIS ILE ASN ALA ILE LEU LEU GLY ALA
SEQRES 30 B 383 HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET NAG A 502 14
HET NAG A 503 14
HET H9A A 504 8
HET H94 A 505 33
HET SO4 A 506 5
HET SO4 A 507 5
HET SO4 A 508 5
HET SO4 A 509 5
HET NI A 510 1
HET NAG B 501 14
HET NAG B 502 14
HET H9A B 503 8
HET H94 B 504 33
HET SO4 B 505 5
HET SO4 B 506 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM H9A PROPAN-2-YL HYDROGEN (R)-ETHYLPHOSPHONATE
HETNAM H94 6-{4-[(4R)-4-HYDROXY-6-OXO-4-(TRIFLUOROMETHYL)-4,5,6,7-
HETNAM 2 H94 TETRAHYDRO-2H-PYRAZOLO[3,4-B]PYRIDIN-3-YL]PIPERIDIN-1-
HETNAM 3 H94 YL}-4-(TRIFLUOROMETHYL)PYRIDINE-3-CARBONITRILE
HETNAM SO4 SULFATE ION
HETNAM NI NICKEL (II) ION
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 6 H9A 2(C5 H13 O3 P)
FORMUL 7 H94 2(C19 H16 F6 N6 O2)
FORMUL 8 SO4 6(O4 S 2-)
FORMUL 12 NI NI 2+
FORMUL 19 HOH *20(H2 O)
HELIX 1 AA1 ASP A 63 PHE A 67 5 5
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 130 1 10
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 ARG A 193 1 13
HELIX 8 AA8 PRO A 195 PHE A 202 1 8
HELIX 9 AA9 ILE A 217 GLY A 226 1 10
HELIX 10 AB1 ASP A 277 LEU A 285 1 9
HELIX 11 AB2 PHE A 287 ARG A 298 1 12
HELIX 12 AB3 ALA A 349 GLU A 354 1 6
HELIX 13 AB4 LEU A 355 GLN A 360 5 6
HELIX 14 AB5 GLN A 376 MET A 380 5 5
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 130 1 10
HELIX 20 AC2 GLN B 153 GLY B 172 1 20
HELIX 21 AC3 SER B 181 GLN B 194 1 14
HELIX 22 AC4 PRO B 195 PHE B 202 1 8
HELIX 23 AC5 ILE B 217 GLY B 226 1 10
HELIX 24 AC6 ASP B 277 LEU B 285 1 9
HELIX 25 AC7 PHE B 287 ASP B 299 1 13
HELIX 26 AC8 ALA B 349 GLU B 354 1 6
HELIX 27 AC9 LEU B 355 GLN B 360 5 6
HELIX 28 AD1 LEU B 378 PHE B 382 5 5
HELIX 29 AD2 SER B 383 LEU B 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 LEU A 27 O ARG A 140
SHEET 3 AA1 6 VAL A 175 HIS A 180 1 O ILE A 178 N VAL A 28
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 LEU A 314 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 LEU A 36 O ILE A 60
SHEET 3 AA2 3 VAL A 96 ARG A 99 -1 O ARG A 99 N GLU A 37
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 GLY A 338 N ILE A 326
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 ILE B 178 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 PHE B 206
SHEET 6 AA5 6 VAL B 367 HIS B 373 1 O HIS B 368 N VAL B 311
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 ARG B 99 N GLU B 37
SHEET 1 AA7 2 VAL B 82 ASN B 84 0
SHEET 2 AA7 2 LEU B 89 SER B 91 -1 O LEU B 89 N ASN B 84
SHEET 1 AA8 2 ASP B 227 ASN B 228 0
SHEET 2 AA8 2 ILE B 231 PRO B 232 -1 O ILE B 231 N ASN B 228
SHEET 1 AA9 4 ASN B 272 THR B 274 0
SHEET 2 AA9 4 VAL B 264 SER B 267 -1 N PHE B 265 O TYR B 273
SHEET 3 AA9 4 LEU B 319 ILE B 326 1 O TYR B 325 N SER B 267
SHEET 4 AA9 4 GLY B 338 GLY B 344 -1 O LEU B 340 N ARG B 323
SSBOND 1 CYS A 50 CYS A 74 1555 1555 2.07
SSBOND 2 CYS A 313 CYS A 356 1555 1555 2.08
SSBOND 3 CYS B 50 CYS B 74 1555 1555 2.07
SSBOND 4 CYS B 313 CYS B 356 1555 1555 2.09
LINK ND2 ASN A 84 C1 NAG A 501 1555 1555 1.45
LINK OG SER A 181 P1 H9A A 504 1555 1555 1.61
LINK ND2 ASN A 272 C1 NAG A 502 1555 1555 1.42
LINK NE2 HIS A 368 NI NI A 510 1555 1555 2.27
LINK ND2 ASN A 384 C1 NAG A 503 1555 1555 1.46
LINK ND1 HIS A 398 NI NI A 510 1555 1555 2.74
LINK ND2 ASN B 84 C1 NAG B 501 1555 1555 1.45
LINK OG SER B 181 P1 H9A B 503 1555 1555 1.62
LINK ND2 ASN B 272 C1 NAG B 502 1555 1555 1.43
LINK N HIS A 21 NI NI A 510 1555 2857 2.50
LINK ND1 HIS A 21 NI NI A 510 1555 2857 2.47
LINK NI NI A 510 O HOH A 613 1555 2857 2.79
CISPEP 1 TRP A 61 LEU A 62 0 -5.77
CISPEP 2 PHE A 331 PRO A 332 0 10.33
CISPEP 3 TRP B 61 LEU B 62 0 -6.64
CISPEP 4 PHE B 331 PRO B 332 0 -3.51
SITE 1 AC1 6 GLY A 30 CYS A 31 SER A 181 LEU A 182
SITE 2 AC1 6 VAL A 348 HIS A 377
SITE 1 AC2 15 MET A 49 CYS A 50 TYR A 51 PHE A 58
SITE 2 AC2 15 ILE A 60 ASP A 63 ASN A 65 MET A 66
SITE 3 AC2 15 PRO A 69 GLY A 71 CYS A 74 TRP A 75
SITE 4 AC2 15 ASN A 78 LEU B 117 GLY B 119
SITE 1 AC3 4 ARG A 158 ARG A 193 HIS B 168 ARG B 201
SITE 1 AC4 2 ARG A 99 LYS A 159
SITE 1 AC5 4 ARG A 99 PRO A 101 GLY A 102 TYR A 107
SITE 1 AC6 1 ARG A 323
SITE 1 AC7 2 HIS A 368 HIS A 398
SITE 1 AC8 15 GLY A 119 TYR A 120 MET B 49 CYS B 50
SITE 2 AC8 15 TYR B 51 PHE B 58 ILE B 60 ASP B 63
SITE 3 AC8 15 ASN B 65 MET B 66 PRO B 69 GLY B 71
SITE 4 AC8 15 CYS B 74 TRP B 75 ASN B 78
SITE 1 AC9 4 ARG B 99 PRO B 101 GLY B 102 TYR B 107
SITE 1 AD1 1 ARG B 99
SITE 1 AD2 3 ASN A 84 SER A 86 SER A 87
SITE 1 AD3 3 PRO A 269 SER A 270 ASN A 272
SITE 1 AD4 2 ASN A 127 ASN A 384
SITE 1 AD5 2 ASN B 84 SER B 87
SITE 1 AD6 3 SER B 267 PRO B 269 ASN B 272
SITE 1 AD7 10 GLY B 30 CYS B 31 HIS B 180 LEU B 182
SITE 2 AD7 10 GLY B 183 CYS B 184 LEU B 209 GLY B 210
SITE 3 AD7 10 PRO B 212 HIS B 377
CRYST1 134.697 106.377 117.823 90.00 125.45 90.00 C 1 2 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 0.007424 0.000000 0.005286 0.00000
SCALE2 0.000000 0.009401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010419 0.00000
TER 3020 HIS A 398
TER 5980 LEU B 395
MASTER 464 0 16 29 32 0 25 6 6181 2 200 60
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