HEADER HYDROLASE 09-OCT-01 1K4Y
TITLE CRYSTAL STRUCTURE OF RABBIT LIVER CARBOXYLESTERASE IN COMPLEX WITH 4-
TITLE 2 PIPERIDINO-PIPERIDINE
CAVEAT 1K4Y NAG B 2 HAS WRONG CHIRALITY AT ATOM C1 NAG C 2 HAS WRONG
CAVEAT 2 1K4Y CHIRALITY AT ATOM C1 MAN C 3 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 1K4Y MAN C 4 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HYDROLASE, ESTERASE, SIDE DOOR, CAMPTOTHECIN, IRINOTECAN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BENCHARIT,C.L.MORTON,E.L.HOWARD-WILLIAMS,M.K.DANKS,P.M.POTTER,
AUTHOR 2 M.R.REDINBO
REVDAT 4 29-JUL-20 1K4Y 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 13-JUL-11 1K4Y 1 VERSN
REVDAT 2 24-FEB-09 1K4Y 1 VERSN
REVDAT 1 01-MAY-02 1K4Y 0
JRNL AUTH S.BENCHARIT,C.L.MORTON,E.L.HOWARD-WILLIAMS,M.K.DANKS,
JRNL AUTH 2 P.M.POTTER,M.R.REDINBO
JRNL TITL STRUCTURAL INSIGHTS INTO CPT-11 ACTIVATION BY MAMMALIAN
JRNL TITL 2 CARBOXYLESTERASES.
JRNL REF NAT.STRUCT.BIOL. V. 9 337 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11967565
JRNL DOI 10.1038/NSB790
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4898621.060
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 21233
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 SET) : 0.229
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1569
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3344
REMARK 3 BIN R VALUE (WORKING SET) : 0.3570
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 245
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 101
REMARK 3 SOLVENT ATOMS : 383
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -20.33000
REMARK 3 B22 (A**2) : -20.33000
REMARK 3 B33 (A**2) : 40.65000
REMARK 3 B12 (A**2) : -3.70000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.51
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.460 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.490 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.920 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.870 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 53.30
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : E20.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : E20.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K4Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21233
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CITRATE, LITHIUM
REMARK 280 SULFATE, GLYCEROL, PH 5.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 55.11500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 31.82066
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 94.17333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 55.11500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 31.82066
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 94.17333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 55.11500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 31.82066
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 94.17333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 55.11500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 31.82066
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 94.17333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 55.11500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 31.82066
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 94.17333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 55.11500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 31.82066
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 94.17333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 63.64132
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 188.34667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 63.64132
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 188.34667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 63.64132
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 188.34667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 63.64132
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 188.34667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 63.64132
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 188.34667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 63.64132
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 188.34667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE PROTEIN IS A MONOMER IN ONE ASYMMETRIC UNIT.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLY A 355
REMARK 465 TRP A 356
REMARK 465 ILE A 357
REMARK 465 ILE A 358
REMARK 465 PRO A 359
REMARK 465 MET A 360
REMARK 465 GLN A 361
REMARK 465 MET A 362
REMARK 465 LEU A 363
REMARK 465 GLY A 364
REMARK 465 TYR A 365
REMARK 465 PRO A 366
REMARK 465 LEU A 367
REMARK 465 SER A 368
REMARK 465 GLU A 369
REMARK 465 GLY A 370
REMARK 465 TYR A 450
REMARK 465 ARG A 451
REMARK 465 PRO A 452
REMARK 465 SER A 453
REMARK 465 PHE A 454
REMARK 465 SER A 455
REMARK 465 SER A 456
REMARK 465 ASP A 457
REMARK 465 MET A 458
REMARK 465 ARG A 459
REMARK 465 PRO A 460
REMARK 465 LYS A 461
REMARK 465 THR A 462
REMARK 465 VAL A 463
REMARK 465 ILE A 464
REMARK 465 GLY A 465
REMARK 465 ASP A 466
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O3 NAG C 1 N2 NAG C 2 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 59 55.73 -68.70
REMARK 500 GLN A 89 -179.38 -170.76
REMARK 500 ARG A 130 76.42 -101.92
REMARK 500 SER A 185 74.31 -173.54
REMARK 500 ASN A 204 -29.04 -140.99
REMARK 500 SER A 221 -128.37 59.65
REMARK 500 THR A 260 38.04 -147.79
REMARK 500 ALA A 304 139.36 172.73
REMARK 500 PRO A 311 1.31 -62.93
REMARK 500 ALA A 316 63.77 -65.83
REMARK 500 LYS A 338 18.02 55.51
REMARK 500 TYR A 340 -155.24 -96.04
REMARK 500 GLN A 351 70.12 -63.13
REMARK 500 GLN A 352 147.84 -171.95
REMARK 500 ASN A 389 83.15 37.00
REMARK 500 THR A 395 -60.33 -15.76
REMARK 500 GLU A 400 1.95 -60.52
REMARK 500 THR A 406 -79.51 -93.96
REMARK 500 LYS A 412 40.10 -91.85
REMARK 500 PHE A 425 -36.70 -133.74
REMARK 500 ASP A 438 -6.48 -55.47
REMARK 500 PRO A 478 4.68 -51.62
REMARK 500 LEU A 480 34.83 -92.77
REMARK 500 GLU A 482 -44.04 -18.30
REMARK 500 ALA A 484 -166.12 -110.14
REMARK 500 THR A 485 120.54 -38.63
REMARK 500 ASP A 520 -147.05 -87.19
REMARK 500 LYS A 537 75.32 41.44
REMARK 500 ALA A 555 34.58 -154.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K4Y A 23 556 GB 3219695 AAC39258 23 556
SEQRES 1 A 534 PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL LEU GLY
SEQRES 2 A 534 LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO VAL ALA
SEQRES 3 A 534 VAL PHE LEU GLY VAL PRO PHE ALA LYS PRO PRO LEU GLY
SEQRES 4 A 534 SER LEU ARG PHE ALA PRO PRO GLN PRO ALA GLU SER TRP
SEQRES 5 A 534 SER HIS VAL LYS ASN THR THR SER TYR PRO PRO MET CYS
SEQRES 6 A 534 SER GLN ASP ALA VAL SER GLY HIS MET LEU SER GLU LEU
SEQRES 7 A 534 PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS PHE SER
SEQRES 8 A 534 GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO ALA ASP
SEQRES 9 A 534 LEU THR LYS ARG GLY ARG LEU PRO VAL MET VAL TRP ILE
SEQRES 10 A 534 HIS GLY GLY GLY LEU MET VAL GLY GLY ALA SER THR TYR
SEQRES 11 A 534 ASP GLY LEU ALA LEU SER ALA HIS GLU ASN VAL VAL VAL
SEQRES 12 A 534 VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY PHE PHE
SEQRES 13 A 534 SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP GLY HIS
SEQRES 14 A 534 LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN ASP ASN
SEQRES 15 A 534 ILE ALA ASN PHE GLY GLY ASP PRO GLY SER VAL THR ILE
SEQRES 16 A 534 PHE GLY GLU SER ALA GLY GLY GLN SER VAL SER ILE LEU
SEQRES 17 A 534 LEU LEU SER PRO LEU THR LYS ASN LEU PHE HIS ARG ALA
SEQRES 18 A 534 ILE SER GLU SER GLY VAL ALA LEU LEU SER SER LEU PHE
SEQRES 19 A 534 ARG LYS ASN THR LYS SER LEU ALA GLU LYS ILE ALA ILE
SEQRES 20 A 534 GLU ALA GLY CYS LYS THR THR THR SER ALA VAL MET VAL
SEQRES 21 A 534 HIS CYS LEU ARG GLN LYS THR GLU GLU GLU LEU MET GLU
SEQRES 22 A 534 VAL THR LEU LYS MET LYS PHE MET ALA LEU ASP LEU VAL
SEQRES 23 A 534 GLY ASP PRO LYS GLU ASN THR ALA PHE LEU THR THR VAL
SEQRES 24 A 534 ILE ASP GLY VAL LEU LEU PRO LYS ALA PRO ALA GLU ILE
SEQRES 25 A 534 LEU ALA GLU LYS LYS TYR ASN MET LEU PRO TYR MET VAL
SEQRES 26 A 534 GLY ILE ASN GLN GLN GLU PHE GLY TRP ILE ILE PRO MET
SEQRES 27 A 534 GLN MET LEU GLY TYR PRO LEU SER GLU GLY LYS LEU ASP
SEQRES 28 A 534 GLN LYS THR ALA THR GLU LEU LEU TRP LYS SER TYR PRO
SEQRES 29 A 534 ILE VAL ASN VAL SER LYS GLU LEU THR PRO VAL ALA THR
SEQRES 30 A 534 GLU LYS TYR LEU GLY GLY THR ASP ASP PRO VAL LYS LYS
SEQRES 31 A 534 LYS ASP LEU PHE LEU ASP MET LEU ALA ASP LEU LEU PHE
SEQRES 32 A 534 GLY VAL PRO SER VAL ASN VAL ALA ARG HIS HIS ARG ASP
SEQRES 33 A 534 ALA GLY ALA PRO THR TYR MET TYR GLU TYR ARG TYR ARG
SEQRES 34 A 534 PRO SER PHE SER SER ASP MET ARG PRO LYS THR VAL ILE
SEQRES 35 A 534 GLY ASP HIS GLY ASP GLU ILE PHE SER VAL LEU GLY ALA
SEQRES 36 A 534 PRO PHE LEU LYS GLU GLY ALA THR GLU GLU GLU ILE LYS
SEQRES 37 A 534 LEU SER LYS MET VAL MET LYS TYR TRP ALA ASN PHE ALA
SEQRES 38 A 534 ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO GLN TRP
SEQRES 39 A 534 PRO ALA TYR ASP TYR LYS GLU GLY TYR LEU GLN ILE GLY
SEQRES 40 A 534 ALA THR THR GLN ALA ALA GLN LYS LEU LYS ASP LYS GLU
SEQRES 41 A 534 VAL ALA PHE TRP THR GLU LEU TRP ALA LYS GLU ALA ALA
SEQRES 42 A 534 ARG
MODRES 1K4Y ASN A 79 ASN GLYCOSYLATION SITE
MODRES 1K4Y ASN A 389 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET MAN C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET 4PN A2001 12
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM 4PN 4-PIPERIDINO-PIPERIDINE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 3 MAN 3(C6 H12 O6)
FORMUL 4 4PN C10 H20 N2
FORMUL 5 HOH *383(H2 O)
HELIX 1 1 LEU A 60 ARG A 64 5 5
HELIX 2 2 ASP A 90 THR A 102 1 13
HELIX 3 3 GLY A 154 ASN A 162 1 9
HELIX 4 4 LEU A 172 PHE A 178 1 7
HELIX 5 5 ASN A 188 ILE A 205 1 18
HELIX 6 6 ALA A 206 PHE A 208 5 3
HELIX 7 7 SER A 221 SER A 233 1 13
HELIX 8 8 PRO A 234 LYS A 237 5 4
HELIX 9 9 THR A 260 GLY A 272 1 13
HELIX 10 10 THR A 277 LYS A 288 1 12
HELIX 11 11 THR A 289 LYS A 301 1 13
HELIX 12 12 ALA A 330 LYS A 338 1 9
HELIX 13 13 LYS A 375 SER A 384 1 10
HELIX 14 14 SER A 384 ASN A 389 1 6
HELIX 15 15 LEU A 394 LEU A 403 1 10
HELIX 16 16 LEU A 415 PHE A 425 1 11
HELIX 17 17 PHE A 425 ASP A 438 1 14
HELIX 18 18 GLY A 468 LEU A 475 1 8
HELIX 19 19 THR A 485 GLY A 506 1 22
HELIX 20 20 LYS A 539 GLU A 553 1 15
SHEET 1 A 3 VAL A 25 VAL A 26 0
SHEET 2 A 3 VAL A 33 LEU A 34 -1 O VAL A 33 N VAL A 26
SHEET 3 A 3 LYS A 78 ASN A 79 1 O LYS A 78 N LEU A 34
SHEET 1 B11 LYS A 36 VAL A 38 0
SHEET 2 B11 VAL A 47 PRO A 54 -1 O VAL A 49 N LYS A 36
SHEET 3 B11 TYR A 118 THR A 123 -1 O ILE A 121 N PHE A 50
SHEET 4 B11 VAL A 164 ILE A 168 -1 O VAL A 165 N TYR A 122
SHEET 5 B11 LEU A 133 ILE A 139 1 N MET A 136 O VAL A 166
SHEET 6 B11 GLY A 210 GLU A 220 1 O SER A 214 N VAL A 135
SHEET 7 B11 ARG A 242 GLU A 246 1 O ARG A 242 N ILE A 217
SHEET 8 B11 TYR A 345 ASN A 350 1 O MET A 346 N ALA A 243
SHEET 9 B11 THR A 443 TYR A 448 1 O TYR A 444 N VAL A 347
SHEET 10 B11 TYR A 525 ILE A 528 1 O LEU A 526 N GLU A 447
SHEET 11 B11 GLN A 533 ALA A 535 -1 O GLN A 533 N GLN A 527
SHEET 1 C 2 MET A 86 CYS A 87 0
SHEET 2 C 2 PHE A 112 SER A 113 1 O SER A 113 N MET A 86
SSBOND 1 CYS A 87 CYS A 116 1555 1555 2.02
SSBOND 2 CYS A 273 CYS A 284 1555 1555 2.05
LINK ND2 ASN A 79 C1 NAG B 1 1555 1555 1.46
LINK ND2 ASN A 389 C1 NAG C 1 1555 1555 1.46
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.40
LINK O4 NAG C 2 C1 MAN C 3 1555 1555 1.40
LINK O3 MAN C 3 C1 MAN C 4 1555 1555 1.42
LINK O3 MAN C 4 C1 MAN C 5 1555 1555 1.40
CRYST1 110.230 110.230 282.520 90.00 90.00 120.00 H 3 2 18
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 0.009072 0.005238 0.000000 0.00000
SCALE2 0.000000 0.010475 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
