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HEADER HYDROLASE 05-MAR-13 4BE4
TITLE CLOSED CONFORMATION OF O. PICEAE STEROL ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STEROL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 13-549;
COMPND 5 EC: 3.1.1.13;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: N-ACETYLGLUCOSAMINE GLYCOSYLATIONS IN POSITIONS 362
COMPND 8 AND 380
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPHIOSTOMA PICEAE;
SOURCE 3 ORGANISM_TAXID: 61273;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: KM71;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PPIC9
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,M.J.GONZALEZ,
AUTHOR 2 J.A.HERMOSO
REVDAT 1 19-MAR-14 4BE4 0
JRNL AUTH J.GUTIERREZ-FERNANDEZ,M.E.VAQUERO,A.PRIETO,J.BARRIUSO,
JRNL AUTH 2 M.J.GONZALEZ,J.A.HERMOSO
JRNL TITL CRYSTAL STRUCTURE OF OPE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.600
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.228
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.33
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.00
REMARK 3 NUMBER OF REFLECTIONS : 26656
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1669
REMARK 3 R VALUE (WORKING SET) : 0.1640
REMARK 3 FREE R VALUE : 0.2207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1344
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.2351 - 5.5990 0.93 2669 131 0.1894 0.2293
REMARK 3 2 5.5990 - 4.4453 0.97 2567 134 0.1289 0.1731
REMARK 3 3 4.4453 - 3.8837 0.98 2587 133 0.1182 0.1732
REMARK 3 4 3.8837 - 3.5287 0.98 2567 125 0.1348 0.1653
REMARK 3 5 3.5287 - 3.2759 0.97 2511 143 0.1524 0.2071
REMARK 3 6 3.2759 - 3.0828 0.98 2503 149 0.1758 0.2361
REMARK 3 7 3.0828 - 2.9284 0.98 2522 127 0.1956 0.2939
REMARK 3 8 2.9284 - 2.8010 0.97 2483 140 0.2036 0.2806
REMARK 3 9 2.8010 - 2.6931 0.97 2462 133 0.2267 0.3036
REMARK 3 10 2.6931 - 2.6002 0.96 2441 129 0.2574 0.3793
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.350
REMARK 3 B_SOL : 41.977
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.63
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.0205
REMARK 3 B22 (A**2) : 5.0205
REMARK 3 B33 (A**2) : -10.0411
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4372
REMARK 3 ANGLE : 1.078 5933
REMARK 3 CHIRALITY : 0.073 656
REMARK 3 PLANARITY : 0.004 754
REMARK 3 DIHEDRAL : 12.580 1577
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 11:61)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8263 40.0393 -49.2222
REMARK 3 T TENSOR
REMARK 3 T11: 0.3312 T22: 0.3679
REMARK 3 T33: 0.2106 T12: -0.1496
REMARK 3 T13: 0.0234 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 1.9734 L22: 2.0339
REMARK 3 L33: 1.4837 L12: 0.8762
REMARK 3 L13: -0.4033 L23: 0.2499
REMARK 3 S TENSOR
REMARK 3 S11: -0.1922 S12: 0.6164 S13: -0.1805
REMARK 3 S21: -0.3741 S22: 0.2054 S23: 0.2020
REMARK 3 S31: 0.5010 S32: -0.9199 S33: 0.0312
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 62:98)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8611 56.5362 -32.2748
REMARK 3 T TENSOR
REMARK 3 T11: 0.2639 T22: 0.2531
REMARK 3 T33: 0.3477 T12: 0.0036
REMARK 3 T13: 0.0297 T23: -0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 2.1636 L22: 2.3698
REMARK 3 L33: 4.0617 L12: 1.9456
REMARK 3 L13: 2.5319 L23: 1.4788
REMARK 3 S TENSOR
REMARK 3 S11: -0.0864 S12: -0.0371 S13: 0.3703
REMARK 3 S21: 0.1497 S22: -0.1763 S23: 0.2100
REMARK 3 S31: -0.1314 S32: -0.5511 S33: 0.2642
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 99:187)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8351 43.5877 -39.1054
REMARK 3 T TENSOR
REMARK 3 T11: 0.2316 T22: 0.2219
REMARK 3 T33: 0.1299 T12: -0.0872
REMARK 3 T13: 0.0213 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 2.6168 L22: 0.9809
REMARK 3 L33: 1.8221 L12: 0.5109
REMARK 3 L13: -0.7624 L23: -0.2305
REMARK 3 S TENSOR
REMARK 3 S11: -0.1051 S12: 0.1325 S13: -0.1618
REMARK 3 S21: -0.1750 S22: -0.0235 S23: 0.0287
REMARK 3 S31: 0.3395 S32: -0.4833 S33: 0.0949
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 188:277)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2922 35.2603 -31.7964
REMARK 3 T TENSOR
REMARK 3 T11: 0.3585 T22: 0.2240
REMARK 3 T33: 0.1949 T12: -0.1150
REMARK 3 T13: 0.0551 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.4298 L22: 0.8772
REMARK 3 L33: 1.8111 L12: 0.3571
REMARK 3 L13: -0.2958 L23: -0.3383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.1717 S13: -0.1669
REMARK 3 S21: 0.0901 S22: -0.0750 S23: 0.1518
REMARK 3 S31: 0.5066 S32: -0.2880 S33: 0.0824
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 278:357)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1678 40.2221 -22.6761
REMARK 3 T TENSOR
REMARK 3 T11: 0.3468 T22: 0.4144
REMARK 3 T33: 0.2285 T12: -0.1538
REMARK 3 T13: 0.0966 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 1.3059 L22: 0.8763
REMARK 3 L33: 0.5971 L12: 0.2902
REMARK 3 L13: -0.1429 L23: 0.0655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0960 S12: -0.0473 S13: -0.0613
REMARK 3 S21: 0.0884 S22: -0.0210 S23: 0.1410
REMARK 3 S31: 0.4013 S32: -0.5509 S33: 0.0449
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 358:549)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6111 48.9759 -18.7030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2178 T22: 0.2087
REMARK 3 T33: 0.1483 T12: -0.0461
REMARK 3 T13: 0.0440 T23: 0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 0.7422 L22: 0.7714
REMARK 3 L33: 1.8715 L12: -0.2818
REMARK 3 L13: 0.0252 L23: 0.1964
REMARK 3 S TENSOR
REMARK 3 S11: -0.0561 S12: -0.2449 S13: -0.0759
REMARK 3 S21: 0.1271 S22: -0.0192 S23: 0.0390
REMARK 3 S31: 0.2271 S32: 0.0254 S33: 0.0655
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FIRST 8 AMINO ACIDS (EAEAYVEF)
REMARK 3 CORRESPOND TO A PURIFICATION TAG. ONLY THE LAST TWO AA (EF)
REMARK 3 WERE VISIBLE IN THE ELECTRON DENSITY MAP.
REMARK 4
REMARK 4 4BE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-13.
REMARK 100 THE PDBE ID CODE IS EBI-56045.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26901
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 46.23
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.9
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.15
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.4
REMARK 200 R MERGE FOR SHELL (I) : 0.82
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.90
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% 1,4-DIOXANE, 0.1 M MES PH
REMARK 280 6.5, 1.6 M AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 103.38700
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 103.38700
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 103.38700
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 103.38700
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 103.38700
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 103.38700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 GLU A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 TYR A 9
REMARK 465 VAL A 10
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 O4 SO4 A 1567 O HOH A 2209 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 ASN A 91 -47.73 -18.89
REMARK 500 SER A 220 -120.91 54.99
REMARK 500 SER A 252 79.56 64.38
REMARK 500 SER A 254 -107.06 -151.38
REMARK 500 SER A 312 -117.99 56.50
REMARK 500 VAL A 324 -57.44 -128.26
REMARK 500 ASP A 351 63.42 -115.64
REMARK 500 TYR A 377 -76.67 -104.21
REMARK 500 PHE A 427 -70.70 -125.66
REMARK 500 TYR A 454 0.67 -69.27
REMARK 500 PHE A 460 -29.02 65.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): COVALENTLY BOUND TO ASN362
REMARK 600 AND ASN380 BY N-GLYCOSIDIC LINKAGES
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1563
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1566
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1567
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1550 BOUND TO ASN A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1551 BOUND TO ASN A 380
DBREF 4BE4 A 13 549 UNP Q2TFW1 Q2TFW1_9PEZI 13 549
SEQADV 4BE4 GLU A 5 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 ALA A 6 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 GLU A 7 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 ALA A 8 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 TYR A 9 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 VAL A 10 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 GLU A 11 UNP Q2TFW1 EXPRESSION TAG
SEQADV 4BE4 PHE A 12 UNP Q2TFW1 EXPRESSION TAG
SEQRES 1 A 545 GLU ALA GLU ALA TYR VAL GLU PHE THR THR VAL ASN VAL
SEQRES 2 A 545 ASN TYR PRO GLU GLY GLU VAL VAL GLY VAL SER VAL LEU
SEQRES 3 A 545 GLY ILE GLU SER PHE ARG GLY VAL PRO PHE ALA GLN PRO
SEQRES 4 A 545 PRO VAL GLY ASN LEU ARG LEU LYS PRO PRO VAL ARG TYR
SEQRES 5 A 545 THR GLU ASN ILE GLY THR LYS ASP THR THR GLY ILE GLY
SEQRES 6 A 545 PRO SER CYS PRO GLN MET TYR LEU SER THR GLY ASN GLY
SEQRES 7 A 545 GLU LEU LEU PHE GLN LEU VAL GLY ASN LEU ILE ASN ILE
SEQRES 8 A 545 PRO LEU PHE GLN THR ALA THR LEU SER SER GLU ASP CYS
SEQRES 9 A 545 LEU THR LEU ASN ILE GLN ARG PRO ALA GLY THR THR SER
SEQRES 10 A 545 ASN SER SER LEU PRO VAL LEU PHE TRP ILE PHE GLY GLY
SEQRES 11 A 545 GLY PHE GLU LEU GLY THR ASN GLN TYR TYR ASP GLY ILE
SEQRES 12 A 545 ASP LEU LEU THR GLU GLY ILE SER LEU GLY GLU PRO PHE
SEQRES 13 A 545 ILE PHE VAL ALA ILE ASN TYR ARG VAL GLY GLY PHE GLY
SEQRES 14 A 545 PHE LEU GLY GLY LYS GLU ILE LYS ALA ASP GLY SER SER
SEQRES 15 A 545 ASN LEU GLY LEU LEU ASP GLN ARG ILE ALA LEU GLU TRP
SEQRES 16 A 545 VAL ALA ASP ASN ILE ALA SER PHE GLY GLY ASP PRO SER
SEQRES 17 A 545 LYS VAL THR ILE TRP GLY GLU SER ALA GLY SER ILE SER
SEQRES 18 A 545 VAL PHE ASP GLN MET ALA LEU TYR GLY GLY ASN ASN LYS
SEQRES 19 A 545 TYR LYS GLY LYS ALA LEU PHE ARG GLY GLY ILE MET ASN
SEQRES 20 A 545 SER GLY SER VAL VAL PRO ALA ALA PRO VAL ASP GLY VAL
SEQRES 21 A 545 LYS ALA GLN ALA ILE TYR ASP HIS VAL VAL SER GLU ALA
SEQRES 22 A 545 GLY CYS ALA GLY THR SER ASP THR LEU ALA CYS LEU ARG
SEQRES 23 A 545 THR VAL ASP TYR THR LYS PHE LEU THR ALA VAL ASN SER
SEQRES 24 A 545 VAL PRO GLY ILE VAL SER TYR SER SER ILE ALA LEU SER
SEQRES 25 A 545 TYR LEU PRO ARG PRO ASP GLY VAL VAL LEU ILE ASP SER
SEQRES 26 A 545 PRO GLU GLU ILE VAL LYS ASN LYS GLN TYR ALA ALA VAL
SEQRES 27 A 545 PRO MET ILE ILE GLY ASP GLN GLU ASP GLU GLY THR LEU
SEQRES 28 A 545 PHE ALA VAL LEU PRO ASN ASN ILE THR SER THR ALA LYS
SEQRES 29 A 545 ILE VAL GLN TYR PHE GLN ASP LEU TYR PHE TYR ASN ALA
SEQRES 30 A 545 THR LYS GLU GLN LEU THR ALA PHE VAL ASN THR TYR PRO
SEQRES 31 A 545 THR ASP ILE THR ALA GLY SER PRO PHE ASN THR GLY ILE
SEQRES 32 A 545 PHE ASN GLU LEU TYR PRO GLY PHE LYS ARG LEU ALA ALA
SEQRES 33 A 545 ILE LEU GLY ASP MET THR PHE THR LEU ALA ARG ARG ALA
SEQRES 34 A 545 PHE LEU GLN LEU CYS SER GLU VAL ASN PRO ASP VAL PRO
SEQRES 35 A 545 SER TRP SER TYR LEU ALA SER TYR ASP TYR GLY PHE PRO
SEQRES 36 A 545 PHE LEU GLY THR PHE HIS ALA THR ASP ILE LEU GLN VAL
SEQRES 37 A 545 PHE TYR GLY VAL LEU PRO ASN TYR ALA SER GLY SER ILE
SEQRES 38 A 545 GLN LYS TYR TYR ILE ASN PHE VAL THR THR GLY ASP PRO
SEQRES 39 A 545 ASN LYS GLY ALA ALA VAL ASP ILE GLN TRP PRO GLN TRP
SEQRES 40 A 545 SER ALA LYS LYS ASN ILE LEU GLN ILE TYR ALA THR LYS
SEQRES 41 A 545 ALA VAL ILE VAL ALA ASP ASN PHE ARG ALA LYS SER TYR
SEQRES 42 A 545 GLU TYR LEU TYR ASN ASN ILE GLY ILE PHE ARG ILE
HET NAG A1550 14
HET NAG A1551 14
HET DIO A1552 6
HET DIO A1553 6
HET DIO A1554 6
HET DIO A1555 6
HET DIO A1556 6
HET DIO A1557 6
HET MES A1558 12
HET GOL A1559 6
HET GOL A1560 6
HET GOL A1561 6
HET GOL A1562 6
HET GOL A1563 6
HET GOL A1564 6
HET SO4 A1565 5
HET SO4 A1566 5
HET SO4 A1567 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 DIO 6(C4 H8 O2)
FORMUL 4 MES C6 H13 N O4 S
FORMUL 5 GOL 6(C3 H8 O3)
FORMUL 6 SO4 3(O4 S 2-)
FORMUL 7 HOH *242(H2 O)
HELIX 1 1 VAL A 45 ARG A 49 5 5
HELIX 2 2 GLY A 82 VAL A 89 1 8
HELIX 3 3 GLY A 90 ILE A 95 5 6
HELIX 4 4 ILE A 95 GLN A 99 5 5
HELIX 5 5 THR A 140 TYR A 144 5 5
HELIX 6 6 GLY A 146 LEU A 156 1 11
HELIX 7 7 GLY A 170 LEU A 175 1 6
HELIX 8 8 GLY A 177 ASP A 183 1 7
HELIX 9 9 ASN A 187 ILE A 204 1 18
HELIX 10 10 ALA A 205 PHE A 207 5 3
HELIX 11 11 SER A 220 ASN A 236 1 17
HELIX 12 12 GLY A 263 GLY A 278 1 16
HELIX 13 13 ASP A 284 ARG A 290 1 7
HELIX 14 14 ASP A 293 SER A 303 1 11
HELIX 15 15 SER A 329 ASN A 336 1 8
HELIX 16 16 GLY A 353 VAL A 358 1 6
HELIX 17 17 SER A 365 TYR A 377 1 13
HELIX 18 18 THR A 382 ASN A 391 1 10
HELIX 19 19 GLY A 414 PHE A 427 1 14
HELIX 20 20 PHE A 427 ASN A 442 1 16
HELIX 21 21 ASP A 468 PHE A 473 1 6
HELIX 22 22 TYR A 480 GLY A 496 1 17
HELIX 23 23 GLN A 510 LYS A 515 1 6
HELIX 24 24 ARG A 533 ASN A 543 1 11
HELIX 25 25 ILE A 544 ARG A 548 5 5
SHEET 1 AA 2 PHE A 12 TYR A 19 0
SHEET 2 AA 2 GLY A 22 VAL A 29 -1 O GLY A 22 N TYR A 19
SHEET 1 AB 2 THR A 62 ASP A 64 0
SHEET 2 AB 2 GLY A 22 VAL A 29 1 O GLU A 23 N LYS A 63
SHEET 1 AC12 ALA A 525 ALA A 529 0
SHEET 2 AC12 ASN A 516 ILE A 520 -1 O ILE A 517 N VAL A 528
SHEET 3 AC12 SER A 447 ALA A 452 1 O SER A 449 N LEU A 518
SHEET 4 AC12 MET A 344 GLN A 349 1 O MET A 344 N TRP A 448
SHEET 5 AC12 GLY A 247 ASN A 251 1 O GLY A 248 N ILE A 345
SHEET 6 AC12 GLY A 209 GLU A 219 1 O ILE A 216 N ILE A 249
SHEET 7 AC12 LEU A 125 ILE A 131 1 O LEU A 125 N ASP A 210
SHEET 8 AC12 ILE A 161 ILE A 165 1 O ILE A 161 N LEU A 128
SHEET 9 AC12 THR A 110 PRO A 116 -1 O ASN A 112 N ALA A 164
SHEET 10 AC12 ILE A 32 PRO A 39 -1 O GLU A 33 N ARG A 115
SHEET 11 AC12 GLY A 22 VAL A 29 -1 O VAL A 27 N SER A 34
SHEET 12 AC12 THR A 62 ASP A 64 1 O LYS A 63 N VAL A 25
SHEET 1 AD12 ALA A 525 ALA A 529 0
SHEET 2 AD12 ASN A 516 ILE A 520 -1 O ILE A 517 N VAL A 528
SHEET 3 AD12 SER A 447 ALA A 452 1 O SER A 449 N LEU A 518
SHEET 4 AD12 MET A 344 GLN A 349 1 O MET A 344 N TRP A 448
SHEET 5 AD12 GLY A 247 ASN A 251 1 O GLY A 248 N ILE A 345
SHEET 6 AD12 GLY A 209 GLU A 219 1 O ILE A 216 N ILE A 249
SHEET 7 AD12 LEU A 125 ILE A 131 1 O LEU A 125 N ASP A 210
SHEET 8 AD12 ILE A 161 ILE A 165 1 O ILE A 161 N LEU A 128
SHEET 9 AD12 THR A 110 PRO A 116 -1 O ASN A 112 N ALA A 164
SHEET 10 AD12 ILE A 32 PRO A 39 -1 O GLU A 33 N ARG A 115
SHEET 11 AD12 GLY A 22 VAL A 29 -1 O VAL A 27 N SER A 34
SHEET 12 AD12 PHE A 12 TYR A 19 -1 O THR A 13 N SER A 28
SHEET 1 AE 2 LYS A 238 TYR A 239 0
SHEET 2 AE 2 LYS A 242 ALA A 243 -1 O LYS A 242 N TYR A 239
SSBOND 1 CYS A 72 CYS A 108 1555 1555 2.04
SSBOND 2 CYS A 279 CYS A 288 1555 1555 2.05
LINK ND2 ASN A 362 C1 NAG A1550 1555 1555 1.55
LINK ND2 ASN A 380 C1 NAG A1551 1555 1555 1.56
CISPEP 1 SER A 401 PRO A 402 0 6.23
SITE 1 AC1 4 GLY A 118 THR A 120 SER A 123 GLY A 501
SITE 1 AC2 3 GLU A 198 TYR A 233 HOH A2033
SITE 1 AC3 4 THR A 120 SER A 121 HOH A2004 HOH A2005
SITE 1 AC4 3 ALA A 117 LEU A 156 GLY A 501
SITE 1 AC5 4 PHE A 378 THR A 426 PHE A 547 ILE A 549
SITE 1 AC6 5 SER A 220 ILE A 224 ILE A 307 ILE A 313
SITE 2 AC6 5 LEU A 315
SITE 1 AC7 7 LEU A 92 TYR A 454 ASP A 455 GLN A 471
SITE 2 AC7 7 ASN A 479 ALA A 522 THR A 523
SITE 1 AC8 1 ASN A 94
SITE 1 AC9 3 ASN A 81 GLY A 306 SER A 309
SITE 1 BC1 2 ARG A 533 ALA A 534
SITE 1 BC2 2 TYR A 239 LYS A 240
SITE 1 BC3 4 TYR A 480 GLY A 483 LYS A 487 HOH A2216
SITE 1 BC4 3 VAL A 504 ASP A 505 HOH A2216
SITE 1 BC5 3 SER A 365 THR A 366 SO4 A1566
SITE 1 BC6 3 SER A 365 LYS A 368 SO4 A1565
SITE 1 BC7 5 TYR A 521 ALA A 522 THR A 523 LYS A 524
SITE 2 BC7 5 HOH A2209
SITE 1 BC8 3 TYR A 310 ASN A 362 HOH A2240
SITE 1 BC9 5 ALA A 259 ASN A 380 GLU A 384 ARG A 548
SITE 2 BC9 5 HOH A2241
CRYST1 119.274 119.274 206.774 90.00 90.00 120.00 P 63 2 2 12
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 0.008384 0.004841 0.000000 0.00000
SCALE2 0.000000 0.009681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004836 0.00000
TER 4141 ILE A 549
MASTER 452 0 18 25 30 0 22 6 4508 1 133 42
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