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HEADER HYDROLASE 29-JUL-15 5CXU
TITLE STRUCTURE OF THE CE1 FERULIC ACID ESTERASE AMCE1/FAE1A, FROM THE
TITLE 2 ANAEROBIC FUNGI ANAEROMYCES MUCRONATUS IN THE ABSENCE OF SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE AMCE1/FAE1A;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANAEROMYCES MUCRONATUS;
SOURCE 3 ORGANISM_TAXID: 994854;
SOURCE 4 GENE: FAE1A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS FERULIC ACID, ESTERASE, INDUCED FIT, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.GRUNINGER,D.W.ABBOTT
REVDAT 1 27-APR-16 5CXU 0
JRNL AUTH R.J.GRUNINGER,C.COTE,T.A.MCALLISTER,D.W.ABBOTT
JRNL TITL CONTRIBUTIONS OF A UNIQUE BETA-CLAMP TO SUBSTRATE
JRNL TITL 2 RECOGNITION ILLUMINATES THE MOLECULAR BASIS OF EXOLYSIS IN
JRNL TITL 3 FERULIC ACID ESTERASES.
JRNL REF BIOCHEM.J. V. 473 839 2016
JRNL REFN ESSN 1470-8728
JRNL PMID 27026397
JRNL DOI 10.1042/BJ20151153
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 35462
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1774
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 46.6729 - 3.7616 0.98 2645 140 0.1300 0.1465
REMARK 3 2 3.7616 - 2.9858 0.99 2598 136 0.1280 0.1601
REMARK 3 3 2.9858 - 2.6084 0.99 2589 137 0.1433 0.1694
REMARK 3 4 2.6084 - 2.3699 1.00 2604 137 0.1417 0.1605
REMARK 3 5 2.3699 - 2.2001 1.00 2579 135 0.1378 0.1555
REMARK 3 6 2.2001 - 2.0704 1.00 2594 137 0.1337 0.1950
REMARK 3 7 2.0704 - 1.9667 1.00 2590 136 0.1344 0.1602
REMARK 3 8 1.9667 - 1.8811 1.00 2591 137 0.1392 0.1576
REMARK 3 9 1.8811 - 1.8087 1.00 2572 135 0.1504 0.1713
REMARK 3 10 1.8087 - 1.7462 1.00 2598 137 0.1549 0.1867
REMARK 3 11 1.7462 - 1.6916 1.00 2579 136 0.1776 0.1970
REMARK 3 12 1.6916 - 1.6433 1.00 2570 135 0.1934 0.2222
REMARK 3 13 1.6433 - 1.6000 1.00 2579 136 0.2170 0.2343
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.014 2232
REMARK 3 ANGLE : 1.406 3037
REMARK 3 CHIRALITY : 0.079 327
REMARK 3 PLANARITY : 0.008 396
REMARK 3 DIHEDRAL : 13.487 831
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8712 20.0274 -64.6160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2905 T22: 0.2261
REMARK 3 T33: 0.1723 T12: -0.0039
REMARK 3 T13: 0.0115 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 2.8977 L22: 2.3545
REMARK 3 L33: 1.8080 L12: 1.1495
REMARK 3 L13: -0.1543 L23: -0.2981
REMARK 3 S TENSOR
REMARK 3 S11: -0.1653 S12: 0.5438 S13: -0.1924
REMARK 3 S21: -0.5167 S22: 0.2069 S23: -0.0426
REMARK 3 S31: 0.1340 S32: -0.1796 S33: -0.0889
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2402 26.2208 -60.1433
REMARK 3 T TENSOR
REMARK 3 T11: 0.2080 T22: 0.1748
REMARK 3 T33: 0.1704 T12: -0.0093
REMARK 3 T13: 0.0574 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 1.8303 L22: 1.9245
REMARK 3 L33: 1.2003 L12: 0.4682
REMARK 3 L13: -0.2068 L23: -0.3323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0876 S12: 0.2612 S13: 0.0447
REMARK 3 S21: -0.2344 S22: 0.0510 S23: -0.1243
REMARK 3 S31: -0.0326 S32: 0.0880 S33: 0.0456
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1044 29.6687 -46.8024
REMARK 3 T TENSOR
REMARK 3 T11: 0.2158 T22: 0.1780
REMARK 3 T33: 0.1979 T12: -0.0491
REMARK 3 T13: -0.0006 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 4.4130 L22: 3.2389
REMARK 3 L33: 7.5434 L12: -2.4236
REMARK 3 L13: 1.0172 L23: -3.9592
REMARK 3 S TENSOR
REMARK 3 S11: -0.0567 S12: -0.2518 S13: 0.2402
REMARK 3 S21: 0.4650 S22: -0.2066 S23: -0.4177
REMARK 3 S31: -0.2173 S32: 0.2827 S33: 0.2484
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 132 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1551 38.8370 -63.1798
REMARK 3 T TENSOR
REMARK 3 T11: 0.2947 T22: 0.2519
REMARK 3 T33: 0.3105 T12: -0.0319
REMARK 3 T13: 0.0344 T23: 0.0988
REMARK 3 L TENSOR
REMARK 3 L11: 2.7962 L22: 0.2148
REMARK 3 L33: 0.7540 L12: -0.1058
REMARK 3 L13: 0.4921 L23: -0.3552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0937 S12: 0.2053 S13: 0.3675
REMARK 3 S21: -0.1750 S22: 0.1057 S23: 0.0541
REMARK 3 S31: -0.2902 S32: 0.0142 S33: 0.0194
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 147 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6818 30.1574 -48.7953
REMARK 3 T TENSOR
REMARK 3 T11: 0.1809 T22: 0.1685
REMARK 3 T33: 0.1835 T12: 0.0032
REMARK 3 T13: 0.0302 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 2.0205 L22: 2.3439
REMARK 3 L33: 2.2316 L12: 0.0904
REMARK 3 L13: -0.2798 L23: -0.1866
REMARK 3 S TENSOR
REMARK 3 S11: 0.0263 S12: -0.0643 S13: 0.1815
REMARK 3 S21: -0.0328 S22: 0.0039 S23: 0.0233
REMARK 3 S31: -0.2123 S32: -0.0583 S33: -0.0377
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 185 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0335 30.1045 -36.6179
REMARK 3 T TENSOR
REMARK 3 T11: 0.2524 T22: 0.3256
REMARK 3 T33: 0.2924 T12: 0.0173
REMARK 3 T13: 0.0122 T23: -0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 3.7282 L22: 4.8122
REMARK 3 L33: 5.2845 L12: -1.2785
REMARK 3 L13: 0.4724 L23: 0.9092
REMARK 3 S TENSOR
REMARK 3 S11: -0.0848 S12: -0.5743 S13: 0.3266
REMARK 3 S21: 0.5585 S22: 0.2101 S23: -0.5625
REMARK 3 S31: 0.1600 S32: 0.3780 S33: -0.1027
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 238 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5490 19.8350 -41.1921
REMARK 3 T TENSOR
REMARK 3 T11: 0.1650 T22: 0.2041
REMARK 3 T33: 0.1778 T12: 0.0017
REMARK 3 T13: 0.0447 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 2.5870 L22: 4.4759
REMARK 3 L33: 1.0604 L12: -2.2399
REMARK 3 L13: 0.2984 L23: 0.3496
REMARK 3 S TENSOR
REMARK 3 S11: -0.1045 S12: -0.3081 S13: -0.1132
REMARK 3 S21: 0.2132 S22: 0.1186 S23: 0.1864
REMARK 3 S31: 0.1039 S32: -0.0486 S33: -0.0106
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 239 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8477 21.7988 -51.7173
REMARK 3 T TENSOR
REMARK 3 T11: 0.1595 T22: 0.1678
REMARK 3 T33: 0.1835 T12: -0.0120
REMARK 3 T13: 0.0119 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 2.1436 L22: 1.5466
REMARK 3 L33: 2.0752 L12: -0.1427
REMARK 3 L13: -0.3514 L23: 0.1270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: 0.0098 S13: 0.0668
REMARK 3 S21: -0.1064 S22: 0.0838 S23: 0.1001
REMARK 3 S31: -0.0871 S32: -0.1607 S33: -0.0782
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CXU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212347.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35462
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 46.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.04070
REMARK 200 R SYM (I) : 0.04550
REMARK 200 FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50890
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1JT2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM AMMONIUM ACETATE, 100 MM SODIUM
REMARK 280 ACETATE (PH 4.6), 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,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 -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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 50.93500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.93500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 26.24000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.93500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.93500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.24000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 50.93500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 50.93500
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 26.24000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 50.93500
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 50.93500
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 26.24000
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 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 190
REMARK 465 SER A 191
REMARK 465 PHE A 192
REMARK 465 SER A 193
REMARK 465 ASN A 275
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 O HOH A 582 O HOH A 583 1.98
REMARK 500 O HOH A 411 O HOH A 598 2.00
REMARK 500 O HOH A 540 O HOH A 610 2.06
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 TYR A 50 121.76 -39.83
REMARK 500 MET A 66 -101.71 -142.45
REMARK 500 MET A 66 -102.15 -142.53
REMARK 500 SER A 67 45.50 -147.58
REMARK 500 TYR A 68 -142.26 58.70
REMARK 500 VAL A 132 -53.65 -122.56
REMARK 500 SER A 156 -120.69 57.63
REMARK 500 ASP A 252 -154.48 -99.06
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 residue GOL A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CXX RELATED DB: PDB
DBREF 5CXU A 1 275 UNP F2YCB6 F2YCB6_9FUNG 1 275
SEQRES 1 A 275 MET SER LYS LEU GLN ILE SER ASN THR CYS PRO ASP LYS
SEQRES 2 A 275 TYR ARG THR LYS GLN GLU GLY VAL GLU TYR PRO THR ALA
SEQRES 3 A 275 LYS LYS ILE THR TYR TYR SER LYS VAL THR GLU THR GLU
SEQRES 4 A 275 ARG LYS MET ASN VAL ILE LEU PRO VAL GLY TYR ASP GLU
SEQRES 5 A 275 ASN LYS LYS TYR PRO VAL VAL TYR TYR LEU HIS GLY LEU
SEQRES 6 A 275 MET SER TYR GLU ASP SER MET LEU GLU ASP ASP SER THR
SEQRES 7 A 275 LEU ALA ILE PRO THR ASN LEU LEU LYS GLU GLY ARG ALA
SEQRES 8 A 275 LYS GLU MET ILE ILE VAL LEU PRO ASP VAL TYR ALA PRO
SEQRES 9 A 275 LYS PRO GLY THR ALA VAL THR PRO ASP PHE ASN PRO GLU
SEQRES 10 A 275 TYR TYR LYS GLY TYR ASP ASN PHE ILE ASN GLU LEU ILE
SEQRES 11 A 275 GLU VAL ILE MET PRO TYR MET GLU GLU HIS TYR SER ILE
SEQRES 12 A 275 LEU THR GLY ARG GLU ASN THR ALA LEU CYS GLY PHE SER
SEQRES 13 A 275 MET GLY ALA ARG THR SER LEU TYR ILE GLY TYR MET ARG
SEQRES 14 A 275 SER ASP LEU ILE GLY TYR VAL GLY ALA PHE ALA PRO ALA
SEQRES 15 A 275 PRO GLY ILE THR PRO GLY GLU ASP SER PHE SER GLY LYS
SEQRES 16 A 275 HIS GLU GLY LEU ILE SER GLU ASP GLU PHE ARG ALA GLU
SEQRES 17 A 275 ILE GLN PRO ILE VAL SER LEU ILE ASP CYS GLY THR ASN
SEQRES 18 A 275 ASP SER VAL VAL GLY GLN PHE PRO LYS SER TYR HIS GLU
SEQRES 19 A 275 ILE LEU THR ARG ASN ASN GLN GLU HIS ILE TRP PHE GLU
SEQRES 20 A 275 VAL PRO GLY ALA ASP HIS ASP TRP ASN ALA ILE SER ALA
SEQRES 21 A 275 GLY PHE TYR ASN PHE ILE GLN THR THR PHE GLY ALA LEU
SEQRES 22 A 275 ASN ASN
HET GOL A 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *215(H2 O)
HELIX 1 AA1 PRO A 11 THR A 16 1 6
HELIX 2 AA2 SER A 67 GLU A 74 5 8
HELIX 3 AA3 ASP A 76 LYS A 87 1 12
HELIX 4 AA4 ASN A 115 ASN A 124 1 10
HELIX 5 AA5 ASN A 124 VAL A 132 1 9
HELIX 6 AA6 VAL A 132 TYR A 141 1 10
HELIX 7 AA7 GLY A 146 GLU A 148 5 3
HELIX 8 AA8 SER A 156 ARG A 169 1 14
HELIX 9 AA9 SER A 201 PHE A 205 5 5
HELIX 10 AB1 GLN A 227 ASN A 239 1 13
HELIX 11 AB2 ASP A 254 THR A 269 1 16
HELIX 12 AB3 PHE A 270 ALA A 272 5 3
SHEET 1 AA1 8 ALA A 26 SER A 33 0
SHEET 2 AA1 8 THR A 38 ILE A 45 -1 O MET A 42 N ILE A 29
SHEET 3 AA1 8 ILE A 95 PRO A 99 -1 O ILE A 96 N ILE A 45
SHEET 4 AA1 8 VAL A 58 LEU A 62 1 N VAL A 59 O VAL A 97
SHEET 5 AA1 8 THR A 150 PHE A 155 1 O CYS A 153 N LEU A 62
SHEET 6 AA1 8 TYR A 175 PHE A 179 1 O TYR A 175 N LEU A 152
SHEET 7 AA1 8 VAL A 213 GLY A 219 1 O LEU A 215 N ALA A 178
SHEET 8 AA1 8 ILE A 244 VAL A 248 1 O ILE A 244 N SER A 214
SITE 1 AC1 6 ILE A 212 VAL A 213 SER A 214 GLU A 242
SITE 2 AC1 6 HIS A 243 HOH A 451
CRYST1 101.870 101.870 52.480 90.00 90.00 90.00 I 4 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 0.009816 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009816 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019055 0.00000
TER 2158 ASN A 274
MASTER 397 0 1 12 8 0 2 6 2354 1 6 22
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