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HEADER HYDROLASE 13-OCT-19 6UNV
TITLE CRYSTAL STRUCTURE OF A METHANOL TOLERANT LIPASE/ESTERASE FROM THE
TITLE 2 FUNGUS RASAMSONIA EMERSONII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RASAMSONIA EMERSONII;
SOURCE 3 ORGANISM_TAXID: 68825;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, ESTERASE, MACAW OIL HYDROLYSIS, METHANOL TOLERANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.S.VIEIRA,N.MILAN,M.T.MURAKAMI,L.M.ZANPHORLIN
REVDAT 1 03-JUN-20 6UNV 0
JRNL AUTH L.L.RADE,M.N.P.DA SILVA,P.S.VIEIRA,N.MILAN,C.M.DE SOUZA,
JRNL AUTH 2 R.R.DE MELO,B.C.KLEIN,A.BONOMI,H.F.DE CASTRO,M.T.MURAKAMI,
JRNL AUTH 3 L.M.ZANPHORLIN
JRNL TITL A NOVEL FUNGAL LIPASE WITH METHANOL TOLERANCE AND PREFERENCE
JRNL TITL 2 FOR MACAW PALM OIL.
JRNL REF FRONT BIOENG BIOTECHNOL V. 8 304 2020
JRNL REFN ISSN 2296-4185
JRNL PMID 32435636
JRNL DOI 10.3389/FBIOE.2020.00304
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_3139
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 5129
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.284
REMARK 3 R VALUE (WORKING SET) : 0.279
REMARK 3 FREE R VALUE : 0.329
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 513
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 4.7586 - 3.7784 1.00 1140 127 0.2702 0.3036
REMARK 3 2 3.7784 - 3.3012 1.00 1138 127 0.0000 0.4007
REMARK 3 3 3.3012 - 3.0000 1.00 1117 124 0.0000 0.3914
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3175 -24.3714 -3.9701
REMARK 3 T TENSOR
REMARK 3 T11: 0.5184 T22: 0.4543
REMARK 3 T33: 0.8556 T12: 0.0382
REMARK 3 T13: 0.0169 T23: 0.1823
REMARK 3 L TENSOR
REMARK 3 L11: 2.2048 L22: 7.6276
REMARK 3 L33: 6.4821 L12: -1.2029
REMARK 3 L13: -0.4628 L23: -3.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.2789 S12: -0.1599 S13: 0.0868
REMARK 3 S21: 1.0428 S22: 0.4796 S23: 0.7781
REMARK 3 S31: -0.8081 S32: -0.8989 S33: -0.1969
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9884 -17.1062 -6.9661
REMARK 3 T TENSOR
REMARK 3 T11: 0.6779 T22: 0.4098
REMARK 3 T33: 0.7471 T12: -0.0745
REMARK 3 T13: -0.0635 T23: 0.1516
REMARK 3 L TENSOR
REMARK 3 L11: 2.8252 L22: 4.4238
REMARK 3 L33: 3.6182 L12: -2.3802
REMARK 3 L13: -0.4440 L23: -1.5298
REMARK 3 S TENSOR
REMARK 3 S11: -0.4313 S12: 0.4552 S13: 0.9882
REMARK 3 S21: -0.2085 S22: 0.6725 S23: 0.9610
REMARK 3 S31: -0.6193 S32: -0.3240 S33: -0.3840
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 165 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5002 -23.6311 -11.1804
REMARK 3 T TENSOR
REMARK 3 T11: 0.4333 T22: 0.7088
REMARK 3 T33: 1.5369 T12: -0.0722
REMARK 3 T13: 0.1463 T23: 0.2909
REMARK 3 L TENSOR
REMARK 3 L11: 2.4628 L22: 2.0428
REMARK 3 L33: 4.0983 L12: 1.3127
REMARK 3 L13: -0.9129 L23: -0.5612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0478 S12: -0.0083 S13: 0.1446
REMARK 3 S21: -0.2452 S22: -0.0425 S23: -0.6960
REMARK 3 S31: -0.2276 S32: 0.7901 S33: 2.2553
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 166 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8569 -28.3195 -12.3320
REMARK 3 T TENSOR
REMARK 3 T11: 0.4181 T22: 0.4790
REMARK 3 T33: 1.0524 T12: 0.0683
REMARK 3 T13: 0.1707 T23: 0.2917
REMARK 3 L TENSOR
REMARK 3 L11: 1.0335 L22: 3.1710
REMARK 3 L33: 2.1007 L12: 1.3126
REMARK 3 L13: -0.0401 L23: -1.8296
REMARK 3 S TENSOR
REMARK 3 S11: 0.2250 S12: 0.2806 S13: -0.2352
REMARK 3 S21: -1.1476 S22: -0.8094 S23: -1.1697
REMARK 3 S31: 0.3807 S32: 0.3963 S33: 0.1697
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 197 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5669 -17.2276 -21.3260
REMARK 3 T TENSOR
REMARK 3 T11: 0.9664 T22: 0.6689
REMARK 3 T33: 1.0462 T12: 0.3388
REMARK 3 T13: 0.3055 T23: 0.1612
REMARK 3 L TENSOR
REMARK 3 L11: 1.7377 L22: 0.2690
REMARK 3 L33: 2.3752 L12: 0.6223
REMARK 3 L13: 0.1242 L23: -0.2815
REMARK 3 S TENSOR
REMARK 3 S11: 0.4569 S12: 0.7151 S13: 0.3695
REMARK 3 S21: -2.1441 S22: -1.0226 S23: -1.0289
REMARK 3 S31: 0.5331 S32: 0.2908 S33: 0.4179
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 250 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4419 -12.8920 -18.3645
REMARK 3 T TENSOR
REMARK 3 T11: 0.7420 T22: 0.4137
REMARK 3 T33: 0.9934 T12: 0.1626
REMARK 3 T13: -0.0102 T23: 0.2510
REMARK 3 L TENSOR
REMARK 3 L11: 2.3156 L22: 5.7745
REMARK 3 L33: 2.9687 L12: -0.8488
REMARK 3 L13: 0.1061 L23: -1.3547
REMARK 3 S TENSOR
REMARK 3 S11: 0.6694 S12: 0.5759 S13: 0.4561
REMARK 3 S21: -0.9279 S22: 0.0321 S23: 1.2973
REMARK 3 S31: 0.3700 S32: -0.2812 S33: -0.1528
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 6UNV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1000243968.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL, NON FIXED EXIT SLIT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8208
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 35.587
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 19.69
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 5CH8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MMOL/L MGCL2, 20% PEG 8000, 20%
REMARK 280 PEG 400, 100 MMOL/L TRIS BUFFER PH 8.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -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 45.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 45.50000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.50000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 87.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 45.50000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 45.50000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 58.00000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 45.50000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 87.00000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 29.00000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 45.50000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 29.00000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 87.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 45.50000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 45.50000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 58.00000
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 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 ALA A 24
REMARK 465 PRO A 25
REMARK 465 VAL A 26
REMARK 465 GLU A 27
REMARK 465 LEU A 28
REMARK 465 GLY A 29
REMARK 465 ARG A 30
REMARK 465 SER A 91
REMARK 465 GLU A 125
REMARK 465 SER A 136
REMARK 465 GLY A 137
REMARK 465 ASP A 142
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 CYS A 72 58.25 -149.74
REMARK 500 ASN A 88 82.03 60.31
REMARK 500 GLN A 105 71.87 59.21
REMARK 500 ALA A 131 59.06 -114.26
REMARK 500 SER A 177 -126.85 58.22
REMARK 500 SER A 230 -138.80 51.46
REMARK 500 THR A 275 34.11 -82.01
REMARK 500 PRO A 296 92.53 -67.28
REMARK 500 ALA A 299 24.03 -154.85
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 6UNV A 24 301 UNP A0A0F4YFS6_TALEM
DBREF2 6UNV A A0A0F4YFS6 22 299
SEQADV 6UNV MET A 1 UNP A0A0F4YFS INITIATING METHIONINE
SEQADV 6UNV GLY A 2 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV SER A 3 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV SER A 4 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 5 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 6 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 7 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 8 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 9 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 10 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV SER A 11 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV SER A 12 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV GLY A 13 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV LEU A 14 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV VAL A 15 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV PRO A 16 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV ARG A 17 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV GLY A 18 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV SER A 19 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV HIS A 20 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV MET A 21 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV ALA A 22 UNP A0A0F4YFS EXPRESSION TAG
SEQADV 6UNV SER A 23 UNP A0A0F4YFS EXPRESSION TAG
SEQRES 1 A 301 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 301 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA PRO VAL
SEQRES 3 A 301 GLU LEU GLY ARG ARG ASP VAL SER GLN ASP LEU PHE ASP
SEQRES 4 A 301 GLN LEU ASN LEU PHE GLU GLN TYR SER ALA ALA ALA TYR
SEQRES 5 A 301 CYS SER ALA ASN ASN GLU ALA SER ALA GLY THR ALA ILE
SEQRES 6 A 301 SER CYS SER ALA GLY ASN CYS PRO LEU VAL GLN GLN ALA
SEQRES 7 A 301 GLY ALA THR ILE LEU TYR SER PHE ASN ASN ILE GLY SER
SEQRES 8 A 301 GLY ASP VAL THR GLY PHE LEU ALA LEU ASP SER THR ASN
SEQRES 9 A 301 GLN LEU ILE VAL LEU SER PHE ARG GLY SER GLU THR LEU
SEQRES 10 A 301 GLU ASN TRP ILE ALA ASP LEU GLU ALA ASP LEU VAL ASP
SEQRES 11 A 301 ALA SER ALA ILE CYS SER GLY CYS GLU ALA HIS ASP GLY
SEQRES 12 A 301 PHE LEU SER SER TRP ASN SER VAL ALA SER THR LEU THR
SEQRES 13 A 301 SER LYS ILE SER SER ALA VAL ASN GLU HIS PRO SER TYR
SEQRES 14 A 301 LYS LEU VAL PHE THR GLY HIS SER LEU GLY ALA ALA LEU
SEQRES 15 A 301 ALA THR LEU GLY ALA VAL SER LEU ARG GLU SER GLY TYR
SEQRES 16 A 301 ASN ILE ASP LEU TYR ASN TYR GLY CYS PRO ARG VAL GLY
SEQRES 17 A 301 ASN THR ALA LEU ALA ASP PHE ILE THR THR GLN SER GLY
SEQRES 18 A 301 GLY THR ASN TYR ARG VAL THR HIS SER ASP ASP PRO VAL
SEQRES 19 A 301 PRO LYS LEU PRO PRO ARG SER PHE GLY TYR SER GLN PRO
SEQRES 20 A 301 SER PRO GLU TYR TRP ILE THR SER GLY ASN ASN VAL THR
SEQRES 21 A 301 VAL GLN PRO SER ASP ILE GLU VAL ILE GLU GLY VAL ASP
SEQRES 22 A 301 SER THR ALA GLY ASN ASP GLY THR PRO ALA GLY LEU ASP
SEQRES 23 A 301 ILE ASP ALA HIS ARG TRP TYR PHE GLY PRO ILE SER ALA
SEQRES 24 A 301 CYS SER
HELIX 1 AA1 SER A 34 ALA A 51 1 18
HELIX 2 AA2 CYS A 67 ASN A 71 5 5
HELIX 3 AA3 CYS A 72 GLN A 77 1 6
HELIX 4 AA4 THR A 116 ILE A 121 1 6
HELIX 5 AA5 PHE A 144 HIS A 166 1 23
HELIX 6 AA6 SER A 177 SER A 189 1 13
HELIX 7 AA7 ASN A 209 THR A 218 1 10
HELIX 8 AA8 PRO A 239 GLY A 243 5 5
HELIX 9 AA9 GLN A 262 SER A 264 5 3
HELIX 10 AB1 ASP A 286 TRP A 292 1 7
SHEET 1 AA1 8 THR A 81 PHE A 86 0
SHEET 2 AA1 8 GLY A 96 ASP A 101 -1 O GLY A 96 N PHE A 86
SHEET 3 AA1 8 LEU A 106 PHE A 111 -1 O VAL A 108 N ALA A 99
SHEET 4 AA1 8 LYS A 170 HIS A 176 1 O VAL A 172 N ILE A 107
SHEET 5 AA1 8 ILE A 197 TYR A 202 1 O ASP A 198 N LEU A 171
SHEET 6 AA1 8 ASN A 224 HIS A 229 1 O TYR A 225 N LEU A 199
SHEET 7 AA1 8 GLU A 250 ILE A 253 1 O TYR A 251 N ARG A 226
SHEET 8 AA1 8 ILE A 266 ILE A 269 -1 O GLU A 267 N TRP A 252
SSBOND 1 CYS A 53 CYS A 300 1555 1555 2.03
SSBOND 2 CYS A 67 CYS A 72 1555 1555 2.03
SSBOND 3 CYS A 135 CYS A 138 1555 1555 2.03
CISPEP 1 LEU A 237 PRO A 238 0 -3.31
CISPEP 2 SER A 248 PRO A 249 0 2.45
CRYST1 91.000 91.000 116.000 90.00 90.00 90.00 I 41 2 2 16
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 0.010989 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008621 0.00000
TER 1981 SER A 301
MASTER 399 0 0 10 8 0 0 6 1980 1 6 24
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