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HEADER HYDROLASE 04-OCT-18 6MOT
TITLE BACTEROIDES INTESTINALIS FERULOYL ESTERASE, BACINT_01033
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOAMYLASE N-TERMINAL DOMAIN PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FERULOYL ESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES INTESTINALIS DSM 17393;
SOURCE 3 ORGANISM_TAXID: 471870;
SOURCE 4 GENE: BACINT_01033;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOHYDRATE ESTERASE, FERULOYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.KOROPATKIN,G.V.PEREIRA,I.CANN
REVDAT 1 16-OCT-19 6MOT 0
JRNL AUTH G.V.PEREIRA,C.DALESSANDRO-GABAZZA,J.FARRIS,D.WEFERS,
JRNL AUTH 2 R.MACKIE,N.M.KOROPATKIN,E.C.GABAZZA,I.CANN
JRNL TITL COMPLEX ARABINOXYLAN FERMENTING BACTEROIDETES RELEASE
JRNL TITL 2 DIETARY ANTIOXIDANTS THAT IMPACT HOST IMMUNE FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.470
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 99242
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.760
REMARK 3 FREE R VALUE TEST SET COUNT : 3730
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 86.6781 - 5.1297 1.00 3550 146 0.1692 0.1839
REMARK 3 2 5.1297 - 4.0716 1.00 3549 136 0.1223 0.1438
REMARK 3 3 4.0716 - 3.5569 1.00 3522 141 0.1382 0.1387
REMARK 3 4 3.5569 - 3.2317 1.00 3538 135 0.1515 0.1555
REMARK 3 5 3.2317 - 3.0000 1.00 3556 131 0.1592 0.1848
REMARK 3 6 3.0000 - 2.8231 1.00 3544 141 0.1633 0.1806
REMARK 3 7 2.8231 - 2.6817 1.00 3527 139 0.1731 0.2153
REMARK 3 8 2.6817 - 2.5650 1.00 3513 138 0.1673 0.2095
REMARK 3 9 2.5650 - 2.4662 1.00 3573 135 0.1621 0.1707
REMARK 3 10 2.4662 - 2.3811 1.00 3523 139 0.1607 0.1976
REMARK 3 11 2.3811 - 2.3067 1.00 3530 140 0.1651 0.1754
REMARK 3 12 2.3067 - 2.2407 1.00 3552 136 0.1565 0.1833
REMARK 3 13 2.2407 - 2.1817 1.00 3534 139 0.1542 0.2152
REMARK 3 14 2.1817 - 2.1285 1.00 3506 138 0.1626 0.2065
REMARK 3 15 2.1285 - 2.0801 1.00 3560 138 0.1782 0.2208
REMARK 3 16 2.0801 - 2.0358 1.00 3502 134 0.1847 0.2401
REMARK 3 17 2.0358 - 1.9951 1.00 3570 140 0.1834 0.2018
REMARK 3 18 1.9951 - 1.9575 1.00 3510 135 0.2005 0.2285
REMARK 3 19 1.9575 - 1.9225 1.00 3534 138 0.2142 0.2418
REMARK 3 20 1.9225 - 1.8899 1.00 3545 138 0.2229 0.2251
REMARK 3 21 1.8899 - 1.8594 1.00 3574 138 0.2466 0.2707
REMARK 3 22 1.8594 - 1.8308 1.00 3513 135 0.2663 0.2611
REMARK 3 23 1.8308 - 1.8039 1.00 3555 143 0.2928 0.3461
REMARK 3 24 1.8039 - 1.7785 1.00 3488 136 0.3093 0.3366
REMARK 3 25 1.7785 - 1.7544 1.00 3557 140 0.3296 0.3721
REMARK 3 26 1.7544 - 1.7317 1.00 3531 138 0.3402 0.3335
REMARK 3 27 1.7317 - 1.7100 1.00 3556 143 0.3523 0.3122
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.15
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 : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9340 33.1527 69.9878
REMARK 3 T TENSOR
REMARK 3 T11: 0.1648 T22: 0.1832
REMARK 3 T33: 0.1425 T12: -0.0367
REMARK 3 T13: 0.0092 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.3409 L22: 1.0518
REMARK 3 L33: 1.0092 L12: -0.5862
REMARK 3 L13: -0.5434 L23: 0.3473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0557 S12: 0.0670 S13: -0.0456
REMARK 3 S21: -0.0461 S22: 0.0698 S23: -0.0498
REMARK 3 S31: 0.0189 S32: 0.0025 S33: -0.0162
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 6MOT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : C 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99242
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 86.567
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 40.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M LITHIUM SULFATE, 0.1 M SODIUM
REMARK 280 ACETATE (HAMPTON SALTRX B10), PH 4.6, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-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 54.73467
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 109.46933
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 0.00000
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 54.73467
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 109.46933
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 54.73467
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 109.46933
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 54.73467
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 0.00000
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 109.46933
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 164.20400
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 508 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 728 LIES ON A SPECIAL POSITION.
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 PHE A 223
REMARK 465 LYS A 224
REMARK 465 THR A 225
REMARK 465 ASN A 226
REMARK 465 SER A 227
REMARK 465 GLY A 228
REMARK 465 GLU A 229
REMARK 465 THR A 230
REMARK 465 PRO A 231
REMARK 465 GLU A 232
REMARK 465 ASP A 233
REMARK 465 ALA A 234
REMARK 465 ARG A 235
REMARK 465 LYS A 236
REMARK 465 ARG A 237
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 754 O HOH A 757 2.11
REMARK 500 O HOH A 740 O HOH A 753 2.15
REMARK 500 O HOH A 550 O HOH A 703 2.15
REMARK 500 O HOH A 637 O HOH A 739 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 797 O HOH A 797 11556 1.90
REMARK 500 O HOH A 774 O HOH A 774 11556 2.02
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 ASP A 129 13.14 -142.15
REMARK 500 ASN A 191 -86.45 -97.36
REMARK 500 GLU A 249 -50.20 -129.38
REMARK 500 SER A 273 -126.75 52.79
REMARK 500 ASN A 286 48.87 -141.69
REMARK 500 ALA A 299 146.15 83.69
REMARK 500 HIS A 337 70.36 60.21
REMARK 500 ALA A 364 -137.46 -124.92
REMARK 500 PHE A 382 34.92 70.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 806 DISTANCE = 6.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
DBREF 6MOT A 25 384 UNP B3C969 B3C969_9BACE 27 386
SEQRES 1 A 360 ASP PHE PRO ALA GLY THR THR PRO ASN GLU HIS ASN ILE
SEQRES 2 A 360 ASN GLY ALA ASP TYR PRO ARG ILE GLY GLU ASP ARG ARG
SEQRES 3 A 360 VAL HIS PHE ARG ILE HIS ALA PRO ASN ALA GLN LYS VAL
SEQRES 4 A 360 GLU ILE SER PHE ARG GLY GLU MSE THR LYS GLU ALA ASP
SEQRES 5 A 360 GLY TYR TRP SER LEU VAL SER LYS GLU PRO GLU VAL ILE
SEQRES 6 A 360 GLY PHE HIS TYR TYR GLN VAL ILE ILE ASP GLY VAL SER
SEQRES 7 A 360 ALA ALA ASP PRO ASN GLY LYS PRO PHE PHE GLY MSE GLY
SEQRES 8 A 360 LYS TRP VAL SER GLY ILE GLU ILE PRO GLU LYS GLY VAL
SEQRES 9 A 360 ASP TYR TYR SER ILE LYS ASN VAL PRO HIS GLY LEU ILE
SEQRES 10 A 360 SER GLN SER TRP TYR TYR SER ASP ILE ARG LYS GLU TRP
SEQRES 11 A 360 ARG ARG CYS ILE VAL TYR THR PRO ALA GLU TYR ASP LYS
SEQRES 12 A 360 ASN PRO THR LYS LYS TYR PRO VAL LEU TYR LEU GLN HIS
SEQRES 13 A 360 GLY MSE GLY GLU ASN GLU THR SER TRP ALA ASN GLN GLY
SEQRES 14 A 360 LYS MSE ASN PHE ILE MSE ASP ASN LEU ILE ALA GLU GLY
SEQRES 15 A 360 LYS ALA LYS PRO MSE ILE VAL VAL MSE ASP ASN GLY ASN
SEQRES 16 A 360 ILE GLU VAL PHE LYS THR ASN SER GLY GLU THR PRO GLU
SEQRES 17 A 360 ASP ALA ARG LYS ARG PHE GLY ALA GLU PHE PRO ALA ILE
SEQRES 18 A 360 LEU VAL ASN GLU ILE ILE PRO HIS ILE GLU SER ASN PHE
SEQRES 19 A 360 ARG THR LEU THR ASP ARG ASP ASN ARG ALA MSE ALA GLY
SEQRES 20 A 360 LEU SER TRP GLY GLY LEU LEU THR PHE ASN THR THR LEU
SEQRES 21 A 360 ASN ASN LEU ASP LYS PHE ALA TYR ILE GLY GLY PHE SER
SEQRES 22 A 360 GLY ALA GLY SER ILE ASP LEU LYS GLN LEU ASP THR VAL
SEQRES 23 A 360 TYR GLY GLY VAL PHE LYS ASN ARG LYS ALA PHE ASN ASP
SEQRES 24 A 360 LYS VAL HIS VAL PHE PHE LEU GLY ILE GLY SER GLU GLU
SEQRES 25 A 360 HIS PRO GLU ARG THR LYS ASN LEU SER ASP GLY LEU GLN
SEQRES 26 A 360 ALA ALA GLY ILE ASN THR ILE TYR TYR GLU SER PRO GLY
SEQRES 27 A 360 THR ALA HIS GLU PHE LEU THR TRP ARG ARG CYS LEU LYS
SEQRES 28 A 360 GLU PHE ALA PRO LEU LEU PHE LYS THR
MODRES 6MOT MSE A 71 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 114 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 182 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 195 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 199 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 211 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 215 MET MODIFIED RESIDUE
MODRES 6MOT MSE A 269 MET MODIFIED RESIDUE
HET MSE A 71 8
HET MSE A 114 8
HET MSE A 182 8
HET MSE A 195 8
HET MSE A 199 8
HET MSE A 211 8
HET MSE A 215 8
HET MSE A 269 8
HET EDO A 401 10
HET EDO A 402 10
HET EDO A 403 10
HET EDO A 404 10
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 EDO 4(C2 H6 O2)
FORMUL 6 HOH *306(H2 O)
HELIX 1 AA1 LYS A 194 GLU A 205 1 12
HELIX 2 AA2 GLU A 241 GLU A 249 1 9
HELIX 3 AA3 GLU A 249 PHE A 258 1 10
HELIX 4 AA4 ASP A 263 ASP A 265 5 3
HELIX 5 AA5 SER A 273 ASN A 285 1 13
HELIX 6 AA6 ASP A 303 LEU A 307 5 5
HELIX 7 AA7 THR A 309 VAL A 314 1 6
HELIX 8 AA8 ASN A 317 VAL A 325 1 9
HELIX 9 AA9 PRO A 338 GLY A 352 1 15
HELIX 10 AB1 GLU A 366 ALA A 378 1 13
HELIX 11 AB2 PRO A 379 LEU A 381 5 3
SHEET 1 AA1 5 THR A 30 PRO A 32 0
SHEET 2 AA1 5 ARG A 44 GLY A 46 -1 O ILE A 45 N THR A 31
SHEET 3 AA1 5 VAL A 51 HIS A 56 -1 O HIS A 52 N ARG A 44
SHEET 4 AA1 5 TYR A 78 VAL A 82 -1 O LEU A 81 N PHE A 53
SHEET 5 AA1 5 THR A 72 LYS A 73 -1 N THR A 72 O SER A 80
SHEET 1 AA2 4 GLY A 69 GLU A 70 0
SHEET 2 AA2 4 VAL A 63 ILE A 65 -1 N ILE A 65 O GLY A 69
SHEET 3 AA2 4 VAL A 96 ILE A 98 -1 O ILE A 97 N GLU A 64
SHEET 4 AA2 4 VAL A 101 ALA A 103 -1 O ALA A 103 N VAL A 96
SHEET 1 AA3 3 GLY A 90 TYR A 94 0
SHEET 2 AA3 3 LYS A 116 ILE A 123 -1 O ILE A 123 N GLY A 90
SHEET 3 AA3 3 PHE A 111 GLY A 113 -1 N PHE A 111 O VAL A 118
SHEET 1 AA4 8 LEU A 140 SER A 148 0
SHEET 2 AA4 8 GLU A 153 THR A 161 -1 O ARG A 155 N TYR A 146
SHEET 3 AA4 8 ILE A 212 MSE A 215 -1 O MSE A 215 N ILE A 158
SHEET 4 AA4 8 VAL A 175 GLN A 179 1 N LEU A 176 O VAL A 214
SHEET 5 AA4 8 ARG A 267 LEU A 272 1 O ALA A 268 N TYR A 177
SHEET 6 AA4 8 TYR A 292 PHE A 296 1 O PHE A 296 N GLY A 271
SHEET 7 AA4 8 VAL A 327 GLY A 333 1 O PHE A 329 N ILE A 293
SHEET 8 AA4 8 ILE A 356 SER A 360 1 O ILE A 356 N LEU A 330
LINK C GLU A 70 N MSE A 71 1555 1555 1.33
LINK C MSE A 71 N THR A 72 1555 1555 1.33
LINK C GLY A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N GLY A 115 1555 1555 1.33
LINK C GLY A 181 N MSE A 182 1555 1555 1.33
LINK C MSE A 182 N GLY A 183 1555 1555 1.33
LINK C LYS A 194 N MSE A 195 1555 1555 1.33
LINK C MSE A 195 N ASN A 196 1555 1555 1.34
LINK C ILE A 198 N MSE A 199 1555 1555 1.34
LINK C MSE A 199 N ASP A 200 1555 1555 1.34
LINK C PRO A 210 N MSE A 211 1555 1555 1.33
LINK C MSE A 211 N ILE A 212 1555 1555 1.33
LINK C VAL A 214 N MSE A 215 1555 1555 1.33
LINK C MSE A 215 N ASP A 216 1555 1555 1.33
LINK C ALA A 268 N MSE A 269 1555 1555 1.34
LINK C MSE A 269 N ALA A 270 1555 1555 1.33
CISPEP 1 TYR A 42 PRO A 43 0 5.03
SITE 1 AC1 6 ALA A 28 GLY A 46 GLU A 47 ASP A 48
SITE 2 AC1 6 HIS A 52 HOH A 660
SITE 1 AC2 6 PHE A 91 HIS A 92 TYR A 93 GLU A 366
SITE 2 AC2 6 PHE A 367 HOH A 538
SITE 1 AC3 8 GLU A 64 SER A 66 PHE A 67 ARG A 68
SITE 2 AC3 8 GLY A 69 ILE A 97 HOH A 650 HOH A 775
SITE 1 AC4 4 GLN A 349 ILE A 356 TYR A 357 HOH A 511
CRYST1 99.959 99.959 164.204 90.00 90.00 120.00 P 64 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 0.010004 0.005776 0.000000 0.00000
SCALE2 0.000000 0.011552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006090 0.00000
TER 2759 THR A 384
MASTER 395 0 12 11 20 0 7 6 3076 1 120 28
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