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HEADER HYDROLASE 04-OCT-18 6MOU
TITLE BACTEROIDES INTESTINALIS FERULOYL ESTERASE, BACINT_01033
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOAMYLASE N-TERMINAL DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 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 6MOU 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. 2.24 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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 98829
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.830
REMARK 3 FREE R VALUE TEST SET COUNT : 3788
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 76.4138 - 6.7185 1.00 3502 142 0.1697 0.2018
REMARK 3 2 6.7185 - 5.3331 1.00 3531 132 0.1583 0.1809
REMARK 3 3 5.3331 - 4.6591 1.00 3532 146 0.1288 0.1823
REMARK 3 4 4.6591 - 4.2331 1.00 3520 139 0.1181 0.1394
REMARK 3 5 4.2331 - 3.9297 1.00 3503 142 0.1373 0.1672
REMARK 3 6 3.9297 - 3.6981 1.00 3534 133 0.1480 0.1898
REMARK 3 7 3.6981 - 3.5129 1.00 3498 138 0.1623 0.2127
REMARK 3 8 3.5129 - 3.3599 1.00 3528 148 0.1803 0.2366
REMARK 3 9 3.3599 - 3.2306 1.00 3527 134 0.1829 0.2121
REMARK 3 10 3.2306 - 3.1191 1.00 3502 148 0.1956 0.2457
REMARK 3 11 3.1191 - 3.0216 1.00 3516 136 0.1975 0.2765
REMARK 3 12 3.0216 - 2.9352 1.00 3530 142 0.2067 0.2502
REMARK 3 13 2.9352 - 2.8579 1.00 3538 140 0.2130 0.2552
REMARK 3 14 2.8579 - 2.7882 1.00 3502 144 0.2269 0.2882
REMARK 3 15 2.7882 - 2.7248 1.00 3501 140 0.2268 0.2690
REMARK 3 16 2.7248 - 2.6668 1.00 3549 140 0.2383 0.2914
REMARK 3 17 2.6668 - 2.6135 1.00 3538 136 0.2392 0.3330
REMARK 3 18 2.6135 - 2.5642 1.00 3480 136 0.2399 0.3306
REMARK 3 19 2.5642 - 2.5184 1.00 3554 146 0.2560 0.2918
REMARK 3 20 2.5184 - 2.4757 1.00 3567 146 0.2533 0.3556
REMARK 3 21 2.4757 - 2.4357 1.00 3430 130 0.2731 0.3219
REMARK 3 22 2.4357 - 2.3983 1.00 3526 138 0.2669 0.2688
REMARK 3 23 2.3983 - 2.3630 1.00 3572 150 0.2709 0.3187
REMARK 3 24 2.3630 - 2.3297 1.00 3438 140 0.2797 0.2985
REMARK 3 25 2.3297 - 2.2982 1.00 3587 148 0.2943 0.3207
REMARK 3 26 2.2982 - 2.2684 1.00 3473 140 0.3076 0.3612
REMARK 3 27 2.2684 - 2.2400 1.00 3563 134 0.3170 0.4218
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.75
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 : NULL
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 6MOU 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_1000237233.
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 : 6.5
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 MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98838
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 76.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.78000
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: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 20% PEG 1,500.
REMARK 280 HAMPTON PEGRX SCREEN WELL B8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 67.53633
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 135.07267
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 135.07267
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 67.53633
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 4
REMARK 465 SER A 5
REMARK 465 HIS A 6
REMARK 465 MSE A 7
REMARK 465 ALA A 8
REMARK 465 SER A 9
REMARK 465 MSE A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLN A 14
REMARK 465 GLN A 15
REMARK 465 MSE A 16
REMARK 465 GLY A 17
REMARK 465 ARG A 18
REMARK 465 GLY A 19
REMARK 465 SER A 20
REMARK 465 MSE A 21
REMARK 465 GLN A 22
REMARK 465 GLN A 23
REMARK 465 GLN A 24
REMARK 465 THR A 384
REMARK 465 LYS A 385
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 HIS B 6
REMARK 465 MSE B 7
REMARK 465 ALA B 8
REMARK 465 SER B 9
REMARK 465 MSE B 10
REMARK 465 THR B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 GLN B 14
REMARK 465 GLN B 15
REMARK 465 MSE B 16
REMARK 465 GLY B 17
REMARK 465 ARG B 18
REMARK 465 GLY B 19
REMARK 465 SER B 20
REMARK 465 MSE B 21
REMARK 465 GLN B 22
REMARK 465 GLN B 23
REMARK 465 GLN B 24
REMARK 465 ASP B 25
REMARK 465 SER B 227
REMARK 465 GLY B 228
REMARK 465 GLU B 229
REMARK 465 THR B 230
REMARK 465 THR B 384
REMARK 465 LYS B 385
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 GLU B 366 O HOH B 501 1.78
REMARK 500 N THR B 369 O HOH B 501 2.07
REMARK 500 N ASP A 25 O HOH A 501 2.14
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 679 O HOH B 658 3544 2.17
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 ALA A 57 72.00 -153.99
REMARK 500 ASP A 76 15.98 59.40
REMARK 500 VAL A 118 -163.53 -124.22
REMARK 500 ASP A 129 12.49 -149.15
REMARK 500 ASN A 191 -86.69 -98.07
REMARK 500 GLU A 249 -37.11 -132.96
REMARK 500 SER A 273 -127.26 53.68
REMARK 500 ASN A 286 48.58 -144.00
REMARK 500 HIS A 337 61.71 61.50
REMARK 500 ALA A 364 -134.24 -125.81
REMARK 500 ASP B 76 18.76 81.14
REMARK 500 VAL B 118 -162.23 -119.70
REMARK 500 ASN B 191 -86.96 -101.91
REMARK 500 GLU B 249 -51.87 -128.34
REMARK 500 SER B 273 -122.66 57.91
REMARK 500 ASN B 286 46.67 -149.73
REMARK 500 HIS B 337 71.17 56.56
REMARK 500 ALA B 364 -140.64 -121.17
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 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 B 401
DBREF 6MOU A 22 385 UNP B3C969 B3C969_9BACE 24 387
DBREF 6MOU B 22 385 UNP B3C969 B3C969_9BACE 24 387
SEQADV 6MOU GLY A 4 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU SER A 5 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU HIS A 6 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE A 7 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU ALA A 8 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU SER A 9 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE A 10 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU THR A 11 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY A 12 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY A 13 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLN A 14 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLN A 15 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE A 16 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY A 17 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU ARG A 18 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY A 19 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU SER A 20 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE A 21 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY B 4 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU SER B 5 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU HIS B 6 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE B 7 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU ALA B 8 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU SER B 9 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE B 10 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU THR B 11 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY B 12 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY B 13 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLN B 14 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLN B 15 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE B 16 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY B 17 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU ARG B 18 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU GLY B 19 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU SER B 20 UNP B3C969 EXPRESSION TAG
SEQADV 6MOU MSE B 21 UNP B3C969 EXPRESSION TAG
SEQRES 1 A 382 GLY SER HIS MSE ALA SER MSE THR GLY GLY GLN GLN MSE
SEQRES 2 A 382 GLY ARG GLY SER MSE GLN GLN GLN ASP PHE PRO ALA GLY
SEQRES 3 A 382 THR THR PRO ASN GLU HIS ASN ILE ASN GLY ALA ASP TYR
SEQRES 4 A 382 PRO ARG ILE GLY GLU ASP ARG ARG VAL HIS PHE ARG ILE
SEQRES 5 A 382 HIS ALA PRO ASN ALA GLN LYS VAL GLU ILE SER PHE ARG
SEQRES 6 A 382 GLY GLU MSE THR LYS GLU ALA ASP GLY TYR TRP SER LEU
SEQRES 7 A 382 VAL SER LYS GLU PRO GLU VAL ILE GLY PHE HIS TYR TYR
SEQRES 8 A 382 GLN VAL ILE ILE ASP GLY VAL SER ALA ALA ASP PRO ASN
SEQRES 9 A 382 GLY LYS PRO PHE PHE GLY MSE GLY LYS TRP VAL SER GLY
SEQRES 10 A 382 ILE GLU ILE PRO GLU LYS GLY VAL ASP TYR TYR SER ILE
SEQRES 11 A 382 LYS ASN VAL PRO HIS GLY LEU ILE SER GLN SER TRP TYR
SEQRES 12 A 382 TYR SER ASP ILE ARG LYS GLU TRP ARG ARG CYS ILE VAL
SEQRES 13 A 382 TYR THR PRO ALA GLU TYR ASP LYS ASN PRO THR LYS LYS
SEQRES 14 A 382 TYR PRO VAL LEU TYR LEU GLN HIS GLY MSE GLY GLU ASN
SEQRES 15 A 382 GLU THR SER TRP ALA ASN GLN GLY LYS MSE ASN PHE ILE
SEQRES 16 A 382 MSE ASP ASN LEU ILE ALA GLU GLY LYS ALA LYS PRO MSE
SEQRES 17 A 382 ILE VAL VAL MSE ASP ASN GLY ASN ILE GLU VAL PHE LYS
SEQRES 18 A 382 THR ASN SER GLY GLU THR PRO GLU ASP ALA ARG LYS ARG
SEQRES 19 A 382 PHE GLY ALA GLU PHE PRO ALA ILE LEU VAL ASN GLU ILE
SEQRES 20 A 382 ILE PRO HIS ILE GLU SER ASN PHE ARG THR LEU THR ASP
SEQRES 21 A 382 ARG ASP ASN ARG ALA MSE ALA GLY LEU SER TRP GLY GLY
SEQRES 22 A 382 LEU LEU THR PHE ASN THR THR LEU ASN ASN LEU ASP LYS
SEQRES 23 A 382 PHE ALA TYR ILE GLY GLY PHE SER GLY ALA GLY SER ILE
SEQRES 24 A 382 ASP LEU LYS GLN LEU ASP THR VAL TYR GLY GLY VAL PHE
SEQRES 25 A 382 LYS ASN ARG LYS ALA PHE ASN ASP LYS VAL HIS VAL PHE
SEQRES 26 A 382 PHE LEU GLY ILE GLY SER GLU GLU HIS PRO GLU ARG THR
SEQRES 27 A 382 LYS ASN LEU SER ASP GLY LEU GLN ALA ALA GLY ILE ASN
SEQRES 28 A 382 THR ILE TYR TYR GLU SER PRO GLY THR ALA HIS GLU PHE
SEQRES 29 A 382 LEU THR TRP ARG ARG CYS LEU LYS GLU PHE ALA PRO LEU
SEQRES 30 A 382 LEU PHE LYS THR LYS
SEQRES 1 B 382 GLY SER HIS MSE ALA SER MSE THR GLY GLY GLN GLN MSE
SEQRES 2 B 382 GLY ARG GLY SER MSE GLN GLN GLN ASP PHE PRO ALA GLY
SEQRES 3 B 382 THR THR PRO ASN GLU HIS ASN ILE ASN GLY ALA ASP TYR
SEQRES 4 B 382 PRO ARG ILE GLY GLU ASP ARG ARG VAL HIS PHE ARG ILE
SEQRES 5 B 382 HIS ALA PRO ASN ALA GLN LYS VAL GLU ILE SER PHE ARG
SEQRES 6 B 382 GLY GLU MSE THR LYS GLU ALA ASP GLY TYR TRP SER LEU
SEQRES 7 B 382 VAL SER LYS GLU PRO GLU VAL ILE GLY PHE HIS TYR TYR
SEQRES 8 B 382 GLN VAL ILE ILE ASP GLY VAL SER ALA ALA ASP PRO ASN
SEQRES 9 B 382 GLY LYS PRO PHE PHE GLY MSE GLY LYS TRP VAL SER GLY
SEQRES 10 B 382 ILE GLU ILE PRO GLU LYS GLY VAL ASP TYR TYR SER ILE
SEQRES 11 B 382 LYS ASN VAL PRO HIS GLY LEU ILE SER GLN SER TRP TYR
SEQRES 12 B 382 TYR SER ASP ILE ARG LYS GLU TRP ARG ARG CYS ILE VAL
SEQRES 13 B 382 TYR THR PRO ALA GLU TYR ASP LYS ASN PRO THR LYS LYS
SEQRES 14 B 382 TYR PRO VAL LEU TYR LEU GLN HIS GLY MSE GLY GLU ASN
SEQRES 15 B 382 GLU THR SER TRP ALA ASN GLN GLY LYS MSE ASN PHE ILE
SEQRES 16 B 382 MSE ASP ASN LEU ILE ALA GLU GLY LYS ALA LYS PRO MSE
SEQRES 17 B 382 ILE VAL VAL MSE ASP ASN GLY ASN ILE GLU VAL PHE LYS
SEQRES 18 B 382 THR ASN SER GLY GLU THR PRO GLU ASP ALA ARG LYS ARG
SEQRES 19 B 382 PHE GLY ALA GLU PHE PRO ALA ILE LEU VAL ASN GLU ILE
SEQRES 20 B 382 ILE PRO HIS ILE GLU SER ASN PHE ARG THR LEU THR ASP
SEQRES 21 B 382 ARG ASP ASN ARG ALA MSE ALA GLY LEU SER TRP GLY GLY
SEQRES 22 B 382 LEU LEU THR PHE ASN THR THR LEU ASN ASN LEU ASP LYS
SEQRES 23 B 382 PHE ALA TYR ILE GLY GLY PHE SER GLY ALA GLY SER ILE
SEQRES 24 B 382 ASP LEU LYS GLN LEU ASP THR VAL TYR GLY GLY VAL PHE
SEQRES 25 B 382 LYS ASN ARG LYS ALA PHE ASN ASP LYS VAL HIS VAL PHE
SEQRES 26 B 382 PHE LEU GLY ILE GLY SER GLU GLU HIS PRO GLU ARG THR
SEQRES 27 B 382 LYS ASN LEU SER ASP GLY LEU GLN ALA ALA GLY ILE ASN
SEQRES 28 B 382 THR ILE TYR TYR GLU SER PRO GLY THR ALA HIS GLU PHE
SEQRES 29 B 382 LEU THR TRP ARG ARG CYS LEU LYS GLU PHE ALA PRO LEU
SEQRES 30 B 382 LEU PHE LYS THR LYS
MODRES 6MOU MSE A 71 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 114 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 182 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 195 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 199 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 211 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 215 MET MODIFIED RESIDUE
MODRES 6MOU MSE A 269 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 71 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 114 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 182 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 195 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 199 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 211 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 215 MET MODIFIED RESIDUE
MODRES 6MOU MSE B 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 MSE B 71 8
HET MSE B 114 8
HET MSE B 182 8
HET MSE B 195 8
HET MSE B 199 8
HET MSE B 211 8
HET MSE B 215 8
HET MSE B 269 8
HET EDO A 401 10
HET EDO A 402 10
HET EDO A 403 10
HET EDO B 401 10
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 7 HOH *445(H2 O)
HELIX 1 AA1 LYS A 194 GLU A 205 1 12
HELIX 2 AA2 THR A 230 PHE A 238 1 9
HELIX 3 AA3 GLU A 241 GLU A 249 1 9
HELIX 4 AA4 GLU A 249 PHE A 258 1 10
HELIX 5 AA5 ASP A 263 ASP A 265 5 3
HELIX 6 AA6 TRP A 274 ASN A 285 1 12
HELIX 7 AA7 ASP A 303 LEU A 307 5 5
HELIX 8 AA8 THR A 309 VAL A 314 5 6
HELIX 9 AA9 ASN A 317 VAL A 325 1 9
HELIX 10 AB1 PRO A 338 GLY A 352 1 15
HELIX 11 AB2 GLU A 366 ALA A 378 1 13
HELIX 12 AB3 PRO A 379 LEU A 381 5 3
HELIX 13 AB4 GLU B 164 ASN B 168 5 5
HELIX 14 AB5 THR B 187 ASN B 191 5 5
HELIX 15 AB6 LYS B 194 GLU B 205 1 12
HELIX 16 AB7 GLU B 232 PHE B 238 1 7
HELIX 17 AB8 GLU B 241 GLU B 249 1 9
HELIX 18 AB9 GLU B 249 PHE B 258 1 10
HELIX 19 AC1 ASP B 263 ASP B 265 5 3
HELIX 20 AC2 TRP B 274 ASN B 285 1 12
HELIX 21 AC3 ASP B 303 LEU B 307 5 5
HELIX 22 AC4 THR B 309 VAL B 314 1 6
HELIX 23 AC5 ASN B 317 VAL B 325 1 9
HELIX 24 AC6 PRO B 338 GLY B 352 1 15
HELIX 25 AC7 GLU B 366 ALA B 378 1 13
HELIX 26 AC8 PRO B 379 LEU B 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 121 N HIS A 92
SHEET 3 AA3 3 PHE A 111 GLY A 113 -1 N PHE A 111 O VAL A 118
SHEET 1 AA416 ILE A 356 SER A 360 0
SHEET 2 AA416 VAL A 327 GLY A 333 1 N LEU A 330 O ILE A 356
SHEET 3 AA416 TYR A 292 PHE A 296 1 N GLY A 295 O PHE A 329
SHEET 4 AA416 ARG A 267 LEU A 272 1 N GLY A 271 O PHE A 296
SHEET 5 AA416 VAL A 175 GLN A 179 1 N TYR A 177 O ALA A 268
SHEET 6 AA416 ILE A 212 MSE A 215 1 O VAL A 214 N LEU A 176
SHEET 7 AA416 GLU A 153 THR A 161 -1 N ILE A 158 O MSE A 215
SHEET 8 AA416 LEU A 140 SER A 148 -1 N SER A 148 O GLU A 153
SHEET 9 AA416 LEU B 140 SER B 148 -1 O ILE B 141 N GLN A 143
SHEET 10 AA416 GLU B 153 THR B 161 -1 O VAL B 159 N SER B 142
SHEET 11 AA416 ILE B 212 MSE B 215 -1 O MSE B 215 N ILE B 158
SHEET 12 AA416 VAL B 175 GLN B 179 1 N LEU B 176 O VAL B 214
SHEET 13 AA416 ARG B 267 LEU B 272 1 O ALA B 270 N GLN B 179
SHEET 14 AA416 TYR B 292 PHE B 296 1 O PHE B 296 N GLY B 271
SHEET 15 AA416 VAL B 327 GLY B 333 1 O PHE B 329 N GLY B 295
SHEET 16 AA416 ILE B 356 SER B 360 1 O SER B 360 N ILE B 332
SHEET 1 AA5 5 THR B 30 PRO B 32 0
SHEET 2 AA5 5 ARG B 44 GLY B 46 -1 O ILE B 45 N THR B 31
SHEET 3 AA5 5 VAL B 51 HIS B 56 -1 O HIS B 52 N ARG B 44
SHEET 4 AA5 5 TYR B 78 VAL B 82 -1 O LEU B 81 N PHE B 53
SHEET 5 AA5 5 THR B 72 LYS B 73 -1 N THR B 72 O SER B 80
SHEET 1 AA6 4 GLY B 69 GLU B 70 0
SHEET 2 AA6 4 VAL B 63 ILE B 65 -1 N ILE B 65 O GLY B 69
SHEET 3 AA6 4 VAL B 96 ILE B 98 -1 O ILE B 97 N GLU B 64
SHEET 4 AA6 4 VAL B 101 ALA B 103 -1 O ALA B 103 N VAL B 96
SHEET 1 AA7 3 GLY B 90 TYR B 94 0
SHEET 2 AA7 3 LYS B 116 ILE B 123 -1 O ILE B 123 N GLY B 90
SHEET 3 AA7 3 PHE B 111 GLY B 113 -1 N PHE B 111 O VAL B 118
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 1.32
LINK C MSE A 195 N ASN A 196 1555 1555 1.33
LINK C ILE A 198 N MSE A 199 1555 1555 1.33
LINK C MSE A 199 N ASP A 200 1555 1555 1.34
LINK C PRO A 210 N MSE A 211 1555 1555 1.32
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 1.33
LINK C MSE A 269 N ALA A 270 1555 1555 1.33
LINK C GLU B 70 N MSE B 71 1555 1555 1.33
LINK C MSE B 71 N THR B 72 1555 1555 1.33
LINK C GLY B 113 N MSE B 114 1555 1555 1.33
LINK C MSE B 114 N GLY B 115 1555 1555 1.33
LINK C GLY B 181 N MSE B 182 1555 1555 1.33
LINK C MSE B 182 N GLY B 183 1555 1555 1.33
LINK C LYS B 194 N MSE B 195 1555 1555 1.33
LINK C MSE B 195 N ASN B 196 1555 1555 1.33
LINK C ILE B 198 N MSE B 199 1555 1555 1.33
LINK C MSE B 199 N ASP B 200 1555 1555 1.34
LINK C PRO B 210 N MSE B 211 1555 1555 1.32
LINK C MSE B 211 N ILE B 212 1555 1555 1.32
LINK C VAL B 214 N MSE B 215 1555 1555 1.33
LINK C MSE B 215 N ASP B 216 1555 1555 1.32
LINK C ALA B 268 N MSE B 269 1555 1555 1.33
LINK C MSE B 269 N ALA B 270 1555 1555 1.33
CISPEP 1 TYR A 42 PRO A 43 0 0.91
CISPEP 2 TYR B 42 PRO B 43 0 -0.10
SITE 1 AC1 7 ALA A 28 GLY A 29 THR A 30 GLY A 46
SITE 2 AC1 7 GLU A 47 ASP A 48 HIS A 52
SITE 1 AC2 7 ILE A 65 SER A 66 PHE A 67 ARG A 68
SITE 2 AC2 7 GLY A 69 ASN A 168 HOH A 622
SITE 1 AC3 3 GLU A 64 GLY A 100 LYS A 171
SITE 1 AC4 7 GLU B 64 ILE B 65 SER B 66 PHE B 67
SITE 2 AC4 7 ARG B 68 GLY B 69 ILE B 97
CRYST1 95.206 95.206 202.609 90.00 90.00 120.00 P 31 2 1 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 0.010504 0.006064 0.000000 0.00000
SCALE2 0.000000 0.012128 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004936 0.00000
TER 2869 LYS A 383
TER 5704 LYS B 383
MASTER 368 0 20 26 40 0 7 6 6163 2 200 60
END |