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HEADER HYDROLASE 13-JUN-19 6RZO
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL CARBOHYDRATE BINDING MODULE FAMILY
TITLE 2 48 AND FERULIC ACID ESTERASE FROM THE MULTI-ENZYME CE1-GH62-GH10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FERULIC ACID ESTERASE;
COMPND 8 CHAIN: B;
COMPND 9 EC: 3.1.1.73;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 8 ORGANISM_TAXID: 77133;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERULIC ACID ESTEREASE, CARBOHYDRATE ESTERASE FAMILY 1, CE1, CBM48,
KEYWDS 2 CARBOHYDRATE BINDING MODULE FAMILY 48, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FREDSLUND,D.H.WELNER,C.WILKENS
REVDAT 1 25-SEP-19 6RZO 0
JRNL AUTH J.HOLCK,F.FREDSLUND,M.S.MOELLER,J.BRASK,K.B.R.M.KROGH,
JRNL AUTH 2 L.LANGE,D.H.WELNER,B.SVENSSON,A.S.MEYER,S.JANECEK,C.WILKENS
JRNL TITL CARBOHYDRATE BINDING MODULE OF FAMILY 48 ENABLES ACTION OF
JRNL TITL 2 FERULIC ACID ESTERASES ON POLYMERIC ARABINOXYLAN
JRNL REF J.BIOL.CHEM. 2019
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.63 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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.310
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 89975
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) : 0.170
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 4438
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 49.6611 - 5.0697 1.00 3259 160 0.1766 0.1881
REMARK 3 2 5.0697 - 4.0245 1.00 3122 165 0.1295 0.1394
REMARK 3 3 4.0245 - 3.5160 1.00 3091 151 0.1426 0.1426
REMARK 3 4 3.5160 - 3.1946 1.00 3065 152 0.1516 0.1838
REMARK 3 5 3.1946 - 2.9656 1.00 3060 147 0.1624 0.1839
REMARK 3 6 2.9656 - 2.7908 1.00 3026 145 0.1669 0.1688
REMARK 3 7 2.7908 - 2.6510 1.00 3024 181 0.1621 0.1821
REMARK 3 8 2.6510 - 2.5356 1.00 3012 170 0.1612 0.2052
REMARK 3 9 2.5356 - 2.4380 1.00 3018 147 0.1592 0.1846
REMARK 3 10 2.4380 - 2.3539 1.00 3047 154 0.1584 0.1961
REMARK 3 11 2.3539 - 2.2803 1.00 2982 180 0.1526 0.1989
REMARK 3 12 2.2803 - 2.2151 1.00 3003 151 0.1629 0.1941
REMARK 3 13 2.2151 - 2.1568 1.00 3023 159 0.1571 0.2003
REMARK 3 14 2.1568 - 2.1042 1.00 2975 155 0.1681 0.2008
REMARK 3 15 2.1042 - 2.0563 1.00 3011 166 0.1675 0.2260
REMARK 3 16 2.0563 - 2.0126 0.99 2963 165 0.1713 0.1964
REMARK 3 17 2.0126 - 1.9723 1.00 2993 150 0.1802 0.2063
REMARK 3 18 1.9723 - 1.9351 1.00 2991 164 0.1891 0.2144
REMARK 3 19 1.9351 - 1.9005 1.00 2993 139 0.1940 0.2274
REMARK 3 20 1.9005 - 1.8683 1.00 3013 150 0.2021 0.2352
REMARK 3 21 1.8683 - 1.8382 1.00 2985 152 0.2080 0.2836
REMARK 3 22 1.8382 - 1.8099 0.99 2971 150 0.2243 0.2542
REMARK 3 23 1.8099 - 1.7833 0.94 2818 143 0.2393 0.2913
REMARK 3 24 1.7833 - 1.7582 0.90 2683 139 0.2468 0.2664
REMARK 3 25 1.7582 - 1.7344 0.86 2581 139 0.2503 0.2800
REMARK 3 26 1.7344 - 1.7119 0.82 2403 141 0.2707 0.2794
REMARK 3 27 1.7119 - 1.6905 0.77 2307 118 0.2682 0.3207
REMARK 3 28 1.6905 - 1.6701 0.73 2190 107 0.2744 0.3041
REMARK 3 29 1.6701 - 1.6507 0.69 2081 106 0.2928 0.3171
REMARK 3 30 1.6507 - 1.6321 0.62 1847 92 0.2983 0.3520
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.310
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 : 0.009 5634
REMARK 3 ANGLE : 0.864 7646
REMARK 3 CHIRALITY : 0.062 788
REMARK 3 PLANARITY : 0.006 1021
REMARK 3 DIHEDRAL : 12.904 3324
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): 58.2578 43.5699 38.9441
REMARK 3 T TENSOR
REMARK 3 T11: 0.1063 T22: 0.0828
REMARK 3 T33: 0.1280 T12: -0.0001
REMARK 3 T13: -0.0033 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.5429 L22: 0.3602
REMARK 3 L33: 1.1576 L12: -0.0955
REMARK 3 L13: -0.2344 L23: 0.0499
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: 0.0446 S13: -0.0104
REMARK 3 S21: 0.0034 S22: -0.0368 S23: 0.0304
REMARK 3 S31: -0.0514 S32: -0.0698 S33: 0.0351
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 6RZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100733.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87313
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90065
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.632
REMARK 200 RESOLUTION RANGE LOW (A) : 49.638
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.1
REMARK 200 STARTING MODEL: 1JT2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0 W/V POLYETHYLENE GLYCOL 3,350, 100
REMARK 280 MM BIS-TRIS PROPANE PH 6.5, 200 MM SODIUM FLUORIDE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 33.29750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.21450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.90800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.21450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.29750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.90800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 ILE B 198
REMARK 465 ARG B 199
REMARK 465 PHE B 200
REMARK 465 GLY B 201
REMARK 465 GLY B 202
REMARK 465 ILE B 203
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 HD21 ASN B 166 O HOH B 404 1.55
REMARK 500 HZ3 LYS B 118 O HOH B 406 1.59
REMARK 500 OD1 ASN A 166 O HOH A 401 2.17
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 N ARG B 204 O HOH B 483 4456 2.18
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 30 71.95 -154.23
REMARK 500 ASN A 166 -83.29 -105.27
REMARK 500 ASN A 166 -85.36 -103.18
REMARK 500 GLU A 218 -56.30 -122.80
REMARK 500 SER A 242 -126.99 53.73
REMARK 500 GLU A 296 -136.89 -91.42
REMARK 500 ALA A 324 -133.20 -125.51
REMARK 500 ALA B 30 72.62 -150.75
REMARK 500 ASN B 166 -82.83 -105.01
REMARK 500 ASN B 166 -83.02 -104.50
REMARK 500 GLU B 218 -57.41 -125.39
REMARK 500 SER B 242 -128.09 51.98
REMARK 500 ASN B 255 53.90 -140.02
REMARK 500 GLU B 296 -147.62 -81.76
REMARK 500 ASN B 297 66.96 -111.93
REMARK 500 ALA B 324 -138.60 -119.35
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 837 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B 829 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 830 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 831 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B 832 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B 833 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 834 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 835 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH B 836 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B 837 DISTANCE = 7.93 ANGSTROMS
DBREF 6RZO A 0 343 PDB 6RZO 6RZO 0 343
DBREF 6RZO B 0 344 PDB 6RZO 6RZO 0 344
SEQRES 1 A 344 MET GLU ASP PHE LYS PRO THR SER THR ASN GLN PRO GLY
SEQRES 2 A 344 ARG GLN TYR PRO GLN VAL ASN SER GLU GLY ARG VAL ARG
SEQRES 3 A 344 ALA ARG ILE GLU ALA PRO GLN ALA HIS THR VAL LEU LEU
SEQRES 4 A 344 ASP ILE GLY GLY VAL ARG TYR PRO MET THR GLN GLY GLU
SEQRES 5 A 344 ASP GLY ALA TRP ILE GLY ASP SER ARG PRO GLN ASP GLU
SEQRES 6 A 344 GLY PHE HIS TYR TYR GLN LEU VAL ILE ASP GLY ALA ARG
SEQRES 7 A 344 VAL PRO ASP PRO GLY SER LEU TYR PHE PHE GLY ALA ASN
SEQRES 8 A 344 ARG TRP GLY SER GLY VAL GLU VAL PRO ALA HIS ASP GLN
SEQRES 9 A 344 ASP PHE TYR ALA ILE LYS ASP VAL PRO HIS GLY ARG VAL
SEQRES 10 A 344 GLN LYS ILE LEU PHE PRO SER GLY SER THR SER THR ILE
SEQRES 11 A 344 ARG ARG ALA PHE VAL TYR THR PRO PRO ASP TYR GLY LYS
SEQRES 12 A 344 ASP LEU SER LYS ARG TYR PRO VAL LEU TYR LEU GLN HIS
SEQRES 13 A 344 GLY TRP GLY GLU ASP GLU THR GLY TRP ALA ASN GLN GLY
SEQRES 14 A 344 ARG VAL ASN LEU ILE MET ASP ASN LEU ILE ALA GLU GLY
SEQRES 15 A 344 LYS ALA ARG PRO PHE ILE ILE VAL MET THR TYR GLY MET
SEQRES 16 A 344 THR ASN GLU ILE ARG PHE GLY GLY ILE ARG GLU PHE ASP
SEQRES 17 A 344 ILE ARG PRO PHE GLN THR VAL LEU VAL ASP GLU LEU ILE
SEQRES 18 A 344 PRO TYR ILE ASP ALA ASN PHE ARG THR ARG SER ASP GLN
SEQRES 19 A 344 PRO HIS ARG ALA MET ALA GLY LEU SER MET GLY GLY MET
SEQRES 20 A 344 GLU THR ARG LEU ILE THR MET ASN ASN LEU ASP LEU PHE
SEQRES 21 A 344 SER HIS ILE GLY LEU PHE SER GLY GLY THR ILE SER ALA
SEQRES 22 A 344 SER ASP ILE THR ASP ARG ASP VAL PHE LYS GLN LYS ILE
SEQRES 23 A 344 LYS LEU VAL PHE VAL SER CYS GLY SER ARG GLU ASN PRO
SEQRES 24 A 344 GLY ARG PHE ARG PRO ALA VAL ASP SER LEU GLN GLN ALA
SEQRES 25 A 344 GLY ILE SER ALA VAL SER TYR VAL SER PRO ASP THR ALA
SEQRES 26 A 344 HIS GLU TRP GLN THR TRP ARG ARG SER PHE TYR GLN PHE
SEQRES 27 A 344 ALA GLN LEU LEU PHE GLN
SEQRES 1 B 345 MET GLU ASP PHE LYS PRO THR SER THR ASN GLN PRO GLY
SEQRES 2 B 345 ARG GLN TYR PRO GLN VAL ASN SER GLU GLY ARG VAL ARG
SEQRES 3 B 345 ALA ARG ILE GLU ALA PRO GLN ALA HIS THR VAL LEU LEU
SEQRES 4 B 345 ASP ILE GLY GLY VAL ARG TYR PRO MET THR GLN GLY GLU
SEQRES 5 B 345 ASP GLY ALA TRP ILE GLY ASP SER ARG PRO GLN ASP GLU
SEQRES 6 B 345 GLY PHE HIS TYR TYR GLN LEU VAL ILE ASP GLY ALA ARG
SEQRES 7 B 345 VAL PRO ASP PRO GLY SER LEU TYR PHE PHE GLY ALA ASN
SEQRES 8 B 345 ARG TRP GLY SER GLY VAL GLU VAL PRO ALA HIS ASP GLN
SEQRES 9 B 345 ASP PHE TYR ALA ILE LYS ASP VAL PRO HIS GLY ARG VAL
SEQRES 10 B 345 GLN LYS ILE LEU PHE PRO SER GLY SER THR SER THR ILE
SEQRES 11 B 345 ARG ARG ALA PHE VAL TYR THR PRO PRO ASP TYR GLY LYS
SEQRES 12 B 345 ASP LEU SER LYS ARG TYR PRO VAL LEU TYR LEU GLN HIS
SEQRES 13 B 345 GLY TRP GLY GLU ASP GLU THR GLY TRP ALA ASN GLN GLY
SEQRES 14 B 345 ARG VAL ASN LEU ILE MET ASP ASN LEU ILE ALA GLU GLY
SEQRES 15 B 345 LYS ALA ARG PRO PHE ILE ILE VAL MET THR TYR GLY MET
SEQRES 16 B 345 THR ASN GLU ILE ARG PHE GLY GLY ILE ARG GLU PHE ASP
SEQRES 17 B 345 ILE ARG PRO PHE GLN THR VAL LEU VAL ASP GLU LEU ILE
SEQRES 18 B 345 PRO TYR ILE ASP ALA ASN PHE ARG THR ARG SER ASP GLN
SEQRES 19 B 345 PRO HIS ARG ALA MET ALA GLY LEU SER MET GLY GLY MET
SEQRES 20 B 345 GLU THR ARG LEU ILE THR MET ASN ASN LEU ASP LEU PHE
SEQRES 21 B 345 SER HIS ILE GLY LEU PHE SER GLY GLY THR ILE SER ALA
SEQRES 22 B 345 SER ASP ILE THR ASP ARG ASP VAL PHE LYS GLN LYS ILE
SEQRES 23 B 345 LYS LEU VAL PHE VAL SER CYS GLY SER ARG GLU ASN PRO
SEQRES 24 B 345 GLY ARG PHE ARG PRO ALA VAL ASP SER LEU GLN GLN ALA
SEQRES 25 B 345 GLY ILE SER ALA VAL SER TYR VAL SER PRO ASP THR ALA
SEQRES 26 B 345 HIS GLU TRP GLN THR TRP ARG ARG SER PHE TYR GLN PHE
SEQRES 27 B 345 ALA GLN LEU LEU PHE GLN LEU
FORMUL 3 HOH *876(H2 O)
HELIX 1 AA1 ASP A 102 ALA A 107 5 6
HELIX 2 AA2 ARG A 169 GLU A 180 1 12
HELIX 3 AA3 ILE A 208 GLU A 218 1 11
HELIX 4 AA4 GLU A 218 PHE A 227 1 10
HELIX 5 AA5 ASP A 232 PRO A 234 5 3
HELIX 6 AA6 SER A 242 ASN A 255 1 14
HELIX 7 AA7 SER A 271 ILE A 275 5 5
HELIX 8 AA8 ASP A 277 ILE A 285 1 9
HELIX 9 AA9 ASN A 297 GLY A 299 5 3
HELIX 10 AB1 ARG A 300 ALA A 311 1 12
HELIX 11 AB2 GLU A 326 GLN A 339 1 14
HELIX 12 AB3 ASP B 102 ALA B 107 5 6
HELIX 13 AB4 ARG B 169 GLU B 180 1 12
HELIX 14 AB5 ILE B 208 GLU B 218 1 11
HELIX 15 AB6 GLU B 218 PHE B 227 1 10
HELIX 16 AB7 ASP B 232 PRO B 234 5 3
HELIX 17 AB8 SER B 242 ASN B 255 1 14
HELIX 18 AB9 SER B 271 ILE B 275 5 5
HELIX 19 AC1 ASP B 277 ILE B 285 1 9
HELIX 20 AC2 ASN B 297 ALA B 311 1 15
HELIX 21 AC3 GLU B 326 GLN B 339 1 14
SHEET 1 AA1 8 LYS A 4 PRO A 5 0
SHEET 2 AA1 8 GLN A 17 VAL A 18 -1 O VAL A 18 N LYS A 4
SHEET 3 AA1 8 VAL A 24 ILE A 28 -1 O ARG A 25 N GLN A 17
SHEET 4 AA1 8 TRP A 55 ASP A 58 -1 O TRP A 55 N ILE A 28
SHEET 5 AA1 8 VAL A 43 GLN A 49 -1 N THR A 48 O ILE A 56
SHEET 6 AA1 8 VAL A 36 ILE A 40 -1 N LEU A 38 O TYR A 45
SHEET 7 AA1 8 GLY A 65 ILE A 73 -1 O GLN A 70 N ASP A 39
SHEET 8 AA1 8 ALA A 76 VAL A 78 -1 O VAL A 78 N LEU A 71
SHEET 1 AA2 9 LYS A 4 PRO A 5 0
SHEET 2 AA2 9 GLN A 17 VAL A 18 -1 O VAL A 18 N LYS A 4
SHEET 3 AA2 9 VAL A 24 ILE A 28 -1 O ARG A 25 N GLN A 17
SHEET 4 AA2 9 TRP A 55 ASP A 58 -1 O TRP A 55 N ILE A 28
SHEET 5 AA2 9 VAL A 43 GLN A 49 -1 N THR A 48 O ILE A 56
SHEET 6 AA2 9 VAL A 36 ILE A 40 -1 N LEU A 38 O TYR A 45
SHEET 7 AA2 9 GLY A 65 ILE A 73 -1 O GLN A 70 N ASP A 39
SHEET 8 AA2 9 ARG A 91 VAL A 98 -1 O VAL A 98 N GLY A 65
SHEET 9 AA2 9 TYR A 85 GLY A 88 -1 N PHE A 86 O GLY A 93
SHEET 1 AA316 ALA A 315 SER A 320 0
SHEET 2 AA316 LEU A 287 GLY A 293 1 N VAL A 288 O VAL A 316
SHEET 3 AA316 HIS A 261 PHE A 265 1 N ILE A 262 O PHE A 289
SHEET 4 AA316 ARG A 236 LEU A 241 1 N GLY A 240 O PHE A 265
SHEET 5 AA316 VAL A 150 GLN A 154 1 N TYR A 152 O ALA A 239
SHEET 6 AA316 ILE A 187 THR A 191 1 O VAL A 189 N LEU A 151
SHEET 7 AA316 THR A 128 THR A 136 -1 N TYR A 135 O ILE A 188
SHEET 8 AA316 ARG A 115 SER A 123 -1 N GLN A 117 O VAL A 134
SHEET 9 AA316 ARG B 115 SER B 123 -1 O VAL B 116 N LYS A 118
SHEET 10 AA316 THR B 128 THR B 136 -1 O ARG B 130 N PHE B 121
SHEET 11 AA316 ILE B 187 THR B 191 -1 O MET B 190 N PHE B 133
SHEET 12 AA316 VAL B 150 GLN B 154 1 N LEU B 151 O VAL B 189
SHEET 13 AA316 ARG B 236 LEU B 241 1 O ALA B 237 N TYR B 152
SHEET 14 AA316 HIS B 261 PHE B 265 1 O PHE B 265 N GLY B 240
SHEET 15 AA316 LEU B 287 GLY B 293 1 O PHE B 289 N ILE B 262
SHEET 16 AA316 ALA B 315 SER B 320 1 O VAL B 316 N VAL B 288
SHEET 1 AA4 8 LYS B 4 PRO B 5 0
SHEET 2 AA4 8 GLN B 17 VAL B 18 -1 O VAL B 18 N LYS B 4
SHEET 3 AA4 8 VAL B 24 ILE B 28 -1 O ARG B 25 N GLN B 17
SHEET 4 AA4 8 TRP B 55 ASP B 58 -1 O TRP B 55 N ILE B 28
SHEET 5 AA4 8 VAL B 43 GLN B 49 -1 N THR B 48 O ILE B 56
SHEET 6 AA4 8 VAL B 36 ILE B 40 -1 N LEU B 38 O TYR B 45
SHEET 7 AA4 8 GLY B 65 ILE B 73 -1 O GLN B 70 N ASP B 39
SHEET 8 AA4 8 ALA B 76 VAL B 78 -1 O VAL B 78 N LEU B 71
SHEET 1 AA5 9 LYS B 4 PRO B 5 0
SHEET 2 AA5 9 GLN B 17 VAL B 18 -1 O VAL B 18 N LYS B 4
SHEET 3 AA5 9 VAL B 24 ILE B 28 -1 O ARG B 25 N GLN B 17
SHEET 4 AA5 9 TRP B 55 ASP B 58 -1 O TRP B 55 N ILE B 28
SHEET 5 AA5 9 VAL B 43 GLN B 49 -1 N THR B 48 O ILE B 56
SHEET 6 AA5 9 VAL B 36 ILE B 40 -1 N LEU B 38 O TYR B 45
SHEET 7 AA5 9 GLY B 65 ILE B 73 -1 O GLN B 70 N ASP B 39
SHEET 8 AA5 9 ARG B 91 VAL B 98 -1 O VAL B 98 N GLY B 65
SHEET 9 AA5 9 TYR B 85 GLY B 88 -1 N GLY B 88 O ARG B 91
CISPEP 1 TYR A 15 PRO A 16 0 8.13
CISPEP 2 TYR B 15 PRO B 16 0 5.35
CRYST1 66.595 99.816 114.429 90.00 90.00 90.00 P 21 21 21 4
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 0.015016 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010018 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008739 0.00000
TER 5390 GLN A 343
TER 10735 LEU B 344
MASTER 338 0 0 21 50 0 0 6 6324 2 0 54
END |