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HEADER HYDROLASE 14-SEP-12 4BAG
TITLE FERULOYL ESTERASE DOMAIN OF XYNY FROM CLOSTRIDIUM
TITLE 2 THERMOCELLUM AFTER EXPOSURE TO 266NM UV LASER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: XYLANASE Y, 1,4-BETA-D-XYLAN XYLANOHYDROLASE Y, XYLY;
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1515;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.B.PEREIRA,D.DE SANCTIS
REVDAT 1 17-APR-13 4BAG 0
JRNL AUTH P.J.B.PEREIRA,A.ROYANT,S.PANJIKAR,D.DE SANCTIS
JRNL TITL IN-HOUSE UV RADIATION-DAMAGE-INDUCED PHASING OF
JRNL TITL 2 SELENOMETHIONINE-LABELED PROTEIN STRUCTURES.
JRNL REF J.STRUCT.BIOL. V. 181 89 2013
JRNL REFN ISSN 1047-8477
JRNL PMID 23178456
JRNL DOI 10.1016/J.JSB.2012.11.003
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.900
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.860
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.08
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.42
REMARK 3 NUMBER OF REFLECTIONS : 63588
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1682
REMARK 3 R VALUE (WORKING SET) : 0.1671
REMARK 3 FREE R VALUE : 0.1874
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 6191
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 14.8609 - 5.7890 0.98 3746 227 0.1707 0.2080
REMARK 3 2 5.7890 - 4.6409 0.98 3785 198 0.1525 0.1406
REMARK 3 3 4.6409 - 4.0680 0.99 3778 238 0.1331 0.1242
REMARK 3 4 4.0680 - 3.7024 1.00 3890 172 0.1396 0.1548
REMARK 3 5 3.7024 - 3.4405 1.00 3823 220 0.1565 0.1620
REMARK 3 6 3.4405 - 3.2399 1.00 3849 220 0.1668 0.1864
REMARK 3 7 3.2399 - 3.0791 1.00 3845 203 0.1677 0.1850
REMARK 3 8 3.0791 - 2.9462 1.00 3824 225 0.1638 0.1858
REMARK 3 9 2.9462 - 2.8336 1.00 3842 214 0.1672 0.1976
REMARK 3 10 2.8336 - 2.7364 1.00 3870 227 0.1672 0.2111
REMARK 3 11 2.7364 - 2.6513 1.00 3855 195 0.1639 0.1799
REMARK 3 12 2.6513 - 2.5760 1.00 3832 224 0.1611 0.1844
REMARK 3 13 2.5760 - 2.5085 1.00 3812 239 0.1546 0.1585
REMARK 3 14 2.5085 - 2.4475 1.00 3869 218 0.1529 0.1681
REMARK 3 15 2.4475 - 2.3921 1.00 3855 197 0.1511 0.1648
REMARK 3 16 2.3921 - 2.3414 1.00 3850 221 0.1477 0.2005
REMARK 3 17 2.3414 - 2.2948 1.00 3843 201 0.1628 0.2009
REMARK 3 18 2.2948 - 2.2516 1.00 3844 205 0.1602 0.1729
REMARK 3 19 2.2516 - 2.2115 1.00 3828 222 0.1625 0.2052
REMARK 3 20 2.2115 - 2.1742 1.00 3812 192 0.1683 0.2287
REMARK 3 21 2.1742 - 2.1392 1.00 3931 186 0.1719 0.2295
REMARK 3 22 2.1392 - 2.1064 1.00 3833 190 0.1774 0.2267
REMARK 3 23 2.1064 - 2.0755 0.99 3865 199 0.1778 0.2133
REMARK 3 24 2.0755 - 2.0463 1.00 3837 177 0.1959 0.2077
REMARK 3 25 2.0463 - 2.0187 1.00 3864 210 0.1983 0.2234
REMARK 3 26 2.0187 - 1.9926 1.00 3839 216 0.2010 0.2309
REMARK 3 27 1.9926 - 1.9677 0.99 3866 189 0.2058 0.2375
REMARK 3 28 1.9677 - 1.9441 0.99 3839 189 0.2130 0.2275
REMARK 3 29 1.9441 - 1.9215 1.00 3819 197 0.2253 0.2692
REMARK 3 30 1.9215 - 1.9000 0.93 3658 180 0.2442 0.2716
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 : 0.50
REMARK 3 B_SOL : 7.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.13
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.6
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 : 0.008 4768
REMARK 3 ANGLE : 1.113 6495
REMARK 3 CHIRALITY : 0.082 641
REMARK 3 PLANARITY : 0.005 853
REMARK 3 DIHEDRAL : 13.248 1678
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-12.
REMARK 100 THE PDBE ID CODE IS EBI-54092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION GEMINI PX
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : AGILENT
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63630
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.5
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.5
REMARK 200 R MERGE FOR SHELL (I) : 0.36
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES PH 7.5 100MM,
REMARK 280 NA ACETATE 1M, CD ACETATE 50 MM, GLYCEROL 5%
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 32.68500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.43000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.43000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.68500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 MSE A 789
REMARK 465 ALA A 790
REMARK 465 SER A 791
REMARK 465 ASP A 792
REMARK 465 LYS A 793
REMARK 465 PHE A 794
REMARK 465 PRO A 795
REMARK 465 VAL A 796
REMARK 465 ALA A 797
REMARK 465 GLU A 798
REMARK 465 ASN A 799
REMARK 465 PRO A 800
REMARK 465 SER A 801
REMARK 465 SER A 802
REMARK 465 MSE B 789
REMARK 465 ALA B 790
REMARK 465 SER B 791
REMARK 465 ASP B 792
REMARK 465 LYS B 793
REMARK 465 PHE B 794
REMARK 465 PRO B 795
REMARK 465 VAL B 796
REMARK 465 ALA B 797
REMARK 465 GLU B 798
REMARK 465 ASN B 799
REMARK 465 PRO B 800
REMARK 465 SER B 801
REMARK 465 SER B 802
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 OH TYR A 819 OE2 GLU A 892 2.04
REMARK 500 O GLU A 926 O HOH A 3096 2.20
REMARK 500 O LEU A 1034 O HOH A 3144 2.15
REMARK 500 OH TYR B 819 OE2 GLU B 892 2.00
REMARK 500 O LEU B 1034 O HOH B 3118 2.19
REMARK 500 HE2 HIS B 1081 O HOH B 3142 1.49
REMARK 500 O HOH A 3135 O HOH A 3137 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS B1083 CB - CG - ND1 ANGL. DEV. = 9.6 DEGREES
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 VAL A 878 -50.04 -131.21
REMARK 500 THR A 931 -166.77 -104.80
REMARK 500 SEP A 954 -112.68 62.55
REMARK 500 TRP A 982 49.98 -95.67
REMARK 500 THR A1040 147.79 172.25
REMARK 500 ASN A1047 17.85 -148.94
REMARK 500 VAL B 878 -53.17 -129.31
REMARK 500 THR B 931 -166.51 -103.90
REMARK 500 SEP B 954 -117.31 63.88
REMARK 500 THR B1040 150.07 176.84
REMARK 500 ASN B1047 16.39 -147.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2086 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 823 SG
REMARK 620 2 HIS A 886 ND1 95.6
REMARK 620 3 HOH A3074 O 128.0 90.3
REMARK 620 4 GLU B1017 OE1 110.5 90.4 121.0
REMARK 620 5 GLU B1017 OE2 155.1 100.9 70.8 51.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2087 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A3109 O
REMARK 620 2 HIS A1080 NE2 107.0
REMARK 620 3 HIS A 947 NE2 92.8 92.7
REMARK 620 4 HOH A3112 O 153.8 99.0 89.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2088 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 894 OE1
REMARK 620 2 GLU A1079 OE1 76.4
REMARK 620 3 HIS A1076 ND1 92.0 94.7
REMARK 620 4 GLU A 894 OE2 44.4 120.8 87.7
REMARK 620 5 HIS A1083 ND1 81.5 87.2 172.7 85.2
REMARK 620 6 GLU A1079 OE2 128.7 52.8 98.2 171.4 88.6
REMARK 620 7 HIS A1085 NE2 137.8 145.8 85.1 93.4 97.2 93.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2089 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1082 NE2
REMARK 620 2 HIS A1084 NE2 103.1
REMARK 620 3 GLU B1007 OE1 150.9 93.0
REMARK 620 4 GLU B1007 OE2 97.5 114.7 53.6
REMARK 620 5 HOH A3173 O 104.0 98.5 97.2 134.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2086 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1017 OE1
REMARK 620 2 GLU A1017 OE2 51.4
REMARK 620 3 CYS B 823 SG 108.5 152.9
REMARK 620 4 HIS B 886 ND1 89.3 102.2 94.5
REMARK 620 5 HOH B3071 O 123.0 73.2 128.3 90.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2087 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1083 ND1
REMARK 620 2 GLU B1079 OE1 86.9
REMARK 620 3 GLU B1079 OE2 90.1 52.7
REMARK 620 4 GLU B 894 OE2 83.1 126.3 173.2
REMARK 620 5 HIS B1085 NE2 98.2 143.4 90.9 90.3
REMARK 620 6 GLU B 894 OE1 80.6 79.8 132.1 46.5 136.7
REMARK 620 7 HIS B1076 ND1 169.7 95.2 99.2 87.5 86.1 89.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2088 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B3144 O
REMARK 620 2 GLU A1007 OE1 95.9
REMARK 620 3 GLU A1007 OE2 129.0 52.6
REMARK 620 4 HIS B1082 NE2 100.5 152.1 99.8
REMARK 620 5 HIS B1084 NE2 101.1 91.4 116.5 107.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2089 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1080 NE2
REMARK 620 2 HOH B3095 O 102.8
REMARK 620 3 HOH B3140 O 87.7 83.2
REMARK 620 4 HIS B 947 NE2 87.6 92.5 172.8
REMARK 620 5 HOH B3098 O 96.6 160.6 96.5 89.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2087
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2089
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2087
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2089
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2090
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DYO RELATED DB: PDB
REMARK 900 XYLAN-BINDING DOMAIN FROM CBM 22, FORMALLY X6B DOMAIN
REMARK 900 RELATED ID: 1GKK RELATED DB: PDB
REMARK 900 FERULOYL ESTERASE DOMAIN OF XYNY FROM CLOSTRIDIUM
REMARK 900 THERMOCELLUM
REMARK 900 RELATED ID: 1GKL RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH FERULIC ACID
REMARK 900 RELATED ID: 1H6X RELATED DB: PDB
REMARK 900 THE ROLE OF CONSERVED AMINO ACIDS IN THE CLEFT OF
REMARK 900 THE C-TERMINAL FAMILY 22 CARBOHYDRATE BINDING MODULE
REMARK 900 OF CLOSTRIDIUM THERMOCELLUM XYN10B IN LIGAND BINDING
REMARK 900 RELATED ID: 1H6Y RELATED DB: PDB
REMARK 900 THE ROLE OF CONSERVED AMINO ACIDS IN THE CLEFT OF
REMARK 900 THE C-TERMINAL FAMILY 22 CARBOHYDRATE BINDING MODULE
REMARK 900 OF CLOSTRIDIUM THERMOCELLUM XYN10B IN LIGAND BINDING
REMARK 900 RELATED ID: 1OHZ RELATED DB: PDB
REMARK 900 COHESIN-DOCKERIN COMPLEX FROM THE CELLULOSOME OF
REMARK 900 CLOSTRIDIUM THERMOCELLUM
REMARK 900 RELATED ID: 1WB4 RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH SINAPINATE
REMARK 900 RELATED ID: 1WB5 RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH SYRINGATE
REMARK 900 RELATED ID: 1WB6 RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH VANILLATE
REMARK 900 RELATED ID: 2CCL RELATED DB: PDB
REMARK 900 THE S45A, T46A MUTANT OF THE TYPE I COHESIN-DOCKERIN
REMARK 900 COMPLEX FROM THE CELLULOSOME OF CLOSTRIDIUM THERMOCELLUM
REMARK 900 RELATED ID: 2W5F RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTALLOGRAPHIC STRUCTURE OF THE
REMARK 900 CLOSTRIDIUM THERMOCELLUM N-TERMINAL ENDO-1,4-BETA-D-
REMARK 900 XYLANASE 10B (XYN10B) CBM22-1-GH10 MODULES COMPLEXED
REMARK 900 WITH XYLOHEXAOSE
REMARK 900 RELATED ID: 2WYS RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTALLOGRAPHIC STRUCTURE OF THE
REMARK 900 CLOSTRIDIUM THERMOCELLUM N-TERMINAL ENDO-1,4-BETA-D-
REMARK 900 XYLANASE 10B (XYN10B) CBM22-1-GH10 MODULES COMPLEXED
REMARK 900 WITH XYLOHEXAOSE
REMARK 900 RELATED ID: 2WZE RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTALLOGRAPHIC STRUCTURE OF THE
REMARK 900 CLOSTRIDIUM THERMOCELLUM N-TERMINAL ENDO-1,4-BETA-D-
REMARK 900 XYLANASE 10B (XYN10B) CBM22-1-GH10 MODULES COMPLEXED
REMARK 900 WITH XYLOHEXAOSE
DBREF 4BAG A 792 1077 UNP P51584 XYNY_CLOTM 792 1077
DBREF 4BAG B 792 1077 UNP P51584 XYNY_CLOTM 792 1077
SEQADV 4BAG MSE A 789 UNP P51584 EXPRESSION TAG
SEQADV 4BAG ALA A 790 UNP P51584 EXPRESSION TAG
SEQADV 4BAG SER A 791 UNP P51584 EXPRESSION TAG
SEQADV 4BAG LEU A 1078 UNP P51584 EXPRESSION TAG
SEQADV 4BAG GLU A 1079 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS A 1080 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS A 1081 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS A 1082 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS A 1083 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS A 1084 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS A 1085 UNP P51584 EXPRESSION TAG
SEQADV 4BAG GLU A 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 4BAG ASP A 1018 UNP P51584 HIS 1018 CONFLICT
SEQADV 4BAG MSE B 789 UNP P51584 EXPRESSION TAG
SEQADV 4BAG ALA B 790 UNP P51584 EXPRESSION TAG
SEQADV 4BAG SER B 791 UNP P51584 EXPRESSION TAG
SEQADV 4BAG LEU B 1078 UNP P51584 EXPRESSION TAG
SEQADV 4BAG GLU B 1079 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS B 1080 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS B 1081 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS B 1082 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS B 1083 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS B 1084 UNP P51584 EXPRESSION TAG
SEQADV 4BAG HIS B 1085 UNP P51584 EXPRESSION TAG
SEQADV 4BAG GLU B 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 4BAG ASP B 1018 UNP P51584 HIS 1018 CONFLICT
SEQRES 1 A 297 MSE ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 A 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 A 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 A 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 A 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 A 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY
SEQRES 7 A 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 A 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU
SEQRES 9 A 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 A 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 A 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 A 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 A 297 ARG MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 A 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 A 297 VAL ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 A 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 A 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 A 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 A 297 ASN MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO
SEQRES 20 A 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 A 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 A 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 A 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 297 MSE ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 B 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 B 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 B 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 B 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 B 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY
SEQRES 7 B 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 B 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU
SEQRES 9 B 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 B 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 B 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 B 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 B 297 ARG MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 B 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 B 297 VAL ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 B 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 B 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 B 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 B 297 ASN MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO
SEQRES 20 B 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 B 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 B 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 B 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 4BAG MSE A 863 MET SELENOMETHIONINE
MODRES 4BAG MSE A 889 MET SELENOMETHIONINE
MODRES 4BAG MSE A 946 MET SELENOMETHIONINE
MODRES 4BAG MSE A 955 MET SELENOMETHIONINE
MODRES 4BAG MSE A 964 MET SELENOMETHIONINE
MODRES 4BAG MSE A 975 MET SELENOMETHIONINE
MODRES 4BAG MSE A 1024 MET SELENOMETHIONINE
MODRES 4BAG MSE A 1031 MET SELENOMETHIONINE
MODRES 4BAG MSE B 863 MET SELENOMETHIONINE
MODRES 4BAG MSE B 889 MET SELENOMETHIONINE
MODRES 4BAG MSE B 946 MET SELENOMETHIONINE
MODRES 4BAG MSE B 955 MET SELENOMETHIONINE
MODRES 4BAG MSE B 964 MET SELENOMETHIONINE
MODRES 4BAG MSE B 975 MET SELENOMETHIONINE
MODRES 4BAG MSE B 1024 MET SELENOMETHIONINE
MODRES 4BAG MSE B 1031 MET SELENOMETHIONINE
MODRES 4BAG SEP A 954 SER PHOSPHOSERINE
MODRES 4BAG SEP B 954 SER PHOSPHOSERINE
HET MSE A 863 17
HET MSE A 889 17
HET MSE A 946 17
HET SEP A 954 13
HET MSE A 955 34
HET MSE A 964 17
HET MSE A 975 17
HET MSE A1024 17
HET MSE A1031 17
HET MSE B 863 17
HET MSE B 889 17
HET MSE B 946 17
HET SEP B 954 13
HET MSE B 955 17
HET MSE B 964 17
HET MSE B 975 17
HET MSE B1024 17
HET MSE B1031 17
HET CD A2086 1
HET CD A2087 1
HET CD A2088 1
HET CD A2089 1
HET CD B2086 1
HET CD B2087 1
HET CD B2088 1
HET CD B2089 1
HET GOL A2090 14
HETNAM SEP PHOSPHOSERINE
HETNAM CD CADMIUM ION
HETNAM GOL GLYCEROL
HETNAM MSE SELENOMETHIONINE
HETSYN SEP PHOSPHONOSERINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 MSE 16(C5 H11 N O2 SE)
FORMUL 3 SEP 2(C3 H8 N O6 P)
FORMUL 4 CD 8(CD 2+)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *318(H2 O)
HELIX 1 1 PRO A 816 ASN A 821 5 6
HELIX 2 2 LYS A 879 ASN A 890 1 12
HELIX 3 3 ASN A 912 ASN A 920 1 9
HELIX 4 4 ASN A 920 TYR A 929 1 10
HELIX 5 5 THR A 937 ALA A 943 1 7
HELIX 6 6 SER A 944 MSE A 946 5 3
HELIX 7 7 SEP A 954 LEU A 968 1 15
HELIX 8 8 SER A 986 GLY A 1002 1 17
HELIX 9 9 ALA A 1020 ALA A 1033 1 14
HELIX 10 10 TRP A 1059 LEU A 1071 1 13
HELIX 11 11 PRO A 1072 PHE A 1074 5 3
HELIX 12 12 PRO B 816 ASN B 821 5 6
HELIX 13 13 LYS B 879 ASN B 890 1 12
HELIX 14 14 ASN B 912 ASN B 920 1 9
HELIX 15 15 ASN B 920 TYR B 929 1 10
HELIX 16 16 THR B 937 ALA B 943 1 7
HELIX 17 17 SER B 944 MSE B 946 5 3
HELIX 18 18 SEP B 954 CYS B 967 1 14
HELIX 19 19 SER B 986 GLY B 1002 1 17
HELIX 20 20 ILE B 1019 ALA B 1033 1 15
HELIX 21 21 TRP B 1059 LEU B 1071 1 13
HELIX 22 22 PRO B 1072 PHE B 1074 5 3
SHEET 1 AA 8 ARG A 828 GLY A 836 0
SHEET 2 AA 8 GLY A 839 LEU A 847 -1 O GLY A 839 N GLY A 836
SHEET 3 AA 8 LEU A 896 THR A 900 -1 O VAL A 898 N TYR A 846
SHEET 4 AA 8 ASN A 858 MSE A 863 1 O ASN A 858 N ILE A 897
SHEET 5 AA 8 ARG A 948 PHE A 953 1 O GLY A 949 N TYR A 861
SHEET 6 AA 8 TYR A 973 LEU A 977 1 O TYR A 973 N PHE A 950
SHEET 7 AA 8 PHE A1009 GLY A1015 1 O PHE A1009 N PHE A 974
SHEET 8 AA 8 PHE A1048 ALA A1053 1 O TYR A1049 N ALA A1012
SHEET 1 BA 8 ARG B 828 GLY B 836 0
SHEET 2 BA 8 GLY B 839 LEU B 847 -1 O GLY B 839 N GLY B 836
SHEET 3 BA 8 LEU B 896 THR B 900 -1 O VAL B 898 N TYR B 846
SHEET 4 BA 8 ASN B 858 MSE B 863 1 O ASN B 858 N ILE B 897
SHEET 5 BA 8 ARG B 948 PHE B 953 1 O GLY B 949 N TYR B 861
SHEET 6 BA 8 TYR B 973 LEU B 977 1 O TYR B 973 N PHE B 950
SHEET 7 BA 8 PHE B1009 GLY B1015 1 O PHE B1009 N PHE B 974
SHEET 8 BA 8 PHE B1048 ALA B1053 1 O TYR B1049 N ALA B1012
LINK N MSE A 863 C LEU A 862 1555 1555 1.33
LINK C MSE A 863 N HIS A 864 1555 1555 1.33
LINK N MSE A 889 C ILE A 888 1555 1555 1.33
LINK C MSE A 889 N ASN A 890 1555 1555 1.33
LINK N MSE A 946 C ARG A 945 1555 1555 1.33
LINK C MSE A 946 N HIS A 947 1555 1555 1.33
LINK N SEP A 954 C PHE A 953 1555 1555 1.33
LINK C SEP A 954 N AMSE A 955 1555 1555 1.33
LINK C SEP A 954 N BMSE A 955 1555 1555 1.33
LINK C AMSE A 955 N GLY A 956 1555 1555 1.33
LINK C BMSE A 955 N GLY A 956 1555 1555 1.33
LINK N MSE A 964 C VAL A 963 1555 1555 1.33
LINK C MSE A 964 N VAL A 965 1555 1555 1.33
LINK N MSE A 975 C PHE A 974 1555 1555 1.33
LINK C MSE A 975 N PRO A 976 1555 1555 1.34
LINK N MSE A1024 C ASN A1023 1555 1555 1.33
LINK C MSE A1024 N ASN A1025 1555 1555 1.33
LINK C MSE A1031 N LYS A1032 1555 1555 1.33
LINK N MSE A1031 C ALA A1030 1555 1555 1.33
LINK CD CD A2086 ND1 HIS A 886 1555 1555 2.54
LINK CD CD A2086 O HOH A3074 1555 1555 2.51
LINK CD CD A2086 OE1 GLU B1017 1555 2574 2.43
LINK CD CD A2086 SG CYS A 823 1555 1555 2.63
LINK CD CD A2086 OE2 GLU B1017 1555 2574 2.63
LINK CD CD A2087 O HOH A3112 1555 1555 2.59
LINK CD CD A2087 NE2 HIS A 947 1555 1555 2.40
LINK CD CD A2087 NE2 HIS A1080 1555 1555 2.52
LINK CD CD A2087 O HOH A3109 1555 1555 2.53
LINK CD CD A2088 OE1 GLU A 894 1555 1555 3.13
LINK CD CD A2088 OE2 GLU A 894 1555 1555 2.40
LINK CD CD A2088 ND1 HIS A1083 1555 1555 2.49
LINK CD CD A2088 NE2 HIS A1085 1555 1555 2.45
LINK CD CD A2088 OE2 GLU A1079 1555 1555 2.50
LINK CD CD A2088 ND1 HIS A1076 1555 1555 2.55
LINK CD CD A2088 OE1 GLU A1079 1555 1555 2.46
LINK CD CD A2089 OE2 GLU B1007 1555 1655 2.41
LINK CD CD A2089 O HOH A3173 1555 1555 2.49
LINK CD CD A2089 NE2 HIS A1084 1555 1555 2.38
LINK CD CD A2089 NE2 HIS A1082 1555 1555 2.44
LINK CD CD A2089 OE1 GLU B1007 1555 1655 2.50
LINK C MSE B 863 N HIS B 864 1555 1555 1.33
LINK N MSE B 863 C LEU B 862 1555 1555 1.34
LINK N MSE B 889 C ILE B 888 1555 1555 1.33
LINK C MSE B 889 N ASN B 890 1555 1555 1.33
LINK C MSE B 946 N HIS B 947 1555 1555 1.33
LINK N MSE B 946 C ARG B 945 1555 1555 1.33
LINK N SEP B 954 C PHE B 953 1555 1555 1.33
LINK C SEP B 954 N MSE B 955 1555 1555 1.33
LINK C MSE B 955 N GLY B 956 1555 1555 1.33
LINK N MSE B 964 C VAL B 963 1555 1555 1.33
LINK C MSE B 964 N VAL B 965 1555 1555 1.32
LINK C MSE B 975 N PRO B 976 1555 1555 1.34
LINK N MSE B 975 C PHE B 974 1555 1555 1.33
LINK N MSE B1024 C ASN B1023 1555 1555 1.33
LINK C MSE B1024 N ASN B1025 1555 1555 1.33
LINK N MSE B1031 C ALA B1030 1555 1555 1.33
LINK C MSE B1031 N LYS B1032 1555 1555 1.33
LINK CD CD B2086 O HOH B3071 1555 1555 2.47
LINK CD CD B2086 ND1 HIS B 886 1555 1555 2.55
LINK CD CD B2086 SG CYS B 823 1555 1555 2.64
LINK CD CD B2086 OE2 GLU A1017 1555 3545 2.60
LINK CD CD B2086 OE1 GLU A1017 1555 3545 2.46
LINK CD CD B2087 ND1 HIS B1076 1555 1555 2.53
LINK CD CD B2087 OE1 GLU B 894 1555 1555 2.97
LINK CD CD B2087 NE2 HIS B1085 1555 1555 2.46
LINK CD CD B2087 OE2 GLU B 894 1555 1555 2.43
LINK CD CD B2087 OE2 GLU B1079 1555 1555 2.54
LINK CD CD B2087 OE1 GLU B1079 1555 1555 2.44
LINK CD CD B2087 ND1 HIS B1083 1555 1555 2.54
LINK CD CD B2088 NE2 HIS B1084 1555 1555 2.39
LINK CD CD B2088 NE2 HIS B1082 1555 1555 2.48
LINK CD CD B2088 OE2 GLU A1007 1555 1455 2.41
LINK CD CD B2088 OE1 GLU A1007 1555 1455 2.55
LINK CD CD B2088 O HOH B3144 1555 1555 2.56
LINK CD CD B2089 O HOH B3098 1555 1555 2.65
LINK CD CD B2089 NE2 HIS B 947 1555 1555 2.42
LINK CD CD B2089 O HOH B3140 1555 1555 2.61
LINK CD CD B2089 O HOH B3095 1555 1555 2.57
LINK CD CD B2089 NE2 HIS B1080 1555 1555 2.45
SITE 1 AC1 5 CYS A 823 HIS A 886 MSE A 889 HOH A3074
SITE 2 AC1 5 GLU B1017
SITE 1 AC2 4 HIS A 947 HIS A1080 HOH A3109 HOH A3112
SITE 1 AC3 5 GLU A 894 HIS A1076 GLU A1079 HIS A1083
SITE 2 AC3 5 HIS A1085
SITE 1 AC4 4 HIS A1082 HIS A1084 HOH A3173 GLU B1007
SITE 1 AC5 5 GLU A1017 CYS B 823 HIS B 886 MSE B 889
SITE 2 AC5 5 HOH B3071
SITE 1 AC6 5 GLU B 894 HIS B1076 GLU B1079 HIS B1083
SITE 2 AC6 5 HIS B1085
SITE 1 AC7 4 GLU A1007 HIS B1082 HIS B1084 HOH B3144
SITE 1 AC8 5 HIS B 947 HIS B1080 HOH B3095 HOH B3098
SITE 2 AC8 5 HOH B3140
SITE 1 AC9 7 LYS A 928 GLU B 926 SER B 927 TYR B 929
SITE 2 AC9 7 SER B 930 HOH B3085 HOH B3090
CRYST1 65.370 108.400 112.860 90.00 90.00 90.00 P 21 21 21 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 0.015298 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008861 0.00000
MTRIX1 1 -0.999900 0.013540 0.002644 14.59970 1
MTRIX2 1 0.004003 0.101400 0.994800 70.67790 1
MTRIX3 1 0.013210 0.994800 -0.101400 -78.58170 1
TER 4442 HIS A1085
TER 8863 HIS B1085
MASTER 496 0 27 22 16 0 15 9 9201 2 407 46
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