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HEADER HYDROLASE 13-SEP-12 4H35
TITLE FERULOYL ESTERASE DOMAIN OF XYNY FROM CLOSTRIDIUM THERMOCELLUM BEFORE
TITLE 2 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 FRAGMENT: FERULOYL ESTERASE DOMAIN (UNP RESIDUES 792-1077);
COMPND 5 SYNONYM: XYNY, XYLANASE Y, 1,4-BETA-D-XYLAN XYLANOHYDROLASE Y, XYLY;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1515;
SOURCE 4 GENE: XYNY;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA AND BETA PROTEINS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.B.PEREIRA,D.DE SANCTIS
REVDAT 1 12-DEC-12 4H35 0
JRNL AUTH P.J.PEREIRA,A.ROYANT,S.PANJIKAR,D.D.SANCTIS
JRNL TITL IN-HOUSE UV RADIATION DAMAGE INDUCED PHASING OF
JRNL TITL 2 SELENOMETHIONINE-LABELED PROTEIN STRUCTURES.
JRNL REF J.STRUCT.BIOL. 2012
JRNL REFN ESSN 1095-8657
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: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 63616
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 3257
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 0.99 3803 203 0.1687 0.1932
REMARK 3 2 5.7890 - 4.6409 0.99 3843 178 0.1406 0.1282
REMARK 3 3 4.6409 - 4.0680 0.99 3837 199 0.1242 0.1400
REMARK 3 4 4.0680 - 3.7024 1.00 3846 227 0.1367 0.1446
REMARK 3 5 3.7024 - 3.4405 1.00 3865 177 0.1489 0.1804
REMARK 3 6 3.4405 - 3.2399 1.00 3862 207 0.1612 0.1708
REMARK 3 7 3.2399 - 3.0791 1.00 3839 210 0.1594 0.1821
REMARK 3 8 3.0791 - 2.9462 1.00 3859 190 0.1577 0.1626
REMARK 3 9 2.9462 - 2.8336 1.00 3822 237 0.1630 0.1842
REMARK 3 10 2.8336 - 2.7364 1.00 3866 230 0.1594 0.1768
REMARK 3 11 2.7364 - 2.6513 1.00 3844 209 0.1549 0.1895
REMARK 3 12 2.6513 - 2.5760 1.00 3818 238 0.1555 0.1792
REMARK 3 13 2.5760 - 2.5085 1.00 3847 202 0.1509 0.1811
REMARK 3 14 2.5085 - 2.4475 1.00 3886 201 0.1492 0.1598
REMARK 3 15 2.4475 - 2.3921 1.00 3837 217 0.1448 0.1727
REMARK 3 16 2.3921 - 2.3414 1.00 3824 243 0.1455 0.1581
REMARK 3 17 2.3414 - 2.2948 1.00 3852 188 0.1558 0.1643
REMARK 3 18 2.2948 - 2.2516 1.00 3862 185 0.1499 0.1669
REMARK 3 19 2.2516 - 2.2115 1.00 3862 193 0.1511 0.1970
REMARK 3 20 2.2115 - 2.1742 1.00 3818 189 0.1535 0.1832
REMARK 3 21 2.1742 - 2.1392 1.00 3909 217 0.1568 0.1709
REMARK 3 22 2.1392 - 2.1064 1.00 3798 229 0.1598 0.1829
REMARK 3 23 2.1064 - 2.0755 1.00 3880 197 0.1638 0.2037
REMARK 3 24 2.0755 - 2.0463 1.00 3815 205 0.1873 0.2165
REMARK 3 25 2.0463 - 2.0187 1.00 3858 216 0.1832 0.2408
REMARK 3 26 2.0187 - 1.9926 1.00 3849 210 0.1841 0.1942
REMARK 3 27 1.9926 - 1.9677 1.00 3867 200 0.1822 0.1985
REMARK 3 28 1.9677 - 1.9441 1.00 3837 206 0.1917 0.2338
REMARK 3 29 1.9441 - 1.9215 1.00 3819 199 0.2000 0.2374
REMARK 3 30 1.9215 - 1.9000 0.96 3754 211 0.2211 0.2236
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.20
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 : 0.008 4754
REMARK 3 ANGLE : 1.107 6476
REMARK 3 CHIRALITY : 0.080 640
REMARK 3 PLANARITY : 0.005 850
REMARK 3 DIHEDRAL : 13.266 1672
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 4H35 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : OTHER
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 : OXFORD ONYX CCD
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) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : 0.11500
REMARK 200 FOR THE DATA SET : 13.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: UV-RIP
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, PH 7.5, 1 M SODIUM
REMARK 280 ACETATE, 50 MM CADMIUM ACETATE, 5% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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 HD1 HIS A 1081 O HOH A 1320 1.40
REMARK 500 O HOH B 1252 O HOH B 1319 1.99
REMARK 500 OH TYR B 819 OE2 GLU B 892 1.99
REMARK 500 O HOH B 1307 O HOH B 1324 2.00
REMARK 500 OH TYR A 819 OE2 GLU A 892 2.03
REMARK 500 O LEU B 1034 O HOH B 1317 2.19
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 1302 O HOH B 1324 2574 2.06
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 -47.68 -133.23
REMARK 500 THR A 931 -166.04 -103.18
REMARK 500 SEP A 954 -115.36 63.44
REMARK 500 TRP A 982 42.72 -92.06
REMARK 500 THR A1040 148.56 172.49
REMARK 500 ASN A1047 18.95 -149.84
REMARK 500 VAL B 878 -53.08 -131.06
REMARK 500 THR B 931 -166.39 -105.84
REMARK 500 SEP B 954 -115.08 63.98
REMARK 500 THR B1040 150.49 175.95
REMARK 500 ASN B1047 16.44 -151.03
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 B1103 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1084 NE2
REMARK 620 2 HIS B1082 NE2 106.9
REMARK 620 3 HOH B1318 O 106.5 101.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1104 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1084 NE2
REMARK 620 2 HIS A1082 NE2 100.6
REMARK 620 3 HOH A1319 O 97.7 103.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1102 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 947 NE2
REMARK 620 2 HIS A1080 NE2 90.7
REMARK 620 3 HOH A1229 O 92.3 106.9
REMARK 620 4 HOH A1349 O 90.7 92.8 160.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1102 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 894 OE2
REMARK 620 2 HIS B1085 NE2 91.0
REMARK 620 3 GLU B1079 OE1 126.2 142.8
REMARK 620 4 HIS B1083 ND1 83.8 95.9 89.4
REMARK 620 5 HIS B1076 ND1 87.1 85.8 94.7 170.8
REMARK 620 6 GLU B1079 OE2 174.0 90.4 52.7 90.2 98.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1104 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1080 NE2
REMARK 620 2 HIS B 947 NE2 86.2
REMARK 620 3 HOH B1319 O 158.8 113.1
REMARK 620 4 HOH B1241 O 102.9 95.6 84.7
REMARK 620 5 HOH B1323 O 91.4 85.8 81.6 165.7
REMARK 620 6 HOH B1345 O 88.4 174.4 72.5 84.1 95.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1103 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1079 OE1
REMARK 620 2 GLU A 894 OE2 121.6
REMARK 620 3 HIS A1085 NE2 145.2 93.2
REMARK 620 4 HIS A1083 ND1 86.9 85.8 95.7
REMARK 620 5 HIS A1076 ND1 95.5 86.5 86.7 172.1
REMARK 620 6 GLU A1079 OE2 53.2 172.0 92.2 87.7 99.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1101 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 886 ND1
REMARK 620 2 CYS A 823 SG 95.7
REMARK 620 3 HOH A1209 O 89.5 126.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B1101 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 886 ND1
REMARK 620 2 CYS B 823 SG 96.7
REMARK 620 3 HOH B1224 O 89.9 125.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GKK RELATED DB: PDB
DBREF 4H35 A 792 1077 UNP P51584 XYNY_CLOTM 792 1077
DBREF 4H35 B 792 1077 UNP P51584 XYNY_CLOTM 792 1077
SEQADV 4H35 MSE A 789 UNP P51584 EXPRESSION TAG
SEQADV 4H35 ALA A 790 UNP P51584 EXPRESSION TAG
SEQADV 4H35 SER A 791 UNP P51584 EXPRESSION TAG
SEQADV 4H35 GLU A 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 4H35 ASP A 1018 UNP P51584 HIS 1018 CONFLICT
SEQADV 4H35 LEU A 1078 UNP P51584 EXPRESSION TAG
SEQADV 4H35 GLU A 1079 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS A 1080 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS A 1081 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS A 1082 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS A 1083 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS A 1084 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS A 1085 UNP P51584 EXPRESSION TAG
SEQADV 4H35 MSE B 789 UNP P51584 EXPRESSION TAG
SEQADV 4H35 ALA B 790 UNP P51584 EXPRESSION TAG
SEQADV 4H35 SER B 791 UNP P51584 EXPRESSION TAG
SEQADV 4H35 GLU B 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 4H35 ASP B 1018 UNP P51584 HIS 1018 CONFLICT
SEQADV 4H35 LEU B 1078 UNP P51584 EXPRESSION TAG
SEQADV 4H35 GLU B 1079 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS B 1080 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS B 1081 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS B 1082 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS B 1083 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS B 1084 UNP P51584 EXPRESSION TAG
SEQADV 4H35 HIS B 1085 UNP P51584 EXPRESSION TAG
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 4H35 MSE A 863 MET SELENOMETHIONINE
MODRES 4H35 MSE A 889 MET SELENOMETHIONINE
MODRES 4H35 MSE A 946 MET SELENOMETHIONINE
MODRES 4H35 SEP A 954 SER PHOSPHOSERINE
MODRES 4H35 MSE A 955 MET SELENOMETHIONINE
MODRES 4H35 MSE A 964 MET SELENOMETHIONINE
MODRES 4H35 MSE A 975 MET SELENOMETHIONINE
MODRES 4H35 MSE A 1024 MET SELENOMETHIONINE
MODRES 4H35 MSE A 1031 MET SELENOMETHIONINE
MODRES 4H35 MSE B 863 MET SELENOMETHIONINE
MODRES 4H35 MSE B 889 MET SELENOMETHIONINE
MODRES 4H35 MSE B 946 MET SELENOMETHIONINE
MODRES 4H35 SEP B 954 SER PHOSPHOSERINE
MODRES 4H35 MSE B 955 MET SELENOMETHIONINE
MODRES 4H35 MSE B 964 MET SELENOMETHIONINE
MODRES 4H35 MSE B 975 MET SELENOMETHIONINE
MODRES 4H35 MSE B 1024 MET SELENOMETHIONINE
MODRES 4H35 MSE B 1031 MET SELENOMETHIONINE
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 A1101 1
HET CD A1102 1
HET CD A1103 1
HET CD A1104 1
HET CD B1101 1
HET CD B1102 1
HET CD B1103 1
HET CD B1104 1
HETNAM MSE SELENOMETHIONINE
HETNAM SEP PHOSPHOSERINE
HETNAM CD CADMIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 CD 8(CD 2+)
FORMUL 11 HOH *315(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 LEU B 968 1 15
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 A 8 ARG A 828 GLY A 836 0
SHEET 2 A 8 GLY A 839 LEU A 847 -1 O LEU A 843 N GLU A 832
SHEET 3 A 8 LEU A 896 THR A 900 -1 O VAL A 898 N TYR A 846
SHEET 4 A 8 ASN A 858 MSE A 863 1 N LEU A 862 O VAL A 899
SHEET 5 A 8 ARG A 948 PHE A 953 1 O GLY A 951 N MSE A 863
SHEET 6 A 8 TYR A 973 LEU A 977 1 O LEU A 977 N GLY A 952
SHEET 7 A 8 PHE A1009 GLY A1015 1 O PHE A1011 N PHE A 974
SHEET 8 A 8 PHE A1048 ALA A1053 1 O LEU A1051 N ALA A1012
SHEET 1 B 8 ARG B 828 GLY B 836 0
SHEET 2 B 8 GLY B 839 LEU B 847 -1 O LEU B 847 N ARG B 828
SHEET 3 B 8 LEU B 896 THR B 900 -1 O VAL B 898 N TYR B 846
SHEET 4 B 8 ASN B 858 MSE B 863 1 N LEU B 862 O VAL B 899
SHEET 5 B 8 ARG B 948 PHE B 953 1 O GLY B 949 N TYR B 861
SHEET 6 B 8 TYR B 973 LEU B 977 1 O TYR B 973 N PHE B 950
SHEET 7 B 8 PHE B1009 GLU B1017 1 O PHE B1011 N PHE B 974
SHEET 8 B 8 PHE B1048 THR B1057 1 O TYR B1049 N ALA B1012
LINK C LEU A 862 N MSE A 863 1555 1555 1.33
LINK C MSE A 863 N HIS A 864 1555 1555 1.33
LINK C ILE A 888 N MSE A 889 1555 1555 1.33
LINK C MSE A 889 N ASN A 890 1555 1555 1.33
LINK C ARG A 945 N MSE A 946 1555 1555 1.33
LINK C MSE A 946 N HIS A 947 1555 1555 1.33
LINK C PHE A 953 N SEP A 954 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 1.34
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 C VAL A 963 N MSE A 964 1555 1555 1.33
LINK C MSE A 964 N VAL A 965 1555 1555 1.33
LINK C PHE A 974 N MSE A 975 1555 1555 1.33
LINK C MSE A 975 N PRO A 976 1555 1555 1.34
LINK C ASN A1023 N MSE A1024 1555 1555 1.33
LINK C MSE A1024 N ASN A1025 1555 1555 1.33
LINK C ALA A1030 N MSE A1031 1555 1555 1.33
LINK C MSE A1031 N LYS A1032 1555 1555 1.34
LINK C LEU B 862 N MSE B 863 1555 1555 1.33
LINK C MSE B 863 N HIS B 864 1555 1555 1.33
LINK C ILE B 888 N MSE B 889 1555 1555 1.33
LINK C MSE B 889 N ASN B 890 1555 1555 1.33
LINK C ARG B 945 N MSE B 946 1555 1555 1.33
LINK C MSE B 946 N HIS B 947 1555 1555 1.33
LINK C PHE B 953 N SEP B 954 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 C VAL B 963 N MSE B 964 1555 1555 1.33
LINK C MSE B 964 N VAL B 965 1555 1555 1.32
LINK C PHE B 974 N MSE B 975 1555 1555 1.33
LINK C MSE B 975 N PRO B 976 1555 1555 1.34
LINK C ASN B1023 N MSE B1024 1555 1555 1.33
LINK C MSE B1024 N ASN B1025 1555 1555 1.33
LINK C ALA B1030 N MSE B1031 1555 1555 1.33
LINK C MSE B1031 N LYS B1032 1555 1555 1.33
LINK NE2 HIS B1084 CD CD B1103 1555 1555 2.37
LINK NE2 HIS A1084 CD CD A1104 1555 1555 2.37
LINK NE2 HIS A 947 CD CD A1102 1555 1555 2.41
LINK OE2 GLU B 894 CD CD B1102 1555 1555 2.42
LINK NE2 HIS B1080 CD CD B1104 1555 1555 2.42
LINK OE1 GLU A1079 CD CD A1103 1555 1555 2.42
LINK OE2 GLU A 894 CD CD A1103 1555 1555 2.42
LINK NE2 HIS A1082 CD CD A1104 1555 1555 2.43
LINK NE2 HIS B1085 CD CD B1102 1555 1555 2.44
LINK NE2 HIS A1085 CD CD A1103 1555 1555 2.45
LINK NE2 HIS B 947 CD CD B1104 1555 1555 2.45
LINK NE2 HIS A1080 CD CD A1102 1555 1555 2.46
LINK OE1 GLU B1079 CD CD B1102 1555 1555 2.46
LINK NE2 HIS B1082 CD CD B1103 1555 1555 2.46
LINK ND1 HIS B1083 CD CD B1102 1555 1555 2.47
LINK ND1 HIS A 886 CD CD A1101 1555 1555 2.50
LINK ND1 HIS B1076 CD CD B1102 1555 1555 2.50
LINK ND1 HIS A1083 CD CD A1103 1555 1555 2.51
LINK ND1 HIS A1076 CD CD A1103 1555 1555 2.51
LINK OE2 GLU A1079 CD CD A1103 1555 1555 2.52
LINK OE2 GLU B1079 CD CD B1102 1555 1555 2.52
LINK ND1 HIS B 886 CD CD B1101 1555 1555 2.53
LINK SG CYS A 823 CD CD A1101 1555 1555 2.62
LINK SG CYS B 823 CD CD B1101 1555 1555 2.62
LINK CD CD A1101 O HOH A1209 1555 1555 2.48
LINK CD CD B1101 O HOH B1224 1555 1555 2.49
LINK CD CD A1104 O HOH A1319 1555 1555 2.51
LINK CD CD B1104 O HOH B1319 1555 1555 2.53
LINK CD CD A1102 O HOH A1229 1555 1555 2.53
LINK CD CD B1103 O HOH B1318 1555 1555 2.54
LINK CD CD B1104 O HOH B1241 1555 1555 2.55
LINK CD CD B1104 O HOH B1323 1555 1555 2.56
LINK CD CD A1102 O HOH A1349 1555 1555 2.59
LINK CD CD B1104 O HOH B1345 1555 1555 2.59
SITE 1 AC1 5 CYS A 823 HIS A 886 MSE A 889 HOH A1209
SITE 2 AC1 5 GLU B1017
SITE 1 AC2 4 HIS A 947 HIS A1080 HOH A1229 HOH A1349
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 A1319 GLU B1007
SITE 1 AC5 5 GLU A1017 CYS B 823 HIS B 886 MSE B 889
SITE 2 AC5 5 HOH B1224
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 B1318
SITE 1 AC8 6 HIS B 947 HIS B1080 HOH B1241 HOH B1319
SITE 2 AC8 6 HOH B1323 HOH B1345
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
TER 4427 HIS A1085
TER 8848 HIS B1085
MASTER 440 0 26 22 16 0 13 6 4903 2 392 46
END |