HEADER TRANSFERASE 09-MAY-14 4PIO
TITLE ERGOTHIONEINE-BIOSYNTHETIC METHYLTRANSFERASE EGTD IN COMPLEX WITH N,N-
TITLE 2 DIMETHYLHISTIDINE AND SAH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE-SPECIFIC METHYLTRANSFERASE EGTD;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HISTIDINE-ALPHA-N-METHYLTRANSFERASE;
COMPND 5 EC: 2.1.1.44;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 1772;
SOURCE 4 STRAIN: ATCC 607;
SOURCE 5 GENE: EGTD, MSMEG_6247, MSMEI_6086;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19M
KEYWDS METHYLTRANSFERASE, ERGOTHIONEINE, HISTIDINE BETAINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VIT,F.P.SEEBECK,W.BLANKENFELDT
REVDAT 4 27-SEP-23 4PIO 1 REMARK LINK
REVDAT 3 22-NOV-17 4PIO 1 SOURCE REMARK
REVDAT 2 07-JAN-15 4PIO 1 JRNL
REVDAT 1 03-DEC-14 4PIO 0
JRNL AUTH A.VIT,L.MISSON,W.BLANKENFELDT,F.P.SEEBECK
JRNL TITL ERGOTHIONEINE BIOSYNTHETIC METHYLTRANSFERASE EGTD REVEALS
JRNL TITL 2 THE STRUCTURAL BASIS OF AROMATIC AMINO ACID BETAINE
JRNL TITL 3 BIOSYNTHESIS.
JRNL REF CHEMBIOCHEM V. 16 119 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 25404173
JRNL DOI 10.1002/CBIC.201402522
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.VIT,L.MISSON,W.BLANKENFELDT,F.P.SEEBECK
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
REMARK 1 TITL 2 ERGOTHIONEINE-BIOSYNTHETIC METHYLTRANSFERASE EGTD.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F 676 2014
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 24817736
REMARK 1 DOI 10.1107/S2053230X1400805X
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 87509
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 4356
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 50.0225 - 4.6794 0.99 2875 155 0.1590 0.1619
REMARK 3 2 4.6794 - 3.7146 1.00 2856 165 0.1153 0.1404
REMARK 3 3 3.7146 - 3.2451 1.00 2828 155 0.1227 0.1485
REMARK 3 4 3.2451 - 2.9485 1.00 2807 150 0.1295 0.1507
REMARK 3 5 2.9485 - 2.7371 1.00 2838 135 0.1404 0.1803
REMARK 3 6 2.7371 - 2.5758 1.00 2813 131 0.1355 0.1644
REMARK 3 7 2.5758 - 2.4468 1.00 2813 136 0.1322 0.1774
REMARK 3 8 2.4468 - 2.3403 1.00 2794 158 0.1275 0.1820
REMARK 3 9 2.3403 - 2.2502 0.99 2814 143 0.1248 0.1655
REMARK 3 10 2.2502 - 2.1725 1.00 2745 180 0.1292 0.1580
REMARK 3 11 2.1725 - 2.1046 0.99 2801 145 0.1318 0.1633
REMARK 3 12 2.1046 - 2.0444 0.99 2748 159 0.1360 0.1641
REMARK 3 13 2.0444 - 1.9906 0.99 2815 137 0.1472 0.1829
REMARK 3 14 1.9906 - 1.9421 0.99 2796 129 0.1526 0.2094
REMARK 3 15 1.9421 - 1.8979 0.99 2790 131 0.1521 0.1702
REMARK 3 16 1.8979 - 1.8575 0.99 2774 144 0.1586 0.1836
REMARK 3 17 1.8575 - 1.8204 0.99 2778 140 0.1543 0.1758
REMARK 3 18 1.8204 - 1.7860 0.99 2791 152 0.1636 0.2284
REMARK 3 19 1.7860 - 1.7541 0.99 2759 147 0.1659 0.2159
REMARK 3 20 1.7541 - 1.7244 0.99 2710 147 0.1728 0.2242
REMARK 3 21 1.7244 - 1.6965 0.99 2771 158 0.1807 0.2079
REMARK 3 22 1.6965 - 1.6704 0.98 2742 157 0.1866 0.2515
REMARK 3 23 1.6704 - 1.6459 0.98 2752 153 0.1952 0.2032
REMARK 3 24 1.6459 - 1.6227 0.98 2735 137 0.1915 0.2503
REMARK 3 25 1.6227 - 1.6008 0.98 2765 126 0.2071 0.2639
REMARK 3 26 1.6008 - 1.5800 0.98 2760 146 0.2136 0.2479
REMARK 3 27 1.5800 - 1.5602 0.98 2741 136 0.2126 0.2666
REMARK 3 28 1.5602 - 1.5414 0.98 2751 151 0.2167 0.2296
REMARK 3 29 1.5414 - 1.5235 0.98 2752 141 0.2252 0.2748
REMARK 3 30 1.5235 - 1.5064 0.87 2439 112 0.2407 0.2749
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.58
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 5116
REMARK 3 ANGLE : 1.278 6981
REMARK 3 CHIRALITY : 0.047 795
REMARK 3 PLANARITY : 0.007 918
REMARK 3 DIHEDRAL : 12.677 1892
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 4PIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201487.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XDS, SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87536
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.506
REMARK 200 RESOLUTION RANGE LOW (A) : 49.995
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.55100
REMARK 200 R SYM FOR SHELL (I) : 0.55100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4PIM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M TRIS
REMARK 280 -HCL, PH 8.5, 30% W/V PEG4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.75550
REMARK 290 SMTRY3 2 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 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 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LEU A 5
REMARK 465 ALA A 6
REMARK 465 ASN A 7
REMARK 465 TYR A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 SER A 13
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA A 14 N CA CB
REMARK 470 HIS A 151 CG ND1 CD2 CE1 NE2
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 217 HD1 HIS B 239 1.22
REMARK 500 HG1 THR A 304 HD1 HIS A 305 1.23
REMARK 500 HG1 THR B 304 HD1 HIS B 305 1.25
REMARK 500 O PRO B 131 O HOH B 501 1.93
REMARK 500 O HOH B 604 O HOH B 643 1.98
REMARK 500 O HOH B 682 O HOH B 832 1.99
REMARK 500 O HOH A 952 O HOH A 972 1.99
REMARK 500 O HOH A 935 O HOH A 952 2.00
REMARK 500 O HOH B 538 O HOH B 590 2.04
REMARK 500 O HOH A 705 O HOH A 771 2.07
REMARK 500 O HOH A 817 O HOH A 865 2.07
REMARK 500 O HOH A 871 O HOH A 937 2.09
REMARK 500 O HOH A 632 O HOH A 715 2.09
REMARK 500 O HOH B 937 O HOH B 947 2.09
REMARK 500 O HOH A 705 O HOH B 647 2.10
REMARK 500 O HOH A 577 O HOH A 957 2.11
REMARK 500 O HOH A 952 O HOH B 955 2.11
REMARK 500 O HOH B 883 O HOH B 946 2.12
REMARK 500 NH2 ARG A 263 O HOH A 501 2.13
REMARK 500 O HOH B 535 O HOH B 961 2.13
REMARK 500 O HOH B 582 O HOH B 682 2.14
REMARK 500 O HOH A 930 O HOH B 1009 2.14
REMARK 500 O HOH A 616 O HOH A 697 2.15
REMARK 500 O HOH A 688 O HOH A 723 2.15
REMARK 500 O HOH B 651 O HOH B 709 2.15
REMARK 500 O HOH A 881 O HOH A 952 2.15
REMARK 500 O HOH B 1008 O HOH B 1009 2.15
REMARK 500 O HOH B 877 O HOH B 1009 2.15
REMARK 500 O HOH B 965 O HOH B 979 2.15
REMARK 500 O HOH A 688 O HOH A 884 2.16
REMARK 500 O HOH A 507 O HOH A 886 2.16
REMARK 500 OD2 ASP A 235 O HOH A 502 2.18
REMARK 500 O HOH A 637 O HOH A 968 2.19
REMARK 500 O HOH A 657 O HOH A 712 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 658 O HOH B 528 2656 1.98
REMARK 500 O HOH A 577 O HOH B 557 2555 2.06
REMARK 500 O HOH A 668 O HOH B 682 2555 2.07
REMARK 500 O HOH A 555 O HOH B 604 2656 2.08
REMARK 500 O HOH A 687 O HOH B 706 2555 2.11
REMARK 500 O HOH A 699 O HOH B 670 2655 2.14
REMARK 500 O HOH A 705 O HOH B 653 2555 2.15
REMARK 500 O HOH A 696 O HOH B 682 2555 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 207 57.33 -155.78
REMARK 500 ASP B 40 -166.67 -105.32
REMARK 500 GLU B 144 -30.47 -130.79
REMARK 500 HIS B 151 75.50 -103.58
REMARK 500 ASP B 207 54.02 -156.46
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 B 971 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B 981 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 983 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 985 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 987 DISTANCE = 6.27 ANGSTROMS
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 MG A 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 233 OD2
REMARK 620 2 HOH A 505 O 71.0
REMARK 620 3 HOH A 556 O 102.3 96.1
REMARK 620 4 HOH A 633 O 96.8 167.4 89.0
REMARK 620 5 HOH B 523 O 85.5 92.9 169.6 83.1
REMARK 620 6 HOH B 664 O 171.0 104.1 85.6 87.7 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 405 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 233 OD1
REMARK 620 2 ASP A 235 OD1 74.8
REMARK 620 3 ASP A 235 OD2 121.0 47.9
REMARK 620 4 HOH A 502 O 166.3 92.7 48.4
REMARK 620 5 HOH A 625 O 94.6 163.7 144.4 96.5
REMARK 620 6 HOH A 856 O 93.6 85.7 72.5 90.7 107.6
REMARK 620 7 HOH B 555 O 95.5 81.8 89.5 77.1 87.1 162.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 851 O
REMARK 620 2 HOH A 875 O 84.1
REMARK 620 3 HOH A 885 O 78.1 83.9
REMARK 620 4 HOH A 922 O 90.9 166.8 83.1
REMARK 620 5 HOH A 973 O 91.1 95.4 169.2 96.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 406 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 571 O
REMARK 620 2 HOH A 685 O 99.4
REMARK 620 3 HOH A 689 O 90.1 86.0
REMARK 620 4 HOH B 560 O 88.4 171.7 91.1
REMARK 620 5 HOH B 804 O 170.5 90.1 89.7 82.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 547 O
REMARK 620 2 HOH A 581 O 84.9
REMARK 620 3 HOH A 664 O 177.8 96.6
REMARK 620 4 HOH A 675 O 98.3 176.3 80.2
REMARK 620 5 HOH A 841 O 95.0 90.5 83.5 91.0
REMARK 620 6 HOH B 680 O 90.6 90.1 91.0 88.1 174.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 513 O
REMARK 620 2 HOH B 597 O 73.4
REMARK 620 3 HOH B 648 O 85.9 78.2
REMARK 620 4 HOH B 887 O 166.9 93.4 91.3
REMARK 620 5 HOH B 891 O 92.2 85.5 163.4 86.9
REMARK 620 6 HOH B 951 O 91.8 165.1 100.3 101.4 96.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AVI A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AVI B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues CSD A 285
REMARK 800 through LYS A 286 bound to SER A 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues CSD B 285
REMARK 800 through LYS B 286 bound to SER B 284
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PIM RELATED DB: PDB
REMARK 900 EGTD, APO FORM
REMARK 900 RELATED ID: 4PIN RELATED DB: PDB
REMARK 900 EGTD IN COMPLEX WITH N,N-DIMETHYLHISTIDINE
REMARK 900 RELATED ID: 4PIP RELATED DB: PDB
REMARK 900 EGTD DOUBLE MUTANT (M252V, E282A) HYOA IN COMPLEX WITH TRYPTOPHAN
REMARK 900 AND SAH
DBREF 4PIO A 1 321 UNP A0R5M8 EGTD_MYCS2 1 321
DBREF 4PIO B 1 321 UNP A0R5M8 EGTD_MYCS2 1 321
SEQADV 4PIO GLY A -1 UNP A0R5M8 EXPRESSION TAG
SEQADV 4PIO HIS A 0 UNP A0R5M8 EXPRESSION TAG
SEQADV 4PIO ALA A 2 UNP A0R5M8 THR 2 ENGINEERED MUTATION
SEQADV 4PIO THR A 29 UNP A0R5M8 ALA 29 ENGINEERED MUTATION
SEQADV 4PIO GLN A 30 UNP A0R5M8 PRO 30 ENGINEERED MUTATION
SEQADV 4PIO SER A 75 UNP A0R5M8 ALA 75 ENGINEERED MUTATION
SEQADV 4PIO GLY B -1 UNP A0R5M8 EXPRESSION TAG
SEQADV 4PIO HIS B 0 UNP A0R5M8 EXPRESSION TAG
SEQADV 4PIO ALA B 2 UNP A0R5M8 THR 2 ENGINEERED MUTATION
SEQADV 4PIO THR B 29 UNP A0R5M8 ALA 29 ENGINEERED MUTATION
SEQADV 4PIO GLN B 30 UNP A0R5M8 PRO 30 ENGINEERED MUTATION
SEQADV 4PIO SER B 75 UNP A0R5M8 ALA 75 ENGINEERED MUTATION
SEQRES 1 A 323 GLY HIS MET ALA LEU SER LEU ALA ASN TYR LEU ALA ALA
SEQRES 2 A 323 ASP SER ALA ALA GLU ALA LEU ARG ARG ASP VAL ARG ALA
SEQRES 3 A 323 GLY LEU THR ALA THR GLN LYS SER LEU PRO PRO LYS TRP
SEQRES 4 A 323 PHE TYR ASP ALA VAL GLY SER ASP LEU PHE ASP GLN ILE
SEQRES 5 A 323 THR ARG LEU PRO GLU TYR TYR PRO THR ARG THR GLU ALA
SEQRES 6 A 323 GLN ILE LEU ARG THR ARG SER ALA GLU ILE ILE SER ALA
SEQRES 7 A 323 ALA GLY ALA ASP THR LEU VAL GLU LEU GLY SER GLY THR
SEQRES 8 A 323 SER GLU LYS THR ARG MET LEU LEU ASP ALA MET ARG ASP
SEQRES 9 A 323 ALA GLU LEU LEU ARG ARG PHE ILE PRO PHE ASP VAL ASP
SEQRES 10 A 323 ALA GLY VAL LEU ARG SER ALA GLY ALA ALA ILE GLY ALA
SEQRES 11 A 323 GLU TYR PRO GLY ILE GLU ILE ASP ALA VAL CYS GLY ASP
SEQRES 12 A 323 PHE GLU GLU HIS LEU GLY LYS ILE PRO HIS VAL GLY ARG
SEQRES 13 A 323 ARG LEU VAL VAL PHE LEU GLY SER THR ILE GLY ASN LEU
SEQRES 14 A 323 THR PRO ALA PRO ARG ALA GLU PHE LEU SER THR LEU ALA
SEQRES 15 A 323 ASP THR LEU GLN PRO GLY ASP SER LEU LEU LEU GLY THR
SEQRES 16 A 323 ASP LEU VAL LYS ASP THR GLY ARG LEU VAL ARG ALA TYR
SEQRES 17 A 323 ASP ASP ALA ALA GLY VAL THR ALA ALA PHE ASN ARG ASN
SEQRES 18 A 323 VAL LEU ALA VAL VAL ASN ARG GLU LEU SER ALA ASP PHE
SEQRES 19 A 323 ASP LEU ASP ALA PHE GLU HIS VAL ALA LYS TRP ASN SER
SEQRES 20 A 323 ASP GLU GLU ARG ILE GLU MET TRP LEU ARG ALA ARG THR
SEQRES 21 A 323 ALA GLN HIS VAL ARG VAL ALA ALA LEU ASP LEU GLU VAL
SEQRES 22 A 323 ASP PHE ALA ALA GLY GLU GLU MET LEU THR GLU VAL SER
SEQRES 23 A 323 CSD LYS PHE ARG PRO GLU ASN VAL VAL ALA GLU LEU ALA
SEQRES 24 A 323 GLU ALA GLY LEU ARG GLN THR HIS TRP TRP THR ASP PRO
SEQRES 25 A 323 ALA GLY ASP PHE GLY LEU SER LEU ALA VAL ARG
SEQRES 1 B 323 GLY HIS MET ALA LEU SER LEU ALA ASN TYR LEU ALA ALA
SEQRES 2 B 323 ASP SER ALA ALA GLU ALA LEU ARG ARG ASP VAL ARG ALA
SEQRES 3 B 323 GLY LEU THR ALA THR GLN LYS SER LEU PRO PRO LYS TRP
SEQRES 4 B 323 PHE TYR ASP ALA VAL GLY SER ASP LEU PHE ASP GLN ILE
SEQRES 5 B 323 THR ARG LEU PRO GLU TYR TYR PRO THR ARG THR GLU ALA
SEQRES 6 B 323 GLN ILE LEU ARG THR ARG SER ALA GLU ILE ILE SER ALA
SEQRES 7 B 323 ALA GLY ALA ASP THR LEU VAL GLU LEU GLY SER GLY THR
SEQRES 8 B 323 SER GLU LYS THR ARG MET LEU LEU ASP ALA MET ARG ASP
SEQRES 9 B 323 ALA GLU LEU LEU ARG ARG PHE ILE PRO PHE ASP VAL ASP
SEQRES 10 B 323 ALA GLY VAL LEU ARG SER ALA GLY ALA ALA ILE GLY ALA
SEQRES 11 B 323 GLU TYR PRO GLY ILE GLU ILE ASP ALA VAL CYS GLY ASP
SEQRES 12 B 323 PHE GLU GLU HIS LEU GLY LYS ILE PRO HIS VAL GLY ARG
SEQRES 13 B 323 ARG LEU VAL VAL PHE LEU GLY SER THR ILE GLY ASN LEU
SEQRES 14 B 323 THR PRO ALA PRO ARG ALA GLU PHE LEU SER THR LEU ALA
SEQRES 15 B 323 ASP THR LEU GLN PRO GLY ASP SER LEU LEU LEU GLY THR
SEQRES 16 B 323 ASP LEU VAL LYS ASP THR GLY ARG LEU VAL ARG ALA TYR
SEQRES 17 B 323 ASP ASP ALA ALA GLY VAL THR ALA ALA PHE ASN ARG ASN
SEQRES 18 B 323 VAL LEU ALA VAL VAL ASN ARG GLU LEU SER ALA ASP PHE
SEQRES 19 B 323 ASP LEU ASP ALA PHE GLU HIS VAL ALA LYS TRP ASN SER
SEQRES 20 B 323 ASP GLU GLU ARG ILE GLU MET TRP LEU ARG ALA ARG THR
SEQRES 21 B 323 ALA GLN HIS VAL ARG VAL ALA ALA LEU ASP LEU GLU VAL
SEQRES 22 B 323 ASP PHE ALA ALA GLY GLU GLU MET LEU THR GLU VAL SER
SEQRES 23 B 323 CSD LYS PHE ARG PRO GLU ASN VAL VAL ALA GLU LEU ALA
SEQRES 24 B 323 GLU ALA GLY LEU ARG GLN THR HIS TRP TRP THR ASP PRO
SEQRES 25 B 323 ALA GLY ASP PHE GLY LEU SER LEU ALA VAL ARG
HET CSD A 285 11
HET CSD B 285 11
HET SAH A 401 46
HET AVI A 402 25
HET MG A 403 1
HET MG A 404 1
HET MG A 405 1
HET MG A 406 1
HET CL A 407 1
HET SAH B 401 45
HET AVI B 402 25
HET MG B 403 1
HET MG B 404 1
HETNAM CSD 3-SULFINOALANINE
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM AVI N,N-DIMETHYL-L-HISTIDINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 4 AVI 2(C8 H13 N3 O2)
FORMUL 5 MG 6(MG 2+)
FORMUL 9 CL CL 1-
FORMUL 14 HOH *985(H2 O)
HELIX 1 AA1 ALA A 15 ALA A 28 1 14
HELIX 2 AA2 PRO A 34 TYR A 39 5 6
HELIX 3 AA3 ASP A 40 THR A 51 1 12
HELIX 4 AA4 TYR A 57 GLY A 78 1 22
HELIX 5 AA5 LYS A 92 ALA A 103 1 12
HELIX 6 AA6 ASP A 115 TYR A 130 1 16
HELIX 7 AA7 HIS A 145 ILE A 149 5 5
HELIX 8 AA8 SER A 162 LEU A 167 5 6
HELIX 9 AA9 THR A 168 ASP A 181 1 14
HELIX 10 AB1 ASP A 198 TYR A 206 1 9
HELIX 11 AB2 GLY A 211 SER A 229 1 19
HELIX 12 AB3 ASP A 233 ASP A 235 5 3
HELIX 13 AB4 ALA A 265 ASP A 268 5 4
HELIX 14 AB5 ARG A 288 ALA A 299 1 12
HELIX 15 AB6 ALA B 10 THR B 27 1 18
HELIX 16 AB7 PRO B 34 TYR B 39 5 6
HELIX 17 AB8 ASP B 40 THR B 51 1 12
HELIX 18 AB9 TYR B 57 GLY B 78 1 22
HELIX 19 AC1 LYS B 92 ALA B 103 1 12
HELIX 20 AC2 ASP B 115 TYR B 130 1 16
HELIX 21 AC3 HIS B 145 ILE B 149 5 5
HELIX 22 AC4 SER B 162 LEU B 167 5 6
HELIX 23 AC5 THR B 168 LEU B 183 1 16
HELIX 24 AC6 ASP B 198 TYR B 206 1 9
HELIX 25 AC7 GLY B 211 SER B 229 1 19
HELIX 26 AC8 ASP B 233 ASP B 235 5 3
HELIX 27 AC9 ALA B 265 ASP B 268 5 4
HELIX 28 AD1 ARG B 288 ALA B 299 1 12
SHEET 1 AA1 3 GLU A 134 ILE A 135 0
SHEET 2 AA1 3 ARG A 108 ASP A 113 1 N PHE A 109 O GLU A 134
SHEET 3 AA1 3 VAL A 138 CYS A 139 1 O VAL A 138 N PRO A 111
SHEET 1 AA2 7 GLU A 134 ILE A 135 0
SHEET 2 AA2 7 ARG A 108 ASP A 113 1 N PHE A 109 O GLU A 134
SHEET 3 AA2 7 THR A 81 LEU A 85 1 N LEU A 82 O ILE A 110
SHEET 4 AA2 7 ARG A 155 PHE A 159 1 O VAL A 158 N VAL A 83
SHEET 5 AA2 7 SER A 188 ASP A 194 1 O SER A 188 N VAL A 157
SHEET 6 AA2 7 PHE A 314 VAL A 320 -1 O GLY A 315 N THR A 193
SHEET 7 AA2 7 ARG A 302 THR A 308 -1 N THR A 304 O LEU A 318
SHEET 1 AA3 3 PHE A 237 ASN A 244 0
SHEET 2 AA3 3 ARG A 249 ALA A 256 -1 O ARG A 255 N GLU A 238
SHEET 3 AA3 3 GLU A 278 CSD A 285 -1 O GLU A 282 N MET A 252
SHEET 1 AA4 2 GLN A 260 VAL A 264 0
SHEET 2 AA4 2 LEU A 269 PHE A 273 -1 O LEU A 269 N VAL A 264
SHEET 1 AA5 4 LEU B 5 ASN B 7 0
SHEET 2 AA5 4 ALA B 137 CYS B 139 1 O CYS B 139 N ALA B 6
SHEET 3 AA5 4 ARG B 108 ASP B 113 1 N PRO B 111 O VAL B 138
SHEET 4 AA5 4 GLU B 134 ILE B 135 1 O GLU B 134 N PHE B 109
SHEET 1 AA6 8 LEU B 5 ASN B 7 0
SHEET 2 AA6 8 ALA B 137 CYS B 139 1 O CYS B 139 N ALA B 6
SHEET 3 AA6 8 ARG B 108 ASP B 113 1 N PRO B 111 O VAL B 138
SHEET 4 AA6 8 THR B 81 LEU B 85 1 N LEU B 82 O ILE B 110
SHEET 5 AA6 8 ARG B 155 PHE B 159 1 O VAL B 158 N VAL B 83
SHEET 6 AA6 8 SER B 188 ASP B 194 1 O LEU B 190 N VAL B 157
SHEET 7 AA6 8 PHE B 314 VAL B 320 -1 O ALA B 319 N LEU B 189
SHEET 8 AA6 8 ARG B 302 THR B 308 -1 N TRP B 307 O LEU B 316
SHEET 1 AA7 3 PHE B 237 ASN B 244 0
SHEET 2 AA7 3 ARG B 249 ALA B 256 -1 O ARG B 255 N GLU B 238
SHEET 3 AA7 3 GLU B 278 CSD B 285 -1 O SER B 284 N ILE B 250
SHEET 1 AA8 2 GLN B 260 VAL B 264 0
SHEET 2 AA8 2 LEU B 269 PHE B 273 -1 O LEU B 269 N VAL B 264
LINK C SER A 284 N CSD A 285 1555 1555 1.32
LINK C CSD A 285 N LYS A 286 1555 1555 1.34
LINK C SER B 284 N CSD B 285 1555 1555 1.32
LINK C CSD B 285 N LYS B 286 1555 1555 1.33
LINK OD2 ASP A 233 MG MG A 404 1555 1555 1.99
LINK OD1 ASP A 233 MG MG A 405 1555 1555 2.07
LINK OD1 ASP A 235 MG MG A 405 1555 1555 2.48
LINK OD2 ASP A 235 MG MG A 405 1555 1555 2.88
LINK MG MG A 403 O HOH A 851 1555 1555 2.07
LINK MG MG A 403 O HOH A 875 1555 1555 2.11
LINK MG MG A 403 O HOH A 885 1555 1555 2.30
LINK MG MG A 403 O HOH A 922 1555 1555 2.09
LINK MG MG A 403 O HOH A 973 1555 1555 2.22
LINK MG MG A 404 O HOH A 505 1555 1555 1.99
LINK MG MG A 404 O HOH A 556 1555 1555 2.08
LINK MG MG A 404 O HOH A 633 1555 1555 2.23
LINK MG MG A 404 O HOH B 523 1555 2556 2.20
LINK MG MG A 404 O HOH B 664 1555 2556 2.11
LINK MG MG A 405 O HOH A 502 1555 1555 2.26
LINK MG MG A 405 O HOH A 625 1555 1555 2.15
LINK MG MG A 405 O HOH A 856 1555 1555 1.99
LINK MG MG A 405 O HOH B 555 1555 2556 1.96
LINK MG MG A 406 O HOH A 571 1555 2645 2.18
LINK MG MG A 406 O HOH A 685 1555 1555 2.54
LINK MG MG A 406 O HOH A 689 1555 1555 2.41
LINK MG MG A 406 O HOH B 560 1555 2555 2.13
LINK MG MG A 406 O HOH B 804 1555 2555 2.35
LINK O HOH A 547 MG MG B 403 2545 1555 2.14
LINK O HOH A 581 MG MG B 403 2545 1555 2.12
LINK O HOH A 664 MG MG B 403 2545 1555 2.11
LINK O HOH A 675 MG MG B 403 2545 1555 2.06
LINK O HOH A 841 MG MG B 403 2545 1555 2.06
LINK MG MG B 403 O HOH B 680 1555 1555 2.08
LINK MG MG B 404 O HOH B 513 1555 1555 2.06
LINK MG MG B 404 O HOH B 597 1555 1555 2.46
LINK MG MG B 404 O HOH B 648 1555 2546 2.20
LINK MG MG B 404 O HOH B 887 1555 2546 2.21
LINK MG MG B 404 O HOH B 891 1555 1555 2.34
LINK MG MG B 404 O HOH B 951 1555 1555 2.16
SITE 1 AC1 20 TYR A 39 PHE A 47 GLY A 86 SER A 87
SITE 2 AC1 20 GLY A 88 LYS A 92 ASP A 113 VAL A 114
SITE 3 AC1 20 GLY A 140 ASP A 141 PHE A 142 GLY A 161
SITE 4 AC1 20 AVI A 402 HOH A 738 HOH A 740 HOH A 746
SITE 5 AC1 20 HOH A 753 HOH A 757 HOH A 759 HOH A 783
SITE 1 AC2 12 TYR A 39 TYR A 56 GLY A 161 SER A 162
SITE 2 AC2 12 THR A 163 ASN A 166 TYR A 206 MET A 252
SITE 3 AC2 12 GLU A 282 SER A 284 SAH A 401 HOH A 772
SITE 1 AC3 5 HOH A 851 HOH A 875 HOH A 885 HOH A 922
SITE 2 AC3 5 HOH A 973
SITE 1 AC4 4 ASP A 233 HOH A 505 HOH A 556 HOH A 633
SITE 1 AC5 5 ASP A 233 ASP A 235 HOH A 502 HOH A 625
SITE 2 AC5 5 HOH A 856
SITE 1 AC6 2 HOH A 685 HOH A 689
SITE 1 AC7 3 ARG A 218 HIS A 239 ARG A 257
SITE 1 AC8 21 LYS B 36 TYR B 39 PHE B 47 GLY B 86
SITE 2 AC8 21 SER B 87 GLY B 88 LYS B 92 ASP B 113
SITE 3 AC8 21 VAL B 114 GLY B 140 ASP B 141 PHE B 142
SITE 4 AC8 21 GLY B 161 AVI B 402 HOH B 741 HOH B 742
SITE 5 AC8 21 HOH B 745 HOH B 746 HOH B 790 HOH B 791
SITE 6 AC8 21 HOH B 792
SITE 1 AC9 13 TYR B 39 TYR B 56 GLY B 161 SER B 162
SITE 2 AC9 13 THR B 163 ASN B 166 TYR B 206 PHE B 216
SITE 3 AC9 13 MET B 252 GLU B 282 SER B 284 SAH B 401
SITE 4 AC9 13 HOH B 739
SITE 1 AD1 1 HOH B 680
SITE 1 AD2 4 HOH B 513 HOH B 597 HOH B 891 HOH B 951
SITE 1 AD3 14 GLY A 165 LEU A 167 PRO A 169 ARG A 172
SITE 2 AD3 14 ASP A 194 TYR A 206 GLU A 248 ARG A 249
SITE 3 AD3 14 SER A 284 PHE A 287 HOH A 743 HOH A 806
SITE 4 AD3 14 HOH A 808 HOH A 836
SITE 1 AD4 14 GLY B 165 LEU B 167 PRO B 169 ARG B 172
SITE 2 AD4 14 ASP B 194 TYR B 206 GLU B 248 ARG B 249
SITE 3 AD4 14 SER B 284 PHE B 287 HOH B 723 HOH B 724
SITE 4 AD4 14 HOH B 725 HOH B 760
CRYST1 56.709 67.511 79.679 90.00 110.98 90.00 P 1 21 1 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 0.017634 0.000000 0.006762 0.00000
SCALE2 0.000000 0.014812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013441 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
