HEADER OXIDOREDUCTASE/ANTIBIOTIC 31-JAN-14 4OOE
TITLE M. TUBERCULOSIS 1-DEOXY-D-XYLULOSE-5-PHOSPHATE REDUCTOISOMERASE W203Y
TITLE 2 MUTANT BOUND TO FOSMIDOMYCIN AND NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 1-389;
COMPND 5 SYNONYM: DXP REDUCTOISOMERASE, 1-DEOXYXYLULOSE-5-PHOSPHATE
COMPND 6 REDUCTOISOMERASE, 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE SYNTHASE;
COMPND 7 EC: 1.1.1.267;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: DXR, RVBD_2870C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS REDUCTOISOMERASE, OXIDOREDUCTASE-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.ALLEN,S.A.KHOLODAR,A.S.MURKIN,A.M.GULICK
REVDAT 2 20-SEP-23 4OOE 1 REMARK SEQADV LINK
REVDAT 1 18-JUN-14 4OOE 0
JRNL AUTH S.A.KHOLODAR,G.TOMBLINE,J.LIU,Z.TAN,C.L.ALLEN,A.M.GULICK,
JRNL AUTH 2 A.S.MURKIN
JRNL TITL ALTERATION OF THE FLEXIBLE LOOP IN
JRNL TITL 2 1-DEOXY-D-XYLULOSE-5-PHOSPHATE REDUCTOISOMERASE BOOSTS
JRNL TITL 3 ENTHALPY-DRIVEN INHIBITION BY FOSMIDOMYCIN.
JRNL REF BIOCHEMISTRY V. 53 3423 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24825256
JRNL DOI 10.1021/BI5004074
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 142154
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.370
REMARK 3 FREE R VALUE TEST SET COUNT : 1949
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 38.8361 - 4.4001 0.92 10263 143 0.1502 0.1761
REMARK 3 2 4.4001 - 3.4932 0.95 10343 142 0.1407 0.1777
REMARK 3 3 3.4932 - 3.0518 0.97 10392 147 0.1617 0.2115
REMARK 3 4 3.0518 - 2.7729 0.97 10390 140 0.1733 0.2246
REMARK 3 5 2.7729 - 2.5742 0.96 10303 145 0.1770 0.2189
REMARK 3 6 2.5742 - 2.4224 0.97 10347 150 0.1784 0.2222
REMARK 3 7 2.4224 - 2.3011 0.98 10417 147 0.1711 0.2113
REMARK 3 8 2.3011 - 2.2010 0.97 10287 141 0.1725 0.1952
REMARK 3 9 2.2010 - 2.1163 0.98 10342 141 0.1742 0.2161
REMARK 3 10 2.1163 - 2.0432 0.96 10229 151 0.1808 0.2260
REMARK 3 11 2.0432 - 1.9793 0.96 10241 129 0.1913 0.2348
REMARK 3 12 1.9793 - 1.9228 0.95 10040 145 0.2037 0.2599
REMARK 3 13 1.9228 - 1.8722 0.88 9251 129 0.2231 0.2747
REMARK 3 14 1.8722 - 1.8260 0.69 7360 99 0.2557 0.3387
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
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 : 0.007 11550
REMARK 3 ANGLE : 1.153 15834
REMARK 3 CHIRALITY : 0.071 1865
REMARK 3 PLANARITY : 0.005 2066
REMARK 3 DIHEDRAL : 16.488 4088
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 4OOE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084747.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.284
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145456
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.826
REMARK 200 RESOLUTION RANGE LOW (A) : 86.712
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.24700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4A03
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG4000, 50 MM MES, 20% MPD, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, 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 56.13500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.59350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.59350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.13500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.12000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 7350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 MET A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 ARG A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 ASP A 6
REMARK 465 GLY A 7
REMARK 465 ARG A 8
REMARK 465 ALA A 9
REMARK 465 ASP A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 388
REMARK 465 MET A 389
REMARK 465 MET B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 ARG B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 THR B 5
REMARK 465 ASP B 6
REMARK 465 GLY B 7
REMARK 465 ARG B 8
REMARK 465 ALA B 9
REMARK 465 ASP B 10
REMARK 465 GLY B 11
REMARK 465 MET C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 LEU C -7
REMARK 465 VAL C -6
REMARK 465 ARG C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ASN C 3
REMARK 465 SER C 4
REMARK 465 THR C 5
REMARK 465 ASP C 6
REMARK 465 GLY C 7
REMARK 465 ARG C 8
REMARK 465 ALA C 9
REMARK 465 ASP C 10
REMARK 465 GLY C 11
REMARK 465 MET C 389
REMARK 465 MET D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 LEU D -7
REMARK 465 VAL D -6
REMARK 465 ARG D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASN D 3
REMARK 465 SER D 4
REMARK 465 THR D 5
REMARK 465 ASP D 6
REMARK 465 GLY D 7
REMARK 465 ARG D 8
REMARK 465 ALA D 9
REMARK 465 ASP D 10
REMARK 465 GLY D 11
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 ARG A 143 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 279 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 297 CD OE1 OE2
REMARK 470 ASP A 359 CG OD1 OD2
REMARK 470 LYS B 171 NZ
REMARK 470 ASP C 37 CG OD1 OD2
REMARK 470 GLN C 75 CG CD OE1 NE2
REMARK 470 ARG C 143 CD NE CZ NH1 NH2
REMARK 470 GLU C 190 CG CD OE1 OE2
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 ARG C 279 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 291 CG ND1 CD2 CE1 NE2
REMARK 470 ASP C 359 CG OD1 OD2
REMARK 470 ARG D 279 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 359 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 675 O HOH A 845 2.01
REMARK 500 O HOH A 775 O HOH A 784 2.03
REMARK 500 O HOH C 760 O HOH C 844 2.08
REMARK 500 O HOH A 912 O HOH A 941 2.09
REMARK 500 O HOH C 740 O HOH C 761 2.10
REMARK 500 O HOH A 1008 O HOH A 1018 2.10
REMARK 500 O HOH D 865 O HOH D 962 2.12
REMARK 500 O HOH A 775 O HOH A 826 2.12
REMARK 500 O HOH A 781 O HOH A 904 2.13
REMARK 500 O HOH B 778 O HOH B 1025 2.13
REMARK 500 O HOH D 830 O HOH D 950 2.14
REMARK 500 O HOH B 990 O HOH B 1004 2.14
REMARK 500 O HOH B 995 O HOH B 1067 2.14
REMARK 500 OD1 ASP B 37 O HOH B 998 2.14
REMARK 500 O HOH A 831 O HOH A 926 2.14
REMARK 500 O HOH C 952 O HOH C 993 2.14
REMARK 500 O HOH C 932 O HOH C 943 2.14
REMARK 500 O HOH D 654 O HOH D 849 2.14
REMARK 500 O HOH B 1030 O HOH B 1054 2.14
REMARK 500 O HOH B 763 O HOH B 883 2.15
REMARK 500 O HOH C 938 O HOH C 966 2.15
REMARK 500 O HOH C 806 O HOH C 929 2.15
REMARK 500 O HOH B 820 O HOH B 889 2.16
REMARK 500 OE2 GLU C 310 O HOH C 838 2.16
REMARK 500 O HOH D 727 O HOH D 872 2.17
REMARK 500 O HOH C 821 O HOH C 849 2.17
REMARK 500 O HOH B 934 O HOH B 1027 2.17
REMARK 500 O HOH B 642 O HOH B 871 2.17
REMARK 500 O HOH D 962 O HOH D 979 2.18
REMARK 500 O HOH B 809 O HOH B 936 2.18
REMARK 500 O HOH D 602 O HOH D 977 2.18
REMARK 500 O HOH D 858 O HOH D 954 2.18
REMARK 500 O HOH C 864 O HOH C 911 2.18
REMARK 500 O HOH B 733 O HOH B 971 2.18
REMARK 500 O HOH A 898 O HOH A 913 2.18
REMARK 500 O HOH C 723 O HOH C 965 2.18
REMARK 500 O HOH B 841 O HOH B 973 2.18
REMARK 500 O HOH A 830 O HOH A 856 2.19
REMARK 500 O HOH D 882 O HOH D 943 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 954 O HOH C 937 1655 2.11
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 SER A 249 171.89 161.73
REMARK 500 ASP A 266 112.06 -160.88
REMARK 500 SER B 249 170.84 162.45
REMARK 500 ASP B 266 104.47 -167.89
REMARK 500 ALA B 362 48.47 -86.45
REMARK 500 SER C 249 173.68 168.75
REMARK 500 ASP C 266 109.29 -163.53
REMARK 500 HIS D 50 77.48 -117.10
REMARK 500 SER D 249 173.44 171.77
REMARK 500 ASP D 266 110.55 -164.73
REMARK 500 ALA D 362 38.29 -82.76
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 MN A 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 151 OD1
REMARK 620 2 GLU A 153 OE1 94.9
REMARK 620 3 GLU A 222 OE2 102.0 95.1
REMARK 620 4 FOM A 500 O2 117.3 146.2 88.5
REMARK 620 5 FOM A 500 O1 88.3 98.1 162.5 74.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 151 OD2
REMARK 620 2 GLU B 153 OE1 98.8
REMARK 620 3 GLU B 222 OE2 104.2 97.3
REMARK 620 4 FOM B 500 O2 112.4 146.2 87.7
REMARK 620 5 FOM B 500 O1 87.5 93.9 162.3 75.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 151 OD1
REMARK 620 2 GLU C 153 OE1 96.5
REMARK 620 3 GLU C 222 OE2 100.2 96.3
REMARK 620 4 FOM C 500 O2 86.9 98.4 162.8
REMARK 620 5 FOM C 500 N1 108.6 121.4 128.0 35.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 151 OD2
REMARK 620 2 GLU D 153 OE1 91.9
REMARK 620 3 GLU D 222 OE2 100.9 91.4
REMARK 620 4 FOM D 500 O2 117.8 149.6 89.1
REMARK 620 5 FOM D 500 O1 87.7 98.0 167.1 78.3
REMARK 620 6 FOM D 500 N1 119.3 131.1 115.5 28.8 51.6
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 FOM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOM C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOM D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZHX RELATED DB: PDB
REMARK 900 DXR
REMARK 900 RELATED ID: 4AIC RELATED DB: PDB
REMARK 900 DXR
REMARK 900 RELATED ID: 4OOF RELATED DB: PDB
DBREF 4OOE A 1 389 UNP I6YAH0 I6YAH0_MYCTU 1 389
DBREF 4OOE B 1 389 UNP I6YAH0 I6YAH0_MYCTU 1 389
DBREF 4OOE C 1 389 UNP I6YAH0 I6YAH0_MYCTU 1 389
DBREF 4OOE D 1 389 UNP I6YAH0 I6YAH0_MYCTU 1 389
SEQADV 4OOE MET A -14 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A -13 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A -12 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A -11 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A -10 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A -9 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A -8 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE LEU A -7 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE VAL A -6 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG A -5 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE PRO A -4 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG A -3 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE GLY A -2 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE SER A -1 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS A 0 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE TYR A 203 UNP I6YAH0 TRP 203 ENGINEERED MUTATION
SEQADV 4OOE MET B -14 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B -13 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B -12 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B -11 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B -10 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B -9 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B -8 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE LEU B -7 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE VAL B -6 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG B -5 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE PRO B -4 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG B -3 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE GLY B -2 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE SER B -1 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS B 0 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE TYR B 203 UNP I6YAH0 TRP 203 ENGINEERED MUTATION
SEQADV 4OOE MET C -14 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C -13 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C -12 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C -11 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C -10 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C -9 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C -8 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE LEU C -7 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE VAL C -6 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG C -5 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE PRO C -4 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG C -3 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE GLY C -2 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE SER C -1 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS C 0 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE TYR C 203 UNP I6YAH0 TRP 203 ENGINEERED MUTATION
SEQADV 4OOE MET D -14 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D -13 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D -12 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D -11 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D -10 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D -9 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D -8 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE LEU D -7 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE VAL D -6 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG D -5 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE PRO D -4 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE ARG D -3 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE GLY D -2 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE SER D -1 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE HIS D 0 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOE TYR D 203 UNP I6YAH0 TRP 203 ENGINEERED MUTATION
SEQRES 1 A 404 MET HIS HIS HIS HIS HIS HIS LEU VAL ARG PRO ARG GLY
SEQRES 2 A 404 SER HIS MET THR ASN SER THR ASP GLY ARG ALA ASP GLY
SEQRES 3 A 404 ARG LEU ARG VAL VAL VAL LEU GLY SER THR GLY SER ILE
SEQRES 4 A 404 GLY THR GLN ALA LEU GLN VAL ILE ALA ASP ASN PRO ASP
SEQRES 5 A 404 ARG PHE GLU VAL VAL GLY LEU ALA ALA GLY GLY ALA HIS
SEQRES 6 A 404 LEU ASP THR LEU LEU ARG GLN ARG ALA GLN THR GLY VAL
SEQRES 7 A 404 THR ASN ILE ALA VAL ALA ASP GLU HIS ALA ALA GLN ARG
SEQRES 8 A 404 VAL GLY ASP ILE PRO TYR HIS GLY SER ASP ALA ALA THR
SEQRES 9 A 404 ARG LEU VAL GLU GLN THR GLU ALA ASP VAL VAL LEU ASN
SEQRES 10 A 404 ALA LEU VAL GLY ALA LEU GLY LEU ARG PRO THR LEU ALA
SEQRES 11 A 404 ALA LEU LYS THR GLY ALA ARG LEU ALA LEU ALA ASN LYS
SEQRES 12 A 404 GLU SER LEU VAL ALA GLY GLY SER LEU VAL LEU ARG ALA
SEQRES 13 A 404 ALA ARG PRO GLY GLN ILE VAL PRO VAL ASP SER GLU HIS
SEQRES 14 A 404 SER ALA LEU ALA GLN CYS LEU ARG GLY GLY THR PRO ASP
SEQRES 15 A 404 GLU VAL ALA LYS LEU VAL LEU THR ALA SER GLY GLY PRO
SEQRES 16 A 404 PHE ARG GLY TRP SER ALA ALA ASP LEU GLU HIS VAL THR
SEQRES 17 A 404 PRO GLU GLN ALA GLY ALA HIS PRO THR TYR SER MET GLY
SEQRES 18 A 404 PRO MET ASN THR LEU ASN SER ALA SER LEU VAL ASN LYS
SEQRES 19 A 404 GLY LEU GLU VAL ILE GLU THR HIS LEU LEU PHE GLY ILE
SEQRES 20 A 404 PRO TYR ASP ARG ILE ASP VAL VAL VAL HIS PRO GLN SER
SEQRES 21 A 404 ILE ILE HIS SER MET VAL THR PHE ILE ASP GLY SER THR
SEQRES 22 A 404 ILE ALA GLN ALA SER PRO PRO ASP MET LYS LEU PRO ILE
SEQRES 23 A 404 SER LEU ALA LEU GLY TRP PRO ARG ARG VAL SER GLY ALA
SEQRES 24 A 404 ALA ALA ALA CYS ASP PHE HIS THR ALA SER SER TRP GLU
SEQRES 25 A 404 PHE GLU PRO LEU ASP THR ASP VAL PHE PRO ALA VAL GLU
SEQRES 26 A 404 LEU ALA ARG GLN ALA GLY VAL ALA GLY GLY CYS MET THR
SEQRES 27 A 404 ALA VAL TYR ASN ALA ALA ASN GLU GLU ALA ALA ALA ALA
SEQRES 28 A 404 PHE LEU ALA GLY ARG ILE GLY PHE PRO ALA ILE VAL GLY
SEQRES 29 A 404 ILE ILE ALA ASP VAL LEU HIS ALA ALA ASP GLN TRP ALA
SEQRES 30 A 404 VAL GLU PRO ALA THR VAL ASP ASP VAL LEU ASP ALA GLN
SEQRES 31 A 404 ARG TRP ALA ARG GLU ARG ALA GLN ARG ALA VAL SER GLY
SEQRES 32 A 404 MET
SEQRES 1 B 404 MET HIS HIS HIS HIS HIS HIS LEU VAL ARG PRO ARG GLY
SEQRES 2 B 404 SER HIS MET THR ASN SER THR ASP GLY ARG ALA ASP GLY
SEQRES 3 B 404 ARG LEU ARG VAL VAL VAL LEU GLY SER THR GLY SER ILE
SEQRES 4 B 404 GLY THR GLN ALA LEU GLN VAL ILE ALA ASP ASN PRO ASP
SEQRES 5 B 404 ARG PHE GLU VAL VAL GLY LEU ALA ALA GLY GLY ALA HIS
SEQRES 6 B 404 LEU ASP THR LEU LEU ARG GLN ARG ALA GLN THR GLY VAL
SEQRES 7 B 404 THR ASN ILE ALA VAL ALA ASP GLU HIS ALA ALA GLN ARG
SEQRES 8 B 404 VAL GLY ASP ILE PRO TYR HIS GLY SER ASP ALA ALA THR
SEQRES 9 B 404 ARG LEU VAL GLU GLN THR GLU ALA ASP VAL VAL LEU ASN
SEQRES 10 B 404 ALA LEU VAL GLY ALA LEU GLY LEU ARG PRO THR LEU ALA
SEQRES 11 B 404 ALA LEU LYS THR GLY ALA ARG LEU ALA LEU ALA ASN LYS
SEQRES 12 B 404 GLU SER LEU VAL ALA GLY GLY SER LEU VAL LEU ARG ALA
SEQRES 13 B 404 ALA ARG PRO GLY GLN ILE VAL PRO VAL ASP SER GLU HIS
SEQRES 14 B 404 SER ALA LEU ALA GLN CYS LEU ARG GLY GLY THR PRO ASP
SEQRES 15 B 404 GLU VAL ALA LYS LEU VAL LEU THR ALA SER GLY GLY PRO
SEQRES 16 B 404 PHE ARG GLY TRP SER ALA ALA ASP LEU GLU HIS VAL THR
SEQRES 17 B 404 PRO GLU GLN ALA GLY ALA HIS PRO THR TYR SER MET GLY
SEQRES 18 B 404 PRO MET ASN THR LEU ASN SER ALA SER LEU VAL ASN LYS
SEQRES 19 B 404 GLY LEU GLU VAL ILE GLU THR HIS LEU LEU PHE GLY ILE
SEQRES 20 B 404 PRO TYR ASP ARG ILE ASP VAL VAL VAL HIS PRO GLN SER
SEQRES 21 B 404 ILE ILE HIS SER MET VAL THR PHE ILE ASP GLY SER THR
SEQRES 22 B 404 ILE ALA GLN ALA SER PRO PRO ASP MET LYS LEU PRO ILE
SEQRES 23 B 404 SER LEU ALA LEU GLY TRP PRO ARG ARG VAL SER GLY ALA
SEQRES 24 B 404 ALA ALA ALA CYS ASP PHE HIS THR ALA SER SER TRP GLU
SEQRES 25 B 404 PHE GLU PRO LEU ASP THR ASP VAL PHE PRO ALA VAL GLU
SEQRES 26 B 404 LEU ALA ARG GLN ALA GLY VAL ALA GLY GLY CYS MET THR
SEQRES 27 B 404 ALA VAL TYR ASN ALA ALA ASN GLU GLU ALA ALA ALA ALA
SEQRES 28 B 404 PHE LEU ALA GLY ARG ILE GLY PHE PRO ALA ILE VAL GLY
SEQRES 29 B 404 ILE ILE ALA ASP VAL LEU HIS ALA ALA ASP GLN TRP ALA
SEQRES 30 B 404 VAL GLU PRO ALA THR VAL ASP ASP VAL LEU ASP ALA GLN
SEQRES 31 B 404 ARG TRP ALA ARG GLU ARG ALA GLN ARG ALA VAL SER GLY
SEQRES 32 B 404 MET
SEQRES 1 C 404 MET HIS HIS HIS HIS HIS HIS LEU VAL ARG PRO ARG GLY
SEQRES 2 C 404 SER HIS MET THR ASN SER THR ASP GLY ARG ALA ASP GLY
SEQRES 3 C 404 ARG LEU ARG VAL VAL VAL LEU GLY SER THR GLY SER ILE
SEQRES 4 C 404 GLY THR GLN ALA LEU GLN VAL ILE ALA ASP ASN PRO ASP
SEQRES 5 C 404 ARG PHE GLU VAL VAL GLY LEU ALA ALA GLY GLY ALA HIS
SEQRES 6 C 404 LEU ASP THR LEU LEU ARG GLN ARG ALA GLN THR GLY VAL
SEQRES 7 C 404 THR ASN ILE ALA VAL ALA ASP GLU HIS ALA ALA GLN ARG
SEQRES 8 C 404 VAL GLY ASP ILE PRO TYR HIS GLY SER ASP ALA ALA THR
SEQRES 9 C 404 ARG LEU VAL GLU GLN THR GLU ALA ASP VAL VAL LEU ASN
SEQRES 10 C 404 ALA LEU VAL GLY ALA LEU GLY LEU ARG PRO THR LEU ALA
SEQRES 11 C 404 ALA LEU LYS THR GLY ALA ARG LEU ALA LEU ALA ASN LYS
SEQRES 12 C 404 GLU SER LEU VAL ALA GLY GLY SER LEU VAL LEU ARG ALA
SEQRES 13 C 404 ALA ARG PRO GLY GLN ILE VAL PRO VAL ASP SER GLU HIS
SEQRES 14 C 404 SER ALA LEU ALA GLN CYS LEU ARG GLY GLY THR PRO ASP
SEQRES 15 C 404 GLU VAL ALA LYS LEU VAL LEU THR ALA SER GLY GLY PRO
SEQRES 16 C 404 PHE ARG GLY TRP SER ALA ALA ASP LEU GLU HIS VAL THR
SEQRES 17 C 404 PRO GLU GLN ALA GLY ALA HIS PRO THR TYR SER MET GLY
SEQRES 18 C 404 PRO MET ASN THR LEU ASN SER ALA SER LEU VAL ASN LYS
SEQRES 19 C 404 GLY LEU GLU VAL ILE GLU THR HIS LEU LEU PHE GLY ILE
SEQRES 20 C 404 PRO TYR ASP ARG ILE ASP VAL VAL VAL HIS PRO GLN SER
SEQRES 21 C 404 ILE ILE HIS SER MET VAL THR PHE ILE ASP GLY SER THR
SEQRES 22 C 404 ILE ALA GLN ALA SER PRO PRO ASP MET LYS LEU PRO ILE
SEQRES 23 C 404 SER LEU ALA LEU GLY TRP PRO ARG ARG VAL SER GLY ALA
SEQRES 24 C 404 ALA ALA ALA CYS ASP PHE HIS THR ALA SER SER TRP GLU
SEQRES 25 C 404 PHE GLU PRO LEU ASP THR ASP VAL PHE PRO ALA VAL GLU
SEQRES 26 C 404 LEU ALA ARG GLN ALA GLY VAL ALA GLY GLY CYS MET THR
SEQRES 27 C 404 ALA VAL TYR ASN ALA ALA ASN GLU GLU ALA ALA ALA ALA
SEQRES 28 C 404 PHE LEU ALA GLY ARG ILE GLY PHE PRO ALA ILE VAL GLY
SEQRES 29 C 404 ILE ILE ALA ASP VAL LEU HIS ALA ALA ASP GLN TRP ALA
SEQRES 30 C 404 VAL GLU PRO ALA THR VAL ASP ASP VAL LEU ASP ALA GLN
SEQRES 31 C 404 ARG TRP ALA ARG GLU ARG ALA GLN ARG ALA VAL SER GLY
SEQRES 32 C 404 MET
SEQRES 1 D 404 MET HIS HIS HIS HIS HIS HIS LEU VAL ARG PRO ARG GLY
SEQRES 2 D 404 SER HIS MET THR ASN SER THR ASP GLY ARG ALA ASP GLY
SEQRES 3 D 404 ARG LEU ARG VAL VAL VAL LEU GLY SER THR GLY SER ILE
SEQRES 4 D 404 GLY THR GLN ALA LEU GLN VAL ILE ALA ASP ASN PRO ASP
SEQRES 5 D 404 ARG PHE GLU VAL VAL GLY LEU ALA ALA GLY GLY ALA HIS
SEQRES 6 D 404 LEU ASP THR LEU LEU ARG GLN ARG ALA GLN THR GLY VAL
SEQRES 7 D 404 THR ASN ILE ALA VAL ALA ASP GLU HIS ALA ALA GLN ARG
SEQRES 8 D 404 VAL GLY ASP ILE PRO TYR HIS GLY SER ASP ALA ALA THR
SEQRES 9 D 404 ARG LEU VAL GLU GLN THR GLU ALA ASP VAL VAL LEU ASN
SEQRES 10 D 404 ALA LEU VAL GLY ALA LEU GLY LEU ARG PRO THR LEU ALA
SEQRES 11 D 404 ALA LEU LYS THR GLY ALA ARG LEU ALA LEU ALA ASN LYS
SEQRES 12 D 404 GLU SER LEU VAL ALA GLY GLY SER LEU VAL LEU ARG ALA
SEQRES 13 D 404 ALA ARG PRO GLY GLN ILE VAL PRO VAL ASP SER GLU HIS
SEQRES 14 D 404 SER ALA LEU ALA GLN CYS LEU ARG GLY GLY THR PRO ASP
SEQRES 15 D 404 GLU VAL ALA LYS LEU VAL LEU THR ALA SER GLY GLY PRO
SEQRES 16 D 404 PHE ARG GLY TRP SER ALA ALA ASP LEU GLU HIS VAL THR
SEQRES 17 D 404 PRO GLU GLN ALA GLY ALA HIS PRO THR TYR SER MET GLY
SEQRES 18 D 404 PRO MET ASN THR LEU ASN SER ALA SER LEU VAL ASN LYS
SEQRES 19 D 404 GLY LEU GLU VAL ILE GLU THR HIS LEU LEU PHE GLY ILE
SEQRES 20 D 404 PRO TYR ASP ARG ILE ASP VAL VAL VAL HIS PRO GLN SER
SEQRES 21 D 404 ILE ILE HIS SER MET VAL THR PHE ILE ASP GLY SER THR
SEQRES 22 D 404 ILE ALA GLN ALA SER PRO PRO ASP MET LYS LEU PRO ILE
SEQRES 23 D 404 SER LEU ALA LEU GLY TRP PRO ARG ARG VAL SER GLY ALA
SEQRES 24 D 404 ALA ALA ALA CYS ASP PHE HIS THR ALA SER SER TRP GLU
SEQRES 25 D 404 PHE GLU PRO LEU ASP THR ASP VAL PHE PRO ALA VAL GLU
SEQRES 26 D 404 LEU ALA ARG GLN ALA GLY VAL ALA GLY GLY CYS MET THR
SEQRES 27 D 404 ALA VAL TYR ASN ALA ALA ASN GLU GLU ALA ALA ALA ALA
SEQRES 28 D 404 PHE LEU ALA GLY ARG ILE GLY PHE PRO ALA ILE VAL GLY
SEQRES 29 D 404 ILE ILE ALA ASP VAL LEU HIS ALA ALA ASP GLN TRP ALA
SEQRES 30 D 404 VAL GLU PRO ALA THR VAL ASP ASP VAL LEU ASP ALA GLN
SEQRES 31 D 404 ARG TRP ALA ARG GLU ARG ALA GLN ARG ALA VAL SER GLY
SEQRES 32 D 404 MET
HET FOM A 500 11
HET MN A 501 1
HET NDP A 502 48
HET FOM B 500 11
HET MN B 501 1
HET NDP B 502 48
HET FOM C 500 11
HET MN C 501 1
HET NDP C 502 48
HET FOM D 500 11
HET MN D 501 1
HET NDP D 502 48
HETNAM FOM 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID
HETNAM MN MANGANESE (II) ION
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETSYN FOM FOSMIDOMYCIN
FORMUL 5 FOM 4(C4 H10 N O5 P)
FORMUL 6 MN 4(MN 2+)
FORMUL 7 NDP 4(C21 H30 N7 O17 P3)
FORMUL 17 HOH *1671(H2 O)
HELIX 1 1 GLY A 22 ASN A 35 1 14
HELIX 2 2 HIS A 50 GLY A 62 1 13
HELIX 3 3 ASP A 70 GLY A 78 1 9
HELIX 4 4 ASP A 86 GLN A 94 1 9
HELIX 5 5 GLY A 106 LEU A 108 5 3
HELIX 6 6 GLY A 109 GLY A 120 1 12
HELIX 7 7 ASN A 127 GLY A 135 1 9
HELIX 8 8 GLY A 135 ALA A 142 1 8
HELIX 9 9 ASP A 151 LEU A 161 1 11
HELIX 10 10 ARG A 162 GLY A 164 5 3
HELIX 11 11 THR A 165 ASP A 167 5 3
HELIX 12 12 SER A 185 GLU A 190 1 6
HELIX 13 13 THR A 193 GLY A 198 1 6
HELIX 14 14 GLY A 206 LEU A 216 1 11
HELIX 15 15 LEU A 216 GLY A 231 1 16
HELIX 16 16 PRO A 233 ASP A 235 5 3
HELIX 17 17 MET A 267 TRP A 277 1 11
HELIX 18 18 PRO A 307 GLY A 319 1 13
HELIX 19 19 CYS A 321 ALA A 339 1 19
HELIX 20 20 PRO A 345 ALA A 357 1 13
HELIX 21 21 ALA A 358 VAL A 363 5 6
HELIX 22 22 THR A 367 SER A 387 1 21
HELIX 23 23 GLY B 22 ASN B 35 1 14
HELIX 24 24 HIS B 50 GLY B 62 1 13
HELIX 25 25 ASP B 70 GLY B 78 1 9
HELIX 26 26 ASP B 86 GLN B 94 1 9
HELIX 27 27 GLY B 106 LEU B 108 5 3
HELIX 28 28 GLY B 109 GLY B 120 1 12
HELIX 29 29 ASN B 127 GLY B 135 1 9
HELIX 30 30 GLY B 135 ALA B 142 1 8
HELIX 31 31 ASP B 151 LEU B 161 1 11
HELIX 32 32 ARG B 162 GLY B 164 5 3
HELIX 33 33 THR B 165 ASP B 167 5 3
HELIX 34 34 SER B 185 GLU B 190 1 6
HELIX 35 35 GLU B 195 ALA B 199 5 5
HELIX 36 36 GLY B 206 LEU B 216 1 11
HELIX 37 37 LEU B 216 GLY B 231 1 16
HELIX 38 38 PRO B 233 ASP B 235 5 3
HELIX 39 39 MET B 267 TRP B 277 1 11
HELIX 40 40 PRO B 307 GLY B 319 1 13
HELIX 41 41 CYS B 321 ALA B 339 1 19
HELIX 42 42 PRO B 345 ALA B 357 1 13
HELIX 43 43 ALA B 358 ALA B 362 5 5
HELIX 44 44 THR B 367 GLY B 388 1 22
HELIX 45 45 GLY C 22 ASN C 35 1 14
HELIX 46 46 HIS C 50 GLY C 62 1 13
HELIX 47 47 ASP C 70 GLY C 78 1 9
HELIX 48 48 ASP C 86 GLN C 94 1 9
HELIX 49 49 GLY C 106 LEU C 108 5 3
HELIX 50 50 GLY C 109 GLY C 120 1 12
HELIX 51 51 ASN C 127 GLY C 135 1 9
HELIX 52 52 GLY C 135 ALA C 142 1 8
HELIX 53 53 ASP C 151 LEU C 161 1 11
HELIX 54 54 ARG C 162 GLY C 164 5 3
HELIX 55 55 THR C 165 ASP C 167 5 3
HELIX 56 56 SER C 185 GLU C 190 1 6
HELIX 57 57 THR C 193 GLY C 198 1 6
HELIX 58 58 GLY C 206 LEU C 216 1 11
HELIX 59 59 LEU C 216 GLY C 231 1 16
HELIX 60 60 PRO C 233 ASP C 235 5 3
HELIX 61 61 MET C 267 TRP C 277 1 11
HELIX 62 62 PRO C 307 GLY C 319 1 13
HELIX 63 63 CYS C 321 ALA C 339 1 19
HELIX 64 64 PRO C 345 ALA C 357 1 13
HELIX 65 65 ALA C 358 VAL C 363 5 6
HELIX 66 66 THR C 367 GLY C 388 1 22
HELIX 67 67 GLY D 22 ASN D 35 1 14
HELIX 68 68 HIS D 50 GLY D 62 1 13
HELIX 69 69 ASP D 70 GLY D 78 1 9
HELIX 70 70 ASP D 86 THR D 95 1 10
HELIX 71 71 GLY D 106 LEU D 108 5 3
HELIX 72 72 GLY D 109 GLY D 120 1 12
HELIX 73 73 ASN D 127 GLY D 135 1 9
HELIX 74 74 GLY D 135 ALA D 141 1 7
HELIX 75 75 ASP D 151 LEU D 161 1 11
HELIX 76 76 ARG D 162 GLY D 164 5 3
HELIX 77 77 THR D 165 ASP D 167 5 3
HELIX 78 78 SER D 185 GLU D 190 1 6
HELIX 79 79 THR D 193 GLY D 198 1 6
HELIX 80 80 GLY D 206 LEU D 216 1 11
HELIX 81 81 LEU D 216 GLY D 231 1 16
HELIX 82 82 PRO D 233 ASP D 235 5 3
HELIX 83 83 MET D 267 TRP D 277 1 11
HELIX 84 84 PRO D 307 GLY D 319 1 13
HELIX 85 85 CYS D 321 ALA D 339 1 19
HELIX 86 86 PRO D 345 ALA D 357 1 13
HELIX 87 87 ALA D 358 ALA D 362 5 5
HELIX 88 88 THR D 367 GLY D 388 1 22
SHEET 1 A 7 TYR A 82 HIS A 83 0
SHEET 2 A 7 ILE A 66 VAL A 68 1 N VAL A 68 O TYR A 82
SHEET 3 A 7 PHE A 39 ALA A 46 1 N ALA A 46 O ALA A 67
SHEET 4 A 7 LEU A 13 LEU A 18 1 N VAL A 15 O GLU A 40
SHEET 5 A 7 VAL A 99 ASN A 102 1 O LEU A 101 N VAL A 16
SHEET 6 A 7 ARG A 122 LEU A 125 1 O ARG A 122 N VAL A 100
SHEET 7 A 7 ILE A 147 PRO A 149 1 O VAL A 148 N LEU A 123
SHEET 1 B 8 ILE A 237 VAL A 241 0
SHEET 2 B 8 VAL A 169 ALA A 176 1 N LEU A 172 O ASP A 238
SHEET 3 B 8 ILE A 247 PHE A 253 -1 O MET A 250 N VAL A 173
SHEET 4 B 8 THR A 258 ALA A 262 -1 O ILE A 259 N VAL A 251
SHEET 5 B 8 THR B 258 ALA B 262 -1 O ALA B 260 N ALA A 260
SHEET 6 B 8 ILE B 247 PHE B 253 -1 N HIS B 248 O GLN B 261
SHEET 7 B 8 VAL B 169 ALA B 176 -1 N VAL B 173 O MET B 250
SHEET 8 B 8 ILE B 237 VAL B 241 1 O ASP B 238 N LEU B 174
SHEET 1 C 2 SER A 294 PHE A 298 0
SHEET 2 C 2 SER B 294 PHE B 298 -1 O TRP B 296 N TRP A 296
SHEET 1 D 7 TYR B 82 HIS B 83 0
SHEET 2 D 7 ILE B 66 VAL B 68 1 N VAL B 68 O TYR B 82
SHEET 3 D 7 PHE B 39 ALA B 46 1 N LEU B 44 O ALA B 67
SHEET 4 D 7 LEU B 13 LEU B 18 1 N VAL B 15 O GLU B 40
SHEET 5 D 7 VAL B 99 ASN B 102 1 O LEU B 101 N VAL B 16
SHEET 6 D 7 ARG B 122 LEU B 125 1 O ARG B 122 N VAL B 100
SHEET 7 D 7 ILE B 147 PRO B 149 1 O VAL B 148 N LEU B 123
SHEET 1 E 7 TYR C 82 HIS C 83 0
SHEET 2 E 7 ILE C 66 VAL C 68 1 N VAL C 68 O TYR C 82
SHEET 3 E 7 PHE C 39 ALA C 46 1 N LEU C 44 O ALA C 67
SHEET 4 E 7 LEU C 13 LEU C 18 1 N VAL C 15 O GLU C 40
SHEET 5 E 7 VAL C 99 ASN C 102 1 O LEU C 101 N VAL C 16
SHEET 6 E 7 ARG C 122 LEU C 125 1 O ARG C 122 N VAL C 100
SHEET 7 E 7 ILE C 147 PRO C 149 1 O VAL C 148 N LEU C 123
SHEET 1 F 8 ILE C 237 VAL C 241 0
SHEET 2 F 8 VAL C 169 ALA C 176 1 N LEU C 174 O ASP C 238
SHEET 3 F 8 ILE C 247 PHE C 253 -1 O MET C 250 N VAL C 173
SHEET 4 F 8 THR C 258 ALA C 262 -1 O GLN C 261 N HIS C 248
SHEET 5 F 8 THR D 258 ALA D 262 -1 O ALA D 262 N THR C 258
SHEET 6 F 8 ILE D 247 PHE D 253 -1 N HIS D 248 O GLN D 261
SHEET 7 F 8 VAL D 169 ALA D 176 -1 N VAL D 173 O MET D 250
SHEET 8 F 8 ILE D 237 VAL D 241 1 O ASP D 238 N LEU D 172
SHEET 1 G 2 SER C 294 PHE C 298 0
SHEET 2 G 2 SER D 294 PHE D 298 -1 O PHE D 298 N SER C 294
SHEET 1 H 7 TYR D 82 HIS D 83 0
SHEET 2 H 7 ILE D 66 VAL D 68 1 N VAL D 68 O TYR D 82
SHEET 3 H 7 PHE D 39 ALA D 46 1 N LEU D 44 O ALA D 67
SHEET 4 H 7 LEU D 13 LEU D 18 1 N VAL D 15 O GLU D 40
SHEET 5 H 7 VAL D 99 ASN D 102 1 O LEU D 101 N VAL D 16
SHEET 6 H 7 ARG D 122 LEU D 125 1 O ARG D 122 N VAL D 100
SHEET 7 H 7 ILE D 147 PRO D 149 1 O VAL D 148 N LEU D 123
LINK OD1 ASP A 151 MN MN A 501 1555 1555 2.01
LINK OE1 GLU A 153 MN MN A 501 1555 1555 2.12
LINK OE2 GLU A 222 MN MN A 501 1555 1555 2.07
LINK O2 FOM A 500 MN MN A 501 1555 1555 1.91
LINK O1 FOM A 500 MN MN A 501 1555 1555 2.24
LINK OD2 ASP B 151 MN MN B 501 1555 1555 2.05
LINK OE1 GLU B 153 MN MN B 501 1555 1555 2.09
LINK OE2 GLU B 222 MN MN B 501 1555 1555 2.12
LINK O2 FOM B 500 MN MN B 501 1555 1555 2.06
LINK O1 FOM B 500 MN MN B 501 1555 1555 2.21
LINK OD1 ASP C 151 MN MN C 501 1555 1555 2.00
LINK OE1 GLU C 153 MN MN C 501 1555 1555 2.13
LINK OE2 GLU C 222 MN MN C 501 1555 1555 2.19
LINK O2 FOM C 500 MN MN C 501 1555 1555 2.20
LINK N1 FOM C 500 MN MN C 501 1555 1555 2.43
LINK OD2 ASP D 151 MN MN D 501 1555 1555 1.94
LINK OE1 GLU D 153 MN MN D 501 1555 1555 2.11
LINK OE2 GLU D 222 MN MN D 501 1555 1555 2.07
LINK O2 FOM D 500 MN MN D 501 1555 1555 2.01
LINK O1 FOM D 500 MN MN D 501 1555 1555 2.23
LINK N1 FOM D 500 MN MN D 501 1555 1555 2.74
CISPEP 1 TRP A 277 PRO A 278 0 5.15
CISPEP 2 TRP B 277 PRO B 278 0 3.35
CISPEP 3 TRP C 277 PRO C 278 0 5.79
CISPEP 4 TRP D 277 PRO D 278 0 4.96
SITE 1 AC1 17 ASP A 151 SER A 152 GLU A 153 ALA A 176
SITE 2 AC1 17 SER A 177 HIS A 200 TYR A 203 MET A 205
SITE 3 AC1 17 SER A 213 ASN A 218 LYS A 219 GLU A 222
SITE 4 AC1 17 MN A 501 NDP A 502 HOH A 610 HOH A 612
SITE 5 AC1 17 HOH A 614
SITE 1 AC2 4 ASP A 151 GLU A 153 GLU A 222 FOM A 500
SITE 1 AC3 39 GLY A 19 THR A 21 GLY A 22 SER A 23
SITE 2 AC3 39 ILE A 24 ALA A 46 GLY A 47 GLY A 48
SITE 3 AC3 39 ALA A 49 HIS A 50 ALA A 69 ALA A 103
SITE 4 AC3 39 LEU A 104 VAL A 105 LEU A 108 ALA A 126
SITE 5 AC3 39 ASN A 127 LYS A 128 GLU A 129 ASP A 151
SITE 6 AC3 39 MET A 205 GLY A 206 ASN A 209 MET A 267
SITE 7 AC3 39 FOM A 500 HOH A 603 HOH A 622 HOH A 632
SITE 8 AC3 39 HOH A 634 HOH A 636 HOH A 637 HOH A 643
SITE 9 AC3 39 HOH A 661 HOH A 665 HOH A 697 HOH A 710
SITE 10 AC3 39 HOH A 742 HOH A 755 HOH A 793
SITE 1 AC4 17 ASP B 151 SER B 152 GLU B 153 ALA B 176
SITE 2 AC4 17 SER B 177 HIS B 200 TYR B 203 MET B 205
SITE 3 AC4 17 SER B 213 ASN B 218 LYS B 219 GLU B 222
SITE 4 AC4 17 MN B 501 NDP B 502 HOH B 602 HOH B 628
SITE 5 AC4 17 HOH B 634
SITE 1 AC5 4 ASP B 151 GLU B 153 GLU B 222 FOM B 500
SITE 1 AC6 36 GLY B 19 THR B 21 GLY B 22 SER B 23
SITE 2 AC6 36 ILE B 24 ALA B 46 GLY B 47 GLY B 48
SITE 3 AC6 36 ALA B 49 HIS B 50 ALA B 69 ALA B 103
SITE 4 AC6 36 LEU B 104 ALA B 126 ASN B 127 LYS B 128
SITE 5 AC6 36 GLU B 129 ASP B 151 MET B 205 GLY B 206
SITE 6 AC6 36 ASN B 209 MET B 267 FOM B 500 HOH B 610
SITE 7 AC6 36 HOH B 630 HOH B 632 HOH B 636 HOH B 643
SITE 8 AC6 36 HOH B 654 HOH B 673 HOH B 742 HOH B 779
SITE 9 AC6 36 HOH B 823 HOH B 840 HOH B 872 HOH B 927
SITE 1 AC7 17 ASP C 151 SER C 152 GLU C 153 ALA C 176
SITE 2 AC7 17 SER C 177 HIS C 200 TYR C 203 SER C 213
SITE 3 AC7 17 ASN C 218 LYS C 219 GLU C 222 MET C 267
SITE 4 AC7 17 MN C 501 NDP C 502 HOH C 603 HOH C 615
SITE 5 AC7 17 HOH C 631
SITE 1 AC8 5 LYS C 128 ASP C 151 GLU C 153 GLU C 222
SITE 2 AC8 5 FOM C 500
SITE 1 AC9 37 GLY C 19 THR C 21 GLY C 22 SER C 23
SITE 2 AC9 37 ILE C 24 ALA C 46 GLY C 47 GLY C 48
SITE 3 AC9 37 ALA C 49 HIS C 50 ALA C 69 ALA C 103
SITE 4 AC9 37 LEU C 104 LEU C 108 ALA C 126 ASN C 127
SITE 5 AC9 37 LYS C 128 GLU C 129 ASP C 151 MET C 205
SITE 6 AC9 37 GLY C 206 PRO C 207 ASN C 209 MET C 267
SITE 7 AC9 37 FOM C 500 HOH C 613 HOH C 625 HOH C 632
SITE 8 AC9 37 HOH C 634 HOH C 647 HOH C 651 HOH C 655
SITE 9 AC9 37 HOH C 680 HOH C 801 HOH C 804 HOH C 840
SITE 10 AC9 37 HOH C 940
SITE 1 BC1 18 LYS D 128 ASP D 151 SER D 152 GLU D 153
SITE 2 BC1 18 ALA D 176 SER D 177 HIS D 200 TYR D 203
SITE 3 BC1 18 MET D 205 SER D 213 ASN D 218 LYS D 219
SITE 4 BC1 18 GLU D 222 MN D 501 NDP D 502 HOH D 610
SITE 5 BC1 18 HOH D 613 HOH D 636
SITE 1 BC2 4 ASP D 151 GLU D 153 GLU D 222 FOM D 500
SITE 1 BC3 37 GLY D 19 THR D 21 GLY D 22 SER D 23
SITE 2 BC3 37 ILE D 24 ALA D 46 GLY D 47 GLY D 48
SITE 3 BC3 37 ALA D 49 HIS D 50 ALA D 69 ALA D 103
SITE 4 BC3 37 LEU D 104 ALA D 126 ASN D 127 LYS D 128
SITE 5 BC3 37 GLU D 129 ASP D 151 MET D 205 GLY D 206
SITE 6 BC3 37 ASN D 209 MET D 267 FOM D 500 HOH D 614
SITE 7 BC3 37 HOH D 615 HOH D 622 HOH D 643 HOH D 647
SITE 8 BC3 37 HOH D 681 HOH D 719 HOH D 752 HOH D 765
SITE 9 BC3 37 HOH D 863 HOH D 881 HOH D 888 HOH D 898
SITE 10 BC3 37 HOH D 947
CRYST1 112.270 114.240 133.187 90.00 90.00 90.00 P 21 21 21 16
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 0.008907 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008754 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007508 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
