HEADER TRANSFERASE 11-JUN-09 3HT0
TITLE CRYSTAL STRUCTURE OF E. COLI HPPK(F123A) IN COMPLEX WITH MGAMPCPP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HPPK;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE, 2-
COMPND 5 AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE, 6-
COMPND 6 HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE, PPPK;
COMPND 7 EC: 2.7.6.3;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K 12;
SOURCE 5 GENE: B0142, FOIK, FOLK, JW0138;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS ALPHA BETA, ATP-BINDING, FOLATE BIOSYNTHESIS, KINASE, NUCLEOTIDE-
KEYWDS 2 BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BLASZCZYK,Y.LI,H.YAN,X.JI
REVDAT 5 06-SEP-23 3HT0 1 REMARK
REVDAT 4 30-AUG-23 3HT0 1 AUTHOR JRNL
REVDAT 3 13-OCT-21 3HT0 1 REMARK SEQADV LINK
REVDAT 2 01-NOV-17 3HT0 1 REMARK
REVDAT 1 23-JUN-10 3HT0 0
JRNL AUTH Y.LI,J.BLASZCZYK,X.JI,H.YAN
JRNL TITL PTERIN-BINDING SITE MUTATION Y53A, N55A OR F123A AND
JRNL TITL 2 ACTIVITY OF E. COLI HPPK
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.XIAO,G.SHI,J.GAO,J.BLASZCZYK,Q.LIU,X.JI,H.YAN
REMARK 1 TITL UNUSUAL CONFORMATIONAL CHANGES IN
REMARK 1 TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE AS
REMARK 1 TITL 3 REVEALED BY X-RAY CRYSTALLOGRAPHY AND NMR
REMARK 1 REF J.BIOL.CHEM. V. 276 40274 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11546767
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 29248
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.420
REMARK 3 FREE R VALUE TEST SET COUNT : 1000
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 29.9110 - 2.6750 1.00 4114 146 0.1390 0.1770
REMARK 3 2 2.6750 - 2.1240 1.00 4068 144 0.1240 0.1830
REMARK 3 3 2.1240 - 1.8550 1.00 4042 143 0.1160 0.1640
REMARK 3 4 1.8550 - 1.6860 1.00 4031 143 0.1330 0.2010
REMARK 3 5 1.6860 - 1.5650 1.00 4041 143 0.1600 0.2160
REMARK 3 6 1.5650 - 1.4720 1.00 3995 141 0.1950 0.2950
REMARK 3 7 1.4720 - 1.4000 0.98 3957 140 0.2380 0.2900
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 52.80
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.77000
REMARK 3 B22 (A**2) : 1.39600
REMARK 3 B33 (A**2) : 1.35900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.75300
REMARK 3 B23 (A**2) : 0.00000
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 : 0.005 1410
REMARK 3 ANGLE : 0.912 1937
REMARK 3 CHIRALITY : 0.061 212
REMARK 3 PLANARITY : 0.004 253
REMARK 3 DIHEDRAL : 16.135 555
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: THE STRUCTURE WAS REFINED FOR A TOTAL
REMARK 3 OF 33 CYCLES, INCLUDING 8 CYCLES WITH CNS, 11 CYCLES WITH SHELX,
REMARK 3 AND 14 CYCLES WITH PHENIX
REMARK 4
REMARK 4 3HT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97793
REMARK 200 MONOCHROMATOR : SILICON 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29249
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0080
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.63300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1EQM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, GLYCEROL,
REMARK 280 AMMONIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 479 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 86 -95.49 61.94
REMARK 500 ALA A 86 -72.88 -44.57
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 MG A 161 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD1
REMARK 620 2 ASP A 97 OD1 94.9
REMARK 620 3 APC A 171 O1A 93.6 168.7
REMARK 620 4 APC A 171 O1B 89.1 100.0 87.6
REMARK 620 5 HOH A 201 O 90.3 82.9 89.6 177.1
REMARK 620 6 HOH A 202 O 178.0 83.6 88.1 89.8 90.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 162 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD2
REMARK 620 2 ASP A 97 OD2 94.7
REMARK 620 3 APC A 171 O1B 90.3 95.0
REMARK 620 4 APC A 171 O3G 174.5 90.2 86.8
REMARK 620 5 HOH A 203 O 88.4 88.6 176.3 94.2
REMARK 620 6 HOH A 204 O 85.3 173.4 91.7 90.2 84.7
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 MG A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 191
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EQM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BINARY COMPLEX OF 6-HYDROXYMETHYL-7,8-
REMARK 900 DIHYDROPTERIN PYROPHOSPHOKINASE WITH ADENOSINE-5'-DIPHOSPHATE
REMARK 900 RELATED ID: 3HSD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI HPPK(Y53A)
REMARK 900 RELATED ID: 3HSG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI HPPK(Y53A) IN COMPLEX WITH MGAMPCPP
REMARK 900 RELATED ID: 3HSJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI HPPK(N55A)
REMARK 900 RELATED ID: 3HSZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI HPPK(F123A)
DBREF 3HT0 A 1 158 UNP P26281 HPPK_ECOLI 2 159
SEQADV 3HT0 ALA A 123 UNP P26281 PHE 124 ENGINEERED MUTATION
SEQRES 1 A 158 THR VAL ALA TYR ILE ALA ILE GLY SER ASN LEU ALA SER
SEQRES 2 A 158 PRO LEU GLU GLN VAL ASN ALA ALA LEU LYS ALA LEU GLY
SEQRES 3 A 158 ASP ILE PRO GLU SER HIS ILE LEU THR VAL SER SER PHE
SEQRES 4 A 158 TYR ARG THR PRO PRO LEU GLY PRO GLN ASP GLN PRO ASP
SEQRES 5 A 158 TYR LEU ASN ALA ALA VAL ALA LEU GLU THR SER LEU ALA
SEQRES 6 A 158 PRO GLU GLU LEU LEU ASN HIS THR GLN ARG ILE GLU LEU
SEQRES 7 A 158 GLN GLN GLY ARG VAL ARG LYS ALA GLU ARG TRP GLY PRO
SEQRES 8 A 158 ARG THR LEU ASP LEU ASP ILE MET LEU PHE GLY ASN GLU
SEQRES 9 A 158 VAL ILE ASN THR GLU ARG LEU THR VAL PRO HIS TYR ASP
SEQRES 10 A 158 MET LYS ASN ARG GLY ALA MET LEU TRP PRO LEU PHE GLU
SEQRES 11 A 158 ILE ALA PRO GLU LEU VAL PHE PRO ASP GLY GLU MET LEU
SEQRES 12 A 158 ARG GLN ILE LEU HIS THR ARG ALA PHE ASP LYS LEU ASN
SEQRES 13 A 158 LYS TRP
HET MG A 161 1
HET MG A 162 1
HET APC A 171 31
HET CL A 191 1
HETNAM MG MAGNESIUM ION
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM CL CHLORIDE ION
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 MG 2(MG 2+)
FORMUL 4 APC C11 H18 N5 O12 P3
FORMUL 5 CL CL 1-
FORMUL 6 HOH *271(H2 O)
HELIX 1 1 PRO A 14 ASP A 27 1 14
HELIX 2 2 ALA A 65 GLY A 81 1 17
HELIX 3 3 ASP A 117 ASN A 120 5 4
HELIX 4 4 ARG A 121 ALA A 132 1 12
HELIX 5 5 MET A 142 ALA A 151 1 10
SHEET 1 A 4 SER A 31 VAL A 36 0
SHEET 2 A 4 TYR A 53 THR A 62 -1 O ALA A 59 N LEU A 34
SHEET 3 A 4 VAL A 2 SER A 9 -1 N ALA A 3 O LEU A 60
SHEET 4 A 4 LEU A 94 PHE A 101 -1 O ASP A 97 N ALA A 6
SHEET 1 B 4 SER A 31 VAL A 36 0
SHEET 2 B 4 TYR A 53 THR A 62 -1 O ALA A 59 N LEU A 34
SHEET 3 B 4 TYR A 40 THR A 42 -1 N THR A 42 O TYR A 53
SHEET 4 B 4 ASN A 156 LYS A 157 -1 O ASN A 156 N ARG A 41
SHEET 1 C 2 ARG A 84 LYS A 85 0
SHEET 2 C 2 ARG A 88 TRP A 89 -1 O ARG A 88 N LYS A 85
SHEET 1 D 2 ILE A 106 ASN A 107 0
SHEET 2 D 2 THR A 112 VAL A 113 -1 O VAL A 113 N ILE A 106
LINK OD1 ASP A 95 MG MG A 161 1555 1555 2.16
LINK OD2 ASP A 95 MG MG A 162 1555 1555 2.14
LINK OD1 ASP A 97 MG MG A 161 1555 1555 2.16
LINK OD2 ASP A 97 MG MG A 162 1555 1555 2.12
LINK MG MG A 161 O1A APC A 171 1555 1555 2.16
LINK MG MG A 161 O1B APC A 171 1555 1555 2.15
LINK MG MG A 161 O HOH A 201 1555 1555 2.16
LINK MG MG A 161 O HOH A 202 1555 1555 2.19
LINK MG MG A 162 O1B APC A 171 1555 1555 2.19
LINK MG MG A 162 O3G APC A 171 1555 1555 2.16
LINK MG MG A 162 O HOH A 203 1555 1555 2.19
LINK MG MG A 162 O HOH A 204 1555 1555 2.24
CISPEP 1 VAL A 113 PRO A 114 0 -2.65
SITE 1 AC1 6 ASP A 95 ASP A 97 MG A 162 APC A 171
SITE 2 AC1 6 HOH A 201 HOH A 202
SITE 1 AC2 6 ASP A 95 ASP A 97 MG A 161 APC A 171
SITE 2 AC2 6 HOH A 203 HOH A 204
SITE 1 AC3 30 LYS A 23 LEU A 70 GLN A 74 ARG A 92
SITE 2 AC3 30 ASP A 95 ASP A 97 ILE A 98 ARG A 110
SITE 3 AC3 30 LEU A 111 THR A 112 HIS A 115 TYR A 116
SITE 4 AC3 30 ARG A 121 HIS A 148 MG A 161 MG A 162
SITE 5 AC3 30 HOH A 201 HOH A 202 HOH A 208 HOH A 210
SITE 6 AC3 30 HOH A 212 HOH A 265 HOH A 313 HOH A 318
SITE 7 AC3 30 HOH A 321 HOH A 375 HOH A 379 HOH A 418
SITE 8 AC3 30 HOH A 459 HOH A 461
SITE 1 AC4 4 ARG A 84 TRP A 89 LYS A 157 HOH A 290
CRYST1 80.180 52.240 36.780 90.00 102.63 90.00 C 1 2 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 0.012472 0.000000 0.002795 0.00000
SCALE2 0.000000 0.019144 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027862 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
