HEADER TRANSFERASE, HYDROLASE 08-OCT-12 4HGR
TITLE CRYSTAL STRUCTURE OF E56A/K67A MUTANT OF 2-KETO-3-DEOXY-D-GLYCERO-D-
TITLE 2 GALACTONONONATE-9-PHOSPHATE PHOSPHOHYDROLASE FROM BACTEROIDES
TITLE 3 THETAIOTAOMICRON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLNEURAMINATE CYTIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_COMMON: 2-KETO-3-DEOXY-D-GLYCERO-D-GALACTONONONATE-9-
SOURCE 4 PHOSPHATE PHOSPHOHYDROLASE;
SOURCE 5 ORGANISM_TAXID: 226186;
SOURCE 6 STRAIN: VPI-5482;
SOURCE 7 GENE: BT_1713;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-3A-626
KEYWDS ROSSMANN FOLD, PHOSPHOHYDROYLASE, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.D.DAUGHTRY,K.N.ALLEN
REVDAT 5 20-SEP-23 4HGR 1 REMARK
REVDAT 4 10-FEB-21 4HGR 1 JRNL REMARK SEQADV LINK
REVDAT 3 12-NOV-14 4HGR 1 KEYWDS
REVDAT 2 28-AUG-13 4HGR 1 JRNL
REVDAT 1 21-AUG-13 4HGR 0
JRNL AUTH K.D.DAUGHTRY,H.HUANG,V.MALASHKEVICH,Y.PATSKOVSKY,W.LIU,
JRNL AUTH 2 U.RAMAGOPAL,J.M.SAUDER,S.K.BURLEY,S.C.ALMO,
JRNL AUTH 3 D.DUNAWAY-MARIANO,K.N.ALLEN
JRNL TITL STRUCTURAL BASIS FOR THE DIVERGENCE OF SUBSTRATE SPECIFICITY
JRNL TITL 2 AND BIOLOGICAL FUNCTION WITHIN HAD PHOSPHATASES IN
JRNL TITL 3 LIPOPOLYSACCHARIDE AND SIALIC ACID BIOSYNTHESIS.
JRNL REF BIOCHEMISTRY V. 52 5372 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23848398
JRNL DOI 10.1021/BI400659K
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 76062
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.230
REMARK 3 FREE R VALUE TEST SET COUNT : 3977
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 50.7150 - 5.5634 0.95 3766 203 0.1811 0.2061
REMARK 3 2 5.5634 - 4.4166 0.95 3723 202 0.1572 0.2210
REMARK 3 3 4.4166 - 3.8586 0.95 3741 195 0.1551 0.2070
REMARK 3 4 3.8586 - 3.5059 0.94 3702 223 0.1651 0.1940
REMARK 3 5 3.5059 - 3.2546 0.94 3651 227 0.1747 0.2256
REMARK 3 6 3.2546 - 3.0628 0.95 3744 184 0.1885 0.2359
REMARK 3 7 3.0628 - 2.9094 0.95 3691 178 0.2013 0.2319
REMARK 3 8 2.9094 - 2.7828 0.95 3690 199 0.2005 0.2295
REMARK 3 9 2.7828 - 2.6756 0.95 3698 180 0.1978 0.2387
REMARK 3 10 2.6756 - 2.5833 0.94 3683 194 0.1995 0.2648
REMARK 3 11 2.5833 - 2.5025 0.93 3614 204 0.2095 0.2562
REMARK 3 12 2.5025 - 2.4310 0.92 3595 188 0.2127 0.2890
REMARK 3 13 2.4310 - 2.3670 0.92 3587 167 0.2103 0.2682
REMARK 3 14 2.3670 - 2.3093 0.91 3540 190 0.2129 0.2595
REMARK 3 15 2.3093 - 2.2568 0.91 3558 165 0.2169 0.3353
REMARK 3 16 2.2568 - 2.2087 0.89 3425 212 0.2179 0.2886
REMARK 3 17 2.2087 - 2.1645 0.89 3507 179 0.2157 0.3088
REMARK 3 18 2.1645 - 2.1237 0.89 3421 188 0.2277 0.3173
REMARK 3 19 2.1237 - 2.0858 0.88 3444 177 0.2256 0.2863
REMARK 3 20 2.0858 - 2.0500 0.88 3403 174 0.2329 0.3363
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.48
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 : 0.006 10374
REMARK 3 ANGLE : 0.922 13999
REMARK 3 CHIRALITY : 0.065 1573
REMARK 3 PLANARITY : 0.004 1796
REMARK 3 DIHEDRAL : 14.602 3788
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 4HGR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-10
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : ROTATING-ANODE
REMARK 200 OPTICS : HELIOS MULTI-LAYER OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS PLUS
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76062
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 10.66
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13080
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.78
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47690
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.730
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 3E8M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 150 MM MAGNESIUM
REMARK 280 CHLORIDE, 25% POLYETHYLENE GLYCOL 3350, 3% DIOXANE. THE CRYSTAL
REMARK 280 WAS DRAGGED THROUGH PARATONE PRIOR TO FLASH-COOLING, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 58.38250
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 GLN A 164
REMARK 465 MET B 1
REMARK 465 ILE C 163
REMARK 465 GLN C 164
REMARK 465 MET D 1
REMARK 465 MET F 1
REMARK 465 GLN F 164
REMARK 465 GLN G 164
REMARK 465 MET H 1
REMARK 465 GLN H 164
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 LYS B 150 CG CD CE NZ
REMARK 470 LYS F 150 CG CD CE NZ
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 B 396 O HOH B 398 1.89
REMARK 500 OD1 ASP B 104 O HOH B 391 2.02
REMARK 500 O HOH D 310 O HOH D 350 2.05
REMARK 500 O HOH A 334 O HOH A 337 2.05
REMARK 500 O HOH C 353 O HOH C 385 2.06
REMARK 500 O HOH F 367 O HOH H 305 2.06
REMARK 500 O HOH A 363 O HOH C 371 2.08
REMARK 500 O HOH B 340 O HOH B 397 2.09
REMARK 500 O HOH F 355 O HOH H 329 2.09
REMARK 500 O HOH A 303 O HOH A 337 2.10
REMARK 500 O HOH H 328 O HOH H 360 2.10
REMARK 500 O HOH F 332 O HOH F 368 2.11
REMARK 500 OH TYR C 22 O HOH C 337 2.12
REMARK 500 ND2 ASN D 106 O HOH D 334 2.12
REMARK 500 OE1 GLU E 149 O HOH E 335 2.13
REMARK 500 O HOH E 317 O HOH E 367 2.13
REMARK 500 O HOH D 334 O HOH D 371 2.13
REMARK 500 O HOH C 364 O HOH C 378 2.13
REMARK 500 O HOH E 309 O HOH E 327 2.14
REMARK 500 O ILE H 101 O HOH H 373 2.14
REMARK 500 O HOH B 353 O HOH D 321 2.14
REMARK 500 O HOH A 305 O HOH B 336 2.14
REMARK 500 OD2 ASP B 107 O HOH B 316 2.15
REMARK 500 OE1 GLU A 59 O HOH A 342 2.15
REMARK 500 O HOH G 311 O HOH G 347 2.16
REMARK 500 OD1 ASP H 10 O HOH H 322 2.16
REMARK 500 OE1 GLU F 149 O HOH F 324 2.16
REMARK 500 O HOH D 314 O HOH D 350 2.16
REMARK 500 O HOH G 343 O HOH G 373 2.17
REMARK 500 OE2 GLU A 146 NZ LYS A 150 2.17
REMARK 500 O HOH D 350 O HOH D 396 2.17
REMARK 500 NH2 ARG D 145 O HOH B 391 2.17
REMARK 500 OD1 ASP A 17 O HOH A 331 2.18
REMARK 500 O HOH E 321 O HOH E 328 2.18
REMARK 500 O HOH A 312 O HOH A 328 2.18
REMARK 500 O ALA H 123 O HOH H 369 2.19
REMARK 500 O HOH B 396 O HOH B 397 2.19
REMARK 500 OD1 ASP B 12 O HOH B 302 2.19
REMARK 500 O HOH C 353 O HOH C 381 2.19
REMARK 500 O HOH D 330 O HOH D 370 2.19
REMARK 500 O HOH F 350 O HOH F 370 2.19
REMARK 500 O HOH C 361 O HOH C 389 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 B 359 O HOH D 381 2646 2.05
REMARK 500 O HOH D 369 O HOH H 363 1455 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 ILE A 11 -73.98 -105.39
REMARK 500 VAL A 14 -61.09 -124.20
REMARK 500 ASN A 155 -166.93 -124.65
REMARK 500 ILE B 11 -69.77 -103.78
REMARK 500 VAL B 14 -64.95 -120.95
REMARK 500 ASP B 23 -161.99 -104.12
REMARK 500 ASP B 79 78.98 -119.36
REMARK 500 ILE C 11 -66.96 -105.36
REMARK 500 ASN C 155 -169.18 -109.51
REMARK 500 ILE D 11 -77.09 -104.80
REMARK 500 ASP D 103 -3.29 -145.19
REMARK 500 ILE D 163 51.88 -105.70
REMARK 500 LYS E 2 -179.90 -66.93
REMARK 500 ILE E 11 -68.01 -106.58
REMARK 500 LEU E 91 -11.04 -141.00
REMARK 500 ILE F 11 -65.38 -100.55
REMARK 500 VAL F 14 -61.32 -120.26
REMARK 500 ASP F 23 -163.83 -105.01
REMARK 500 ILE G 11 -69.20 -96.10
REMARK 500 ASP G 23 -169.92 -104.11
REMARK 500 ILE H 11 -67.78 -100.13
REMARK 500 VAL H 14 -59.12 -120.60
REMARK 500 ASP H 103 -4.45 -140.45
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 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 10 OD2
REMARK 620 2 ASP A 12 O 81.1
REMARK 620 3 ASP A 103 OD1 81.3 80.5
REMARK 620 4 HOH A 301 O 163.4 86.0 86.4
REMARK 620 5 HOH A 302 O 96.0 171.5 91.2 95.2
REMARK 620 6 HOH A 327 O 87.1 111.8 161.6 107.5 75.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 10 OD2
REMARK 620 2 ASP B 12 O 82.3
REMARK 620 3 ASP B 103 OD1 82.1 82.5
REMARK 620 4 HOH B 301 O 158.9 84.8 79.7
REMARK 620 5 HOH B 316 O 88.5 163.7 82.9 99.7
REMARK 620 6 HOH B 396 O 77.3 104.5 157.0 122.3 86.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 10 OD2
REMARK 620 2 ASP C 12 O 88.4
REMARK 620 3 ASP C 103 OD1 86.9 89.5
REMARK 620 4 HOH C 302 O 161.1 72.8 90.9
REMARK 620 5 HOH C 303 O 86.7 173.9 93.8 112.2
REMARK 620 6 HOH C 369 O 91.6 87.4 176.6 89.5 89.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 10 OD2
REMARK 620 2 ASP D 12 O 95.6
REMARK 620 3 ASP D 103 OD1 85.1 96.4
REMARK 620 4 HOH D 308 O 80.4 176.0 83.2
REMARK 620 5 HOH D 312 O 100.5 99.8 162.2 81.2
REMARK 620 6 HOH D 398 O 175.0 82.3 90.6 101.7 84.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 10 OD2
REMARK 620 2 ASP E 10 OD1 49.3
REMARK 620 3 ASP E 12 O 79.0 112.2
REMARK 620 4 HOH E 301 O 115.3 161.9 67.9
REMARK 620 5 HOH E 316 O 98.7 50.6 145.1 139.0
REMARK 620 6 HOH E 342 O 66.7 87.1 112.1 76.6 98.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 10 OD2
REMARK 620 2 ASP F 12 O 86.2
REMARK 620 3 ASP F 103 OD1 79.1 86.9
REMARK 620 4 HOH F 301 O 168.1 87.6 110.6
REMARK 620 5 HOH F 302 O 75.8 160.9 95.8 108.9
REMARK 620 6 HOH F 352 O 79.3 96.5 157.9 91.4 74.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 10 OD2
REMARK 620 2 ASP G 12 O 86.1
REMARK 620 3 ASP G 103 OD1 75.4 83.9
REMARK 620 4 HOH G 302 O 162.5 97.5 87.9
REMARK 620 5 HOH G 303 O 83.2 167.1 86.5 90.8
REMARK 620 6 HOH G 320 O 84.3 110.2 154.5 110.1 75.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 10 OD2
REMARK 620 2 ASP H 12 O 85.7
REMARK 620 3 ASP H 103 OD1 86.6 79.3
REMARK 620 4 HOH H 315 O 100.1 167.3 89.7
REMARK 620 5 HOH H 322 O 75.3 113.4 156.5 79.2
REMARK 620 6 HOH H 324 O 166.4 81.5 86.3 91.5 114.3
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E8M RELATED DB: PDB
REMARK 900 RELATED ID: 4HGN RELATED DB: PDB
REMARK 900 RELATED ID: 4HGO RELATED DB: PDB
REMARK 900 RELATED ID: 4HGP RELATED DB: PDB
REMARK 900 RELATED ID: 4HGQ RELATED DB: PDB
DBREF 4HGR A 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR B 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR C 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR D 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR E 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR F 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR G 1 164 UNP Q8A712 Q8A712_BACTN 1 164
DBREF 4HGR H 1 164 UNP Q8A712 Q8A712_BACTN 1 164
SEQADV 4HGR ALA A 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA A 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA B 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA B 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA C 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA C 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA D 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA D 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA E 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA E 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA F 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA F 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA G 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA G 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQADV 4HGR ALA H 56 UNP Q8A712 GLU 56 ENGINEERED MUTATION
SEQADV 4HGR ALA H 67 UNP Q8A712 LYS 67 ENGINEERED MUTATION
SEQRES 1 A 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 A 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 A 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 A 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 A 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 A 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 A 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 A 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 A 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 A 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 A 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 A 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 A 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 B 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 B 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 B 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 B 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 B 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 B 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 B 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 B 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 B 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 B 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 B 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 B 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 B 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 C 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 C 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 C 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 C 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 C 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 C 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 C 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 C 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 C 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 C 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 C 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 C 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 C 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 D 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 D 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 D 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 D 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 D 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 D 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 D 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 D 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 D 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 D 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 D 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 D 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 D 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 E 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 E 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 E 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 E 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 E 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 E 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 E 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 E 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 E 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 E 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 E 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 E 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 E 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 F 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 F 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 F 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 F 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 F 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 F 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 F 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 F 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 F 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 F 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 F 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 F 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 F 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 G 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 G 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 G 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 G 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 G 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 G 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 G 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 G 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 G 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 G 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 G 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 G 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 G 164 GLU ASP PHE ILE ALA VAL ILE GLN
SEQRES 1 H 164 MET LYS GLU ILE LYS LEU ILE LEU THR ASP ILE ASP GLY
SEQRES 2 H 164 VAL TRP THR ASP GLY GLY MET PHE TYR ASP GLN THR GLY
SEQRES 3 H 164 ASN GLU TRP LYS LYS PHE ASN THR SER ASP SER ALA GLY
SEQRES 4 H 164 ILE PHE TRP ALA HIS ASN LYS GLY ILE PRO VAL GLY ILE
SEQRES 5 H 164 LEU THR GLY ALA LYS THR GLU ILE VAL ARG ARG ARG ALA
SEQRES 6 H 164 GLU ALA LEU LYS VAL ASP TYR LEU PHE GLN GLY VAL VAL
SEQRES 7 H 164 ASP LYS LEU SER ALA ALA GLU GLU LEU CYS ASN GLU LEU
SEQRES 8 H 164 GLY ILE ASN LEU GLU GLN VAL ALA TYR ILE GLY ASP ASP
SEQRES 9 H 164 LEU ASN ASP ALA LYS LEU LEU LYS ARG VAL GLY ILE ALA
SEQRES 10 H 164 GLY VAL PRO ALA SER ALA PRO PHE TYR ILE ARG ARG LEU
SEQRES 11 H 164 SER THR ILE PHE LEU GLU LYS ARG GLY GLY GLU GLY VAL
SEQRES 12 H 164 PHE ARG GLU PHE VAL GLU LYS VAL LEU GLY ILE ASN LEU
SEQRES 13 H 164 GLU ASP PHE ILE ALA VAL ILE GLN
HET MG A 201 1
HET MG B 201 1
HET MG C 201 1
HET MG D 201 1
HET MG E 201 1
HET MG F 201 1
HET MG G 201 1
HET MG H 201 1
HETNAM MG MAGNESIUM ION
FORMUL 9 MG 8(MG 2+)
FORMUL 17 HOH *700(H2 O)
HELIX 1 1 ASP A 36 LYS A 46 1 11
HELIX 2 2 THR A 58 LEU A 68 1 11
HELIX 3 3 ASP A 79 GLY A 92 1 14
HELIX 4 4 ASN A 94 GLU A 96 5 3
HELIX 5 5 ASP A 104 ASN A 106 5 3
HELIX 6 6 ASP A 107 LYS A 112 1 6
HELIX 7 7 PRO A 124 ARG A 129 1 6
HELIX 8 8 GLY A 142 LEU A 152 1 11
HELIX 9 9 ASN A 155 ILE A 163 1 9
HELIX 10 10 ASP B 36 LYS B 46 1 11
HELIX 11 11 THR B 58 LEU B 68 1 11
HELIX 12 12 ASP B 79 GLY B 92 1 14
HELIX 13 13 ASN B 94 GLU B 96 5 3
HELIX 14 14 ASP B 104 ASN B 106 5 3
HELIX 15 15 ASP B 107 LYS B 112 1 6
HELIX 16 16 PRO B 124 ARG B 129 1 6
HELIX 17 17 GLY B 142 LEU B 152 1 11
HELIX 18 18 ASN B 155 ILE B 163 1 9
HELIX 19 19 ASP C 36 LYS C 46 1 11
HELIX 20 20 THR C 58 LEU C 68 1 11
HELIX 21 21 ASP C 79 GLY C 92 1 14
HELIX 22 22 ASN C 94 GLU C 96 5 3
HELIX 23 23 ASP C 104 ASN C 106 5 3
HELIX 24 24 ASP C 107 LYS C 112 1 6
HELIX 25 25 PRO C 124 ARG C 129 1 6
HELIX 26 26 GLY C 142 GLY C 153 1 12
HELIX 27 27 ASN C 155 VAL C 162 1 8
HELIX 28 28 ASP D 36 LYS D 46 1 11
HELIX 29 29 THR D 58 LEU D 68 1 11
HELIX 30 30 ASP D 79 GLY D 92 1 14
HELIX 31 31 ASN D 94 GLU D 96 5 3
HELIX 32 32 ASP D 104 ASN D 106 5 3
HELIX 33 33 ASP D 107 LYS D 112 1 6
HELIX 34 34 PRO D 124 ARG D 129 1 6
HELIX 35 35 GLY D 142 LEU D 152 1 11
HELIX 36 36 ASN D 155 ILE D 163 1 9
HELIX 37 37 ASP E 36 LYS E 46 1 11
HELIX 38 38 THR E 58 LEU E 68 1 11
HELIX 39 39 ASP E 79 GLU E 90 1 12
HELIX 40 40 ASN E 94 GLU E 96 5 3
HELIX 41 41 ASP E 104 ASN E 106 5 3
HELIX 42 42 ASP E 107 LYS E 112 1 6
HELIX 43 43 PRO E 124 ARG E 129 1 6
HELIX 44 44 GLY E 142 LEU E 152 1 11
HELIX 45 45 ASN E 155 ILE E 163 1 9
HELIX 46 46 SER F 35 LYS F 46 1 12
HELIX 47 47 THR F 58 LEU F 68 1 11
HELIX 48 48 ASP F 79 GLY F 92 1 14
HELIX 49 49 ASN F 94 GLU F 96 5 3
HELIX 50 50 ASP F 104 ASN F 106 5 3
HELIX 51 51 ASP F 107 VAL F 114 1 8
HELIX 52 52 PRO F 124 ARG F 129 1 6
HELIX 53 53 GLY F 142 LEU F 152 1 11
HELIX 54 54 ASN F 155 ILE F 163 1 9
HELIX 55 55 ASP G 36 LYS G 46 1 11
HELIX 56 56 THR G 58 LEU G 68 1 11
HELIX 57 57 ASP G 79 GLY G 92 1 14
HELIX 58 58 ASN G 94 GLU G 96 5 3
HELIX 59 59 ASP G 104 ASN G 106 5 3
HELIX 60 60 ASP G 107 LYS G 112 1 6
HELIX 61 61 PRO G 124 ARG G 129 1 6
HELIX 62 62 GLY G 142 LEU G 152 1 11
HELIX 63 63 ASN G 155 ILE G 163 1 9
HELIX 64 64 ASP H 36 LYS H 46 1 11
HELIX 65 65 THR H 58 LEU H 68 1 11
HELIX 66 66 ASP H 79 GLY H 92 1 14
HELIX 67 67 ASN H 94 GLU H 96 5 3
HELIX 68 68 ASP H 104 ASN H 106 5 3
HELIX 69 69 ASP H 107 LYS H 112 1 6
HELIX 70 70 PRO H 124 ARG H 129 1 6
HELIX 71 71 GLY H 142 GLY H 153 1 12
HELIX 72 72 ASN H 155 ILE H 163 1 9
SHEET 1 A 5 TYR A 72 GLN A 75 0
SHEET 2 A 5 VAL A 50 THR A 54 1 N ILE A 52 O PHE A 74
SHEET 3 A 5 LEU A 6 THR A 9 1 N ILE A 7 O GLY A 51
SHEET 4 A 5 VAL A 98 ILE A 101 1 O ALA A 99 N LEU A 8
SHEET 5 A 5 ILE A 116 GLY A 118 1 O GLY A 118 N TYR A 100
SHEET 1 B 9 GLY A 19 ASP A 23 0
SHEET 2 B 9 GLU A 28 ASN A 33 -1 O TRP A 29 N PHE A 21
SHEET 3 B 9 GLY C 19 ASP C 23 -1 O MET C 20 N PHE A 32
SHEET 4 B 9 GLU C 28 ASN C 33 -1 O TRP C 29 N PHE C 21
SHEET 5 B 9 GLY D 19 TYR D 22 -1 O MET D 20 N PHE C 32
SHEET 6 B 9 GLU D 28 ASN D 33 -1 O TRP D 29 N PHE D 21
SHEET 7 B 9 GLY B 19 TYR B 22 -1 N MET B 20 O PHE D 32
SHEET 8 B 9 GLU B 28 ASN B 33 -1 O TRP B 29 N PHE B 21
SHEET 9 B 9 GLY A 19 ASP A 23 -1 N MET A 20 O PHE B 32
SHEET 1 C 5 TYR B 72 PHE B 74 0
SHEET 2 C 5 VAL B 50 LEU B 53 1 N ILE B 52 O PHE B 74
SHEET 3 C 5 LEU B 6 THR B 9 1 N THR B 9 O LEU B 53
SHEET 4 C 5 VAL B 98 ILE B 101 1 O ALA B 99 N LEU B 8
SHEET 5 C 5 ILE B 116 GLY B 118 1 O GLY B 118 N TYR B 100
SHEET 1 D 5 TYR C 72 PHE C 74 0
SHEET 2 D 5 VAL C 50 LEU C 53 1 N ILE C 52 O PHE C 74
SHEET 3 D 5 LEU C 6 THR C 9 1 N ILE C 7 O GLY C 51
SHEET 4 D 5 VAL C 98 ILE C 101 1 O ALA C 99 N LEU C 8
SHEET 5 D 5 ILE C 116 GLY C 118 1 O ILE C 116 N TYR C 100
SHEET 1 E 5 TYR D 72 PHE D 74 0
SHEET 2 E 5 VAL D 50 LEU D 53 1 N ILE D 52 O PHE D 74
SHEET 3 E 5 LEU D 6 THR D 9 1 N ILE D 7 O GLY D 51
SHEET 4 E 5 VAL D 98 ILE D 101 1 O ALA D 99 N LEU D 8
SHEET 5 E 5 ILE D 116 GLY D 118 1 O GLY D 118 N TYR D 100
SHEET 1 F 5 TYR E 72 PHE E 74 0
SHEET 2 F 5 VAL E 50 LEU E 53 1 N ILE E 52 O TYR E 72
SHEET 3 F 5 LEU E 6 THR E 9 1 N ILE E 7 O GLY E 51
SHEET 4 F 5 VAL E 98 ILE E 101 1 O ALA E 99 N LEU E 8
SHEET 5 F 5 ILE E 116 GLY E 118 1 O GLY E 118 N TYR E 100
SHEET 1 G 9 GLY E 19 TYR E 22 0
SHEET 2 G 9 GLU E 28 ASN E 33 -1 O TRP E 29 N PHE E 21
SHEET 3 G 9 GLY G 19 ASP G 23 -1 O MET G 20 N PHE E 32
SHEET 4 G 9 GLU G 28 ASN G 33 -1 O TRP G 29 N PHE G 21
SHEET 5 G 9 GLY H 19 TYR H 22 -1 O MET H 20 N PHE G 32
SHEET 6 G 9 GLU H 28 ASN H 33 -1 O TRP H 29 N PHE H 21
SHEET 7 G 9 GLY F 19 TYR F 22 -1 N TYR F 22 O LYS H 30
SHEET 8 G 9 GLU F 28 ASN F 33 -1 O TRP F 29 N PHE F 21
SHEET 9 G 9 GLY E 19 TYR E 22 -1 N TYR E 22 O LYS F 30
SHEET 1 H 5 TYR F 72 PHE F 74 0
SHEET 2 H 5 VAL F 50 LEU F 53 1 N ILE F 52 O PHE F 74
SHEET 3 H 5 LEU F 6 THR F 9 1 N THR F 9 O LEU F 53
SHEET 4 H 5 VAL F 98 ILE F 101 1 O ALA F 99 N LEU F 6
SHEET 5 H 5 ILE F 116 GLY F 118 1 O GLY F 118 N TYR F 100
SHEET 1 I 5 TYR G 72 PHE G 74 0
SHEET 2 I 5 VAL G 50 LEU G 53 1 N ILE G 52 O PHE G 74
SHEET 3 I 5 LEU G 6 THR G 9 1 N ILE G 7 O GLY G 51
SHEET 4 I 5 VAL G 98 ILE G 101 1 O ALA G 99 N LEU G 8
SHEET 5 I 5 ILE G 116 GLY G 118 1 O GLY G 118 N TYR G 100
SHEET 1 J 5 TYR H 72 PHE H 74 0
SHEET 2 J 5 VAL H 50 LEU H 53 1 N ILE H 52 O TYR H 72
SHEET 3 J 5 LEU H 6 THR H 9 1 N ILE H 7 O GLY H 51
SHEET 4 J 5 VAL H 98 ILE H 101 1 O ALA H 99 N LEU H 8
SHEET 5 J 5 ILE H 116 GLY H 118 1 O GLY H 118 N TYR H 100
LINK OD2 ASP A 10 MG MG A 201 1555 1555 2.10
LINK O ASP A 12 MG MG A 201 1555 1555 2.08
LINK OD1 ASP A 103 MG MG A 201 1555 1555 2.23
LINK MG MG A 201 O HOH A 301 1555 1555 2.11
LINK MG MG A 201 O HOH A 302 1555 1555 2.18
LINK MG MG A 201 O HOH A 327 1555 1555 2.11
LINK OD2 ASP B 10 MG MG B 201 1555 1555 2.07
LINK O ASP B 12 MG MG B 201 1555 1555 2.19
LINK OD1 ASP B 103 MG MG B 201 1555 1555 2.05
LINK MG MG B 201 O HOH B 301 1555 1555 2.18
LINK MG MG B 201 O HOH B 316 1555 1555 2.40
LINK MG MG B 201 O HOH B 396 1555 1555 2.86
LINK OD2 ASP C 10 MG MG C 201 1555 1555 1.98
LINK O ASP C 12 MG MG C 201 1555 1555 2.11
LINK OD1 ASP C 103 MG MG C 201 1555 1555 2.00
LINK MG MG C 201 O HOH C 302 1555 1555 2.11
LINK MG MG C 201 O HOH C 303 1555 1555 2.31
LINK MG MG C 201 O HOH C 369 1555 1555 1.95
LINK OD2 ASP D 10 MG MG D 201 1555 1555 1.96
LINK O ASP D 12 MG MG D 201 1555 1555 2.12
LINK OD1 ASP D 103 MG MG D 201 1555 1555 2.08
LINK MG MG D 201 O HOH D 308 1555 1555 2.24
LINK MG MG D 201 O HOH D 312 1555 1555 1.89
LINK MG MG D 201 O HOH D 398 1555 1555 1.85
LINK OD2 ASP E 10 MG MG E 201 1555 1555 2.15
LINK OD1 ASP E 10 MG MG E 201 1555 1555 2.87
LINK O ASP E 12 MG MG E 201 1555 1555 2.45
LINK MG MG E 201 O HOH E 301 1555 1555 2.15
LINK MG MG E 201 O HOH E 316 1555 1555 2.37
LINK MG MG E 201 O HOH E 342 1555 1555 2.02
LINK OD2 ASP F 10 MG MG F 201 1555 1555 2.17
LINK O ASP F 12 MG MG F 201 1555 1555 2.14
LINK OD1 ASP F 103 MG MG F 201 1555 1555 2.00
LINK MG MG F 201 O HOH F 301 1555 1555 1.84
LINK MG MG F 201 O HOH F 302 1555 1555 2.14
LINK MG MG F 201 O HOH F 352 1555 1555 2.25
LINK OD2 ASP G 10 MG MG G 201 1555 1555 2.13
LINK O ASP G 12 MG MG G 201 1555 1555 1.91
LINK OD1 ASP G 103 MG MG G 201 1555 1555 2.19
LINK MG MG G 201 O HOH G 302 1555 1555 2.04
LINK MG MG G 201 O HOH G 303 1555 1555 2.28
LINK MG MG G 201 O HOH G 320 1555 1555 2.43
LINK OD2 ASP H 10 MG MG H 201 1555 1555 2.05
LINK O ASP H 12 MG MG H 201 1555 1555 2.07
LINK OD1 ASP H 103 MG MG H 201 1555 1555 2.19
LINK MG MG H 201 O HOH H 315 1555 1555 2.17
LINK MG MG H 201 O HOH H 322 1555 1555 2.90
LINK MG MG H 201 O HOH H 324 1555 1555 2.37
SITE 1 AC1 6 ASP A 10 ASP A 12 ASP A 103 HOH A 301
SITE 2 AC1 6 HOH A 302 HOH A 327
SITE 1 AC2 6 ASP B 10 ASP B 12 ASP B 103 HOH B 301
SITE 2 AC2 6 HOH B 316 HOH B 396
SITE 1 AC3 6 ASP C 10 ASP C 12 ASP C 103 HOH C 302
SITE 2 AC3 6 HOH C 303 HOH C 369
SITE 1 AC4 6 ASP D 10 ASP D 12 ASP D 103 HOH D 308
SITE 2 AC4 6 HOH D 312 HOH D 398
SITE 1 AC5 6 ASP E 10 ASP E 12 ASP E 103 HOH E 301
SITE 2 AC5 6 HOH E 316 HOH E 342
SITE 1 AC6 6 ASP F 10 ASP F 12 ASP F 103 HOH F 301
SITE 2 AC6 6 HOH F 302 HOH F 352
SITE 1 AC7 6 ASP G 10 ASP G 12 ASP G 103 HOH G 302
SITE 2 AC7 6 HOH G 303 HOH G 320
SITE 1 AC8 6 ASP H 10 ASP H 12 ASP H 103 HOH H 315
SITE 2 AC8 6 HOH H 322 HOH H 324
CRYST1 72.367 116.765 75.180 90.00 93.09 90.00 P 1 21 1 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 0.013818 0.000000 0.000745 0.00000
SCALE2 0.000000 0.008564 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013321 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
