HEADER HYDROLASE 01-JUN-15 5BRQ
TITLE CRYSTAL STRUCTURE OF BACILLUS LICHENIFORMIS TREHALOSE-6-PHOSPHATE
TITLE 2 HYDROLASE (TREA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSIDE HYDROLASE FAMILY 13;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TREHALOSE-6-PHOSPHATE HYDROLASE;
COMPND 5 EC: 3.2.1.93;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS ATCC 14580 = DSM 13;
SOURCE 3 ORGANISM_TAXID: 279010;
SOURCE 4 STRAIN: ATCC 14580 = DSM 13;
SOURCE 5 GENE: TREA, BL03069;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI M15;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1007065;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS TREHALOSE-6-PHOSPHATE HYDROLASE, TIM BARREL, GH13 FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-D.HSIAO,M.-G.LIN
REVDAT 2 08-NOV-23 5BRQ 1 REMARK LINK
REVDAT 1 02-MAR-16 5BRQ 0
JRNL AUTH M.-G.LIN,M.-C.CHI,V.NAVEEN,Y.-C.LI,L.-L.LIN,C.-D.HSIAO
JRNL TITL BACILLUS LICHENIFORMIS TREHALOSE-6-PHOSPHATE HYDROLASE
JRNL TITL 2 STRUCTURES SUGGEST KEYS TO SUBSTRATE SPECIFICITY
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 72 59 2016
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 26894535
JRNL DOI 10.1107/S2059798315020756
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 146093
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.370
REMARK 3 FREE R VALUE TEST SET COUNT : 2002
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 24.3055 - 4.8151 0.50 10824 152 0.1448 0.1792
REMARK 3 2 4.8151 - 3.8267 0.48 10364 140 0.1386 0.2226
REMARK 3 3 3.8267 - 3.3444 0.49 10545 148 0.1615 0.2299
REMARK 3 4 3.3444 - 3.0392 0.49 10605 151 0.1899 0.2502
REMARK 3 5 3.0392 - 2.8217 0.49 10621 148 0.2046 0.2606
REMARK 3 6 2.8217 - 2.6556 0.49 10569 147 0.2095 0.2856
REMARK 3 7 2.6556 - 2.5227 0.49 10591 138 0.2034 0.2627
REMARK 3 8 2.5227 - 2.4130 0.49 10557 151 0.1996 0.2585
REMARK 3 9 2.4130 - 2.3202 0.48 10522 138 0.2048 0.2556
REMARK 3 10 2.3202 - 2.2402 0.48 10552 142 0.2106 0.2882
REMARK 3 11 2.2402 - 2.1702 0.48 10400 152 0.2108 0.2836
REMARK 3 12 2.1702 - 2.1082 0.47 10244 149 0.2174 0.2832
REMARK 3 13 2.1082 - 2.0527 0.44 9562 135 0.2261 0.3111
REMARK 3 14 2.0527 - 2.0027 0.37 8135 111 0.2356 0.3132
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 18856
REMARK 3 ANGLE : 1.114 25528
REMARK 3 CHIRALITY : 0.081 2580
REMARK 3 PLANARITY : 0.005 3332
REMARK 3 DIHEDRAL : 14.273 6984
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 5BRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210429.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.903
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 149079
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1UOK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350, 0.2 M MAGNESIUM
REMARK 280 ACETATE HEXAHYDRATE, 2% TACSIMATE (PH 5.0), VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLU A 5
REMARK 465 PRO A 561
REMARK 465 CYS A 562
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 LYS B 4
REMARK 465 GLU B 5
REMARK 465 PRO B 561
REMARK 465 CYS B 562
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 THR C 3
REMARK 465 LYS C 4
REMARK 465 GLU C 5
REMARK 465 PRO C 561
REMARK 465 CYS C 562
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 THR D 3
REMARK 465 LYS D 4
REMARK 465 GLU D 5
REMARK 465 PRO D 561
REMARK 465 CYS D 562
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 OD2 ASP C 538 NZ LYS C 549 1.95
REMARK 500 O HOH C 747 O HOH C 999 2.13
REMARK 500 OD2 ASP B 379 OG SER B 381 2.14
REMARK 500 O HOH D 942 O HOH D 988 2.15
REMARK 500 O HOH C 776 O HOH C 1005 2.16
REMARK 500 O HOH C 1016 O HOH C 1021 2.19
REMARK 500 O HOH C 716 O HOH C 1001 2.19
REMARK 500 O HOH D 747 O HOH D 984 2.19
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 TYR A 167 -136.45 -106.95
REMARK 500 VAL A 204 44.13 33.58
REMARK 500 PHE A 214 67.49 25.17
REMARK 500 TYR A 226 -2.39 -146.21
REMARK 500 VAL A 243 -66.21 -124.24
REMARK 500 SER A 257 52.43 34.84
REMARK 500 GLU A 273 -94.10 -114.59
REMARK 500 ARG A 384 -42.14 -135.30
REMARK 500 TYR A 551 19.20 56.85
REMARK 500 PHE B 22 -71.78 -94.56
REMARK 500 TYR B 167 -130.85 -109.14
REMARK 500 VAL B 204 53.52 28.60
REMARK 500 PHE B 214 56.94 38.62
REMARK 500 VAL B 243 -71.94 -130.39
REMARK 500 SER B 257 70.50 23.38
REMARK 500 GLU B 273 -80.10 -114.74
REMARK 500 ARG B 384 -40.31 -133.64
REMARK 500 ASP B 538 86.22 -69.31
REMARK 500 ARG B 545 117.39 -161.99
REMARK 500 PHE C 22 -68.48 -91.52
REMARK 500 ALA C 47 32.99 70.39
REMARK 500 ASP C 63 52.85 -142.08
REMARK 500 SER C 119 26.20 -79.51
REMARK 500 TYR C 167 -134.97 -103.87
REMARK 500 VAL C 204 47.63 30.99
REMARK 500 PHE C 214 55.96 34.93
REMARK 500 GLU C 219 -0.51 -149.23
REMARK 500 VAL C 243 -70.19 -118.68
REMARK 500 SER C 257 52.46 39.48
REMARK 500 GLU C 273 -89.57 -111.63
REMARK 500 TYR C 343 32.48 -94.19
REMARK 500 GLN C 366 122.99 -36.75
REMARK 500 ARG C 384 -38.12 -134.08
REMARK 500 ALA C 429 23.26 48.30
REMARK 500 PHE D 22 -70.05 -84.48
REMARK 500 ASP D 63 53.17 -143.51
REMARK 500 SER D 119 50.18 -98.09
REMARK 500 HIS D 156 77.76 -106.37
REMARK 500 ALA D 157 -6.77 -54.22
REMARK 500 TYR D 167 -129.62 -106.61
REMARK 500 VAL D 204 39.53 36.25
REMARK 500 GLU D 219 -36.46 -133.07
REMARK 500 TYR D 226 -8.52 -142.35
REMARK 500 VAL D 243 -70.94 -120.50
REMARK 500 GLU D 273 -87.45 -117.91
REMARK 500 ARG D 384 -36.99 -133.92
REMARK 500 ASN D 424 -167.82 -161.04
REMARK 500 ARG D 545 118.80 -165.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1080 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH C1053 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH D1025 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH D1026 DISTANCE = 7.00 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 24 OD1
REMARK 620 2 THR A 26 OG1 85.4
REMARK 620 3 ASN A 28 OD1 88.0 73.8
REMARK 620 4 VAL A 30 O 87.2 154.4 81.4
REMARK 620 5 ASP A 32 OD2 94.3 106.1 177.7 98.9
REMARK 620 6 HOH A 798 O 163.9 102.1 80.6 80.0 97.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 24 OD1
REMARK 620 2 THR B 26 OG1 85.7
REMARK 620 3 ASN B 28 OD1 87.6 78.8
REMARK 620 4 VAL B 30 O 86.7 163.6 86.4
REMARK 620 5 ASP B 32 OD2 90.8 96.0 174.6 98.6
REMARK 620 6 HOH B 727 O 178.7 94.1 91.1 93.2 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 24 OD1
REMARK 620 2 THR C 26 OG1 87.5
REMARK 620 3 ASN C 28 OD1 88.6 81.6
REMARK 620 4 VAL C 30 O 83.0 161.0 81.7
REMARK 620 5 ASP C 32 OD2 82.8 99.4 171.2 95.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 24 OD1
REMARK 620 2 THR D 26 OG1 78.1
REMARK 620 3 ASN D 28 OD1 80.2 69.2
REMARK 620 4 VAL D 30 O 75.9 147.1 86.7
REMARK 620 5 ASP D 32 OD2 81.9 95.5 158.5 100.4
REMARK 620 N 1 2 3 4
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5BRP RELATED DB: PDB
DBREF 5BRQ A 1 562 UNP Q65MI2 Q65MI2_BACLD 1 562
DBREF 5BRQ B 1 562 UNP Q65MI2 Q65MI2_BACLD 1 562
DBREF 5BRQ C 1 562 UNP Q65MI2 Q65MI2_BACLD 1 562
DBREF 5BRQ D 1 562 UNP Q65MI2 Q65MI2_BACLD 1 562
SEQADV 5BRQ HIS A -5 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS A -4 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS A -3 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS A -2 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS A -1 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS A 0 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS B -5 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS B -4 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS B -3 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS B -2 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS B -1 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS B 0 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS C -5 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS C -4 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS C -3 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS C -2 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS C -1 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS C 0 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS D -5 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS D -4 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS D -3 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS D -2 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS D -1 UNP Q65MI2 EXPRESSION TAG
SEQADV 5BRQ HIS D 0 UNP Q65MI2 EXPRESSION TAG
SEQRES 1 A 568 HIS HIS HIS HIS HIS HIS MET GLU THR LYS GLU ASN PRO
SEQRES 2 A 568 TRP TRP LYS LYS ALA VAL VAL TYR GLN ILE TYR PRO LYS
SEQRES 3 A 568 SER PHE LYS ASP THR THR GLY ASN GLY VAL GLY ASP ILE
SEQRES 4 A 568 ARG GLY ILE ILE GLU LYS LEU ASP TYR ILE LYS GLU LEU
SEQRES 5 A 568 ALA CYS ASP VAL ILE TRP LEU THR PRO ILE TYR GLN SER
SEQRES 6 A 568 PRO GLN ASN ASP ASN GLY TYR ASP ILE SER ASP TYR TYR
SEQRES 7 A 568 SER ILE HIS GLU GLU TYR GLY THR MET ALA ASP PHE GLU
SEQRES 8 A 568 GLU LEU LEU GLU GLU ALA HIS LYS ARG GLY ILE LYS VAL
SEQRES 9 A 568 ILE MET ASP LEU VAL VAL ASN HIS THR SER THR GLU HIS
SEQRES 10 A 568 ARG TRP PHE LYS GLU ALA ALA SER GLY LYS GLU ASN LEU
SEQRES 11 A 568 TYR ARG ASP PHE TYR ILE TRP LYS ASP MET LYS PRO ASN
SEQRES 12 A 568 GLY ALA PRO PRO THR ASN TRP GLU SER LYS PHE GLY GLY
SEQRES 13 A 568 SER ALA TRP GLU PHE HIS ALA GLU SER GLY GLN TYR TYR
SEQRES 14 A 568 LEU HIS LEU TYR ASP VAL THR GLN ALA ASP LEU ASN TRP
SEQRES 15 A 568 GLU ASN GLU ALA VAL ARG LYS LYS VAL TYR GLU MET MET
SEQRES 16 A 568 HIS PHE TRP PHE GLU LYS GLY ILE ASP GLY PHE ARG LEU
SEQRES 17 A 568 ASP VAL ILE ASN VAL ILE SER LYS ASP GLN ARG PHE PRO
SEQRES 18 A 568 ASP ASP ASP GLU GLY ASP GLY ARG ARG PHE TYR THR ASP
SEQRES 19 A 568 GLY PRO ARG VAL HIS GLU PHE LEU ASN GLU MET ASN ARG
SEQRES 20 A 568 GLU VAL PHE SER LYS TYR ASP SER MET THR VAL GLY GLU
SEQRES 21 A 568 MET SER SER THR THR ILE ALA ASP CYS ILE ARG TYR THR
SEQRES 22 A 568 ASN PRO GLU SER ARG GLU LEU ASP MET VAL PHE ASN PHE
SEQRES 23 A 568 HIS HIS LEU LYS ALA ASP TYR PRO ASN GLY GLU LYS TRP
SEQRES 24 A 568 ALA LEU ALA ASP PHE ASP PHE LEU LYS LEU LYS LYS ILE
SEQRES 25 A 568 LEU SER GLU TRP GLN THR GLU MET ASN LYS GLY GLY GLY
SEQRES 26 A 568 TRP ASN ALA LEU PHE TRP CYS ASN HIS ASP GLN PRO ARG
SEQRES 27 A 568 ILE VAL SER ARG TYR GLY ASP ASP GLY LYS TYR ARG LYS
SEQRES 28 A 568 LYS SER ALA LYS MET LEU ALA THR ALA ILE HIS MET LEU
SEQRES 29 A 568 GLN GLY THR PRO TYR ILE TYR GLN GLY GLU GLU LEU GLY
SEQRES 30 A 568 MET THR ASN PRO LYS PHE ASP ASP ILE SER LEU TYR ARG
SEQRES 31 A 568 ASP VAL GLU SER LEU ASN MET TYR ARG ILE LEU LYS GLU
SEQRES 32 A 568 ALA GLY LYS PRO GLU ALA GLU ILE ILE GLU ILE LEU LYS
SEQRES 33 A 568 ALA LYS SER ARG ASP ASN SER ARG THR PRO VAL GLN TRP
SEQRES 34 A 568 ASN GLY GLU GLU ASN ALA GLY PHE THR ALA GLY THR PRO
SEQRES 35 A 568 TRP ILE PRO VAL PRO ASP ASN TYR LYS GLU ILE ASN ALA
SEQRES 36 A 568 GLU GLU ALA LEU ASN ASP PRO ASP SER ILE PHE TYR HIS
SEQRES 37 A 568 TYR LYS LYS LEU ASN GLU LEU ARG LYS GLU PHE ASP ILE
SEQRES 38 A 568 ILE THR THR GLY ASP TYR GLN LEU ILE LEU GLU ASP ASP
SEQRES 39 A 568 GLN GLU LEU TYR ALA TYR LEU ARG ASN GLY ALA ASP GLU
SEQRES 40 A 568 LYS LEU LEU VAL ILE ASN ASN PHE TYR GLY LYS GLU THR
SEQRES 41 A 568 GLU PHE GLN LEU PRO ASP ASP ILE ASP ILE GLU GLY TYR
SEQRES 42 A 568 ASP ALA LYS VAL LEU ILE SER ASN ASP THR ASP LEU PRO
SEQRES 43 A 568 GLU SER PHE LYS ARG PHE THR VAL LYS PRO TYR GLN SER
SEQRES 44 A 568 ILE VAL TYR HIS LEU ALA LYS PRO CYS
SEQRES 1 B 568 HIS HIS HIS HIS HIS HIS MET GLU THR LYS GLU ASN PRO
SEQRES 2 B 568 TRP TRP LYS LYS ALA VAL VAL TYR GLN ILE TYR PRO LYS
SEQRES 3 B 568 SER PHE LYS ASP THR THR GLY ASN GLY VAL GLY ASP ILE
SEQRES 4 B 568 ARG GLY ILE ILE GLU LYS LEU ASP TYR ILE LYS GLU LEU
SEQRES 5 B 568 ALA CYS ASP VAL ILE TRP LEU THR PRO ILE TYR GLN SER
SEQRES 6 B 568 PRO GLN ASN ASP ASN GLY TYR ASP ILE SER ASP TYR TYR
SEQRES 7 B 568 SER ILE HIS GLU GLU TYR GLY THR MET ALA ASP PHE GLU
SEQRES 8 B 568 GLU LEU LEU GLU GLU ALA HIS LYS ARG GLY ILE LYS VAL
SEQRES 9 B 568 ILE MET ASP LEU VAL VAL ASN HIS THR SER THR GLU HIS
SEQRES 10 B 568 ARG TRP PHE LYS GLU ALA ALA SER GLY LYS GLU ASN LEU
SEQRES 11 B 568 TYR ARG ASP PHE TYR ILE TRP LYS ASP MET LYS PRO ASN
SEQRES 12 B 568 GLY ALA PRO PRO THR ASN TRP GLU SER LYS PHE GLY GLY
SEQRES 13 B 568 SER ALA TRP GLU PHE HIS ALA GLU SER GLY GLN TYR TYR
SEQRES 14 B 568 LEU HIS LEU TYR ASP VAL THR GLN ALA ASP LEU ASN TRP
SEQRES 15 B 568 GLU ASN GLU ALA VAL ARG LYS LYS VAL TYR GLU MET MET
SEQRES 16 B 568 HIS PHE TRP PHE GLU LYS GLY ILE ASP GLY PHE ARG LEU
SEQRES 17 B 568 ASP VAL ILE ASN VAL ILE SER LYS ASP GLN ARG PHE PRO
SEQRES 18 B 568 ASP ASP ASP GLU GLY ASP GLY ARG ARG PHE TYR THR ASP
SEQRES 19 B 568 GLY PRO ARG VAL HIS GLU PHE LEU ASN GLU MET ASN ARG
SEQRES 20 B 568 GLU VAL PHE SER LYS TYR ASP SER MET THR VAL GLY GLU
SEQRES 21 B 568 MET SER SER THR THR ILE ALA ASP CYS ILE ARG TYR THR
SEQRES 22 B 568 ASN PRO GLU SER ARG GLU LEU ASP MET VAL PHE ASN PHE
SEQRES 23 B 568 HIS HIS LEU LYS ALA ASP TYR PRO ASN GLY GLU LYS TRP
SEQRES 24 B 568 ALA LEU ALA ASP PHE ASP PHE LEU LYS LEU LYS LYS ILE
SEQRES 25 B 568 LEU SER GLU TRP GLN THR GLU MET ASN LYS GLY GLY GLY
SEQRES 26 B 568 TRP ASN ALA LEU PHE TRP CYS ASN HIS ASP GLN PRO ARG
SEQRES 27 B 568 ILE VAL SER ARG TYR GLY ASP ASP GLY LYS TYR ARG LYS
SEQRES 28 B 568 LYS SER ALA LYS MET LEU ALA THR ALA ILE HIS MET LEU
SEQRES 29 B 568 GLN GLY THR PRO TYR ILE TYR GLN GLY GLU GLU LEU GLY
SEQRES 30 B 568 MET THR ASN PRO LYS PHE ASP ASP ILE SER LEU TYR ARG
SEQRES 31 B 568 ASP VAL GLU SER LEU ASN MET TYR ARG ILE LEU LYS GLU
SEQRES 32 B 568 ALA GLY LYS PRO GLU ALA GLU ILE ILE GLU ILE LEU LYS
SEQRES 33 B 568 ALA LYS SER ARG ASP ASN SER ARG THR PRO VAL GLN TRP
SEQRES 34 B 568 ASN GLY GLU GLU ASN ALA GLY PHE THR ALA GLY THR PRO
SEQRES 35 B 568 TRP ILE PRO VAL PRO ASP ASN TYR LYS GLU ILE ASN ALA
SEQRES 36 B 568 GLU GLU ALA LEU ASN ASP PRO ASP SER ILE PHE TYR HIS
SEQRES 37 B 568 TYR LYS LYS LEU ASN GLU LEU ARG LYS GLU PHE ASP ILE
SEQRES 38 B 568 ILE THR THR GLY ASP TYR GLN LEU ILE LEU GLU ASP ASP
SEQRES 39 B 568 GLN GLU LEU TYR ALA TYR LEU ARG ASN GLY ALA ASP GLU
SEQRES 40 B 568 LYS LEU LEU VAL ILE ASN ASN PHE TYR GLY LYS GLU THR
SEQRES 41 B 568 GLU PHE GLN LEU PRO ASP ASP ILE ASP ILE GLU GLY TYR
SEQRES 42 B 568 ASP ALA LYS VAL LEU ILE SER ASN ASP THR ASP LEU PRO
SEQRES 43 B 568 GLU SER PHE LYS ARG PHE THR VAL LYS PRO TYR GLN SER
SEQRES 44 B 568 ILE VAL TYR HIS LEU ALA LYS PRO CYS
SEQRES 1 C 568 HIS HIS HIS HIS HIS HIS MET GLU THR LYS GLU ASN PRO
SEQRES 2 C 568 TRP TRP LYS LYS ALA VAL VAL TYR GLN ILE TYR PRO LYS
SEQRES 3 C 568 SER PHE LYS ASP THR THR GLY ASN GLY VAL GLY ASP ILE
SEQRES 4 C 568 ARG GLY ILE ILE GLU LYS LEU ASP TYR ILE LYS GLU LEU
SEQRES 5 C 568 ALA CYS ASP VAL ILE TRP LEU THR PRO ILE TYR GLN SER
SEQRES 6 C 568 PRO GLN ASN ASP ASN GLY TYR ASP ILE SER ASP TYR TYR
SEQRES 7 C 568 SER ILE HIS GLU GLU TYR GLY THR MET ALA ASP PHE GLU
SEQRES 8 C 568 GLU LEU LEU GLU GLU ALA HIS LYS ARG GLY ILE LYS VAL
SEQRES 9 C 568 ILE MET ASP LEU VAL VAL ASN HIS THR SER THR GLU HIS
SEQRES 10 C 568 ARG TRP PHE LYS GLU ALA ALA SER GLY LYS GLU ASN LEU
SEQRES 11 C 568 TYR ARG ASP PHE TYR ILE TRP LYS ASP MET LYS PRO ASN
SEQRES 12 C 568 GLY ALA PRO PRO THR ASN TRP GLU SER LYS PHE GLY GLY
SEQRES 13 C 568 SER ALA TRP GLU PHE HIS ALA GLU SER GLY GLN TYR TYR
SEQRES 14 C 568 LEU HIS LEU TYR ASP VAL THR GLN ALA ASP LEU ASN TRP
SEQRES 15 C 568 GLU ASN GLU ALA VAL ARG LYS LYS VAL TYR GLU MET MET
SEQRES 16 C 568 HIS PHE TRP PHE GLU LYS GLY ILE ASP GLY PHE ARG LEU
SEQRES 17 C 568 ASP VAL ILE ASN VAL ILE SER LYS ASP GLN ARG PHE PRO
SEQRES 18 C 568 ASP ASP ASP GLU GLY ASP GLY ARG ARG PHE TYR THR ASP
SEQRES 19 C 568 GLY PRO ARG VAL HIS GLU PHE LEU ASN GLU MET ASN ARG
SEQRES 20 C 568 GLU VAL PHE SER LYS TYR ASP SER MET THR VAL GLY GLU
SEQRES 21 C 568 MET SER SER THR THR ILE ALA ASP CYS ILE ARG TYR THR
SEQRES 22 C 568 ASN PRO GLU SER ARG GLU LEU ASP MET VAL PHE ASN PHE
SEQRES 23 C 568 HIS HIS LEU LYS ALA ASP TYR PRO ASN GLY GLU LYS TRP
SEQRES 24 C 568 ALA LEU ALA ASP PHE ASP PHE LEU LYS LEU LYS LYS ILE
SEQRES 25 C 568 LEU SER GLU TRP GLN THR GLU MET ASN LYS GLY GLY GLY
SEQRES 26 C 568 TRP ASN ALA LEU PHE TRP CYS ASN HIS ASP GLN PRO ARG
SEQRES 27 C 568 ILE VAL SER ARG TYR GLY ASP ASP GLY LYS TYR ARG LYS
SEQRES 28 C 568 LYS SER ALA LYS MET LEU ALA THR ALA ILE HIS MET LEU
SEQRES 29 C 568 GLN GLY THR PRO TYR ILE TYR GLN GLY GLU GLU LEU GLY
SEQRES 30 C 568 MET THR ASN PRO LYS PHE ASP ASP ILE SER LEU TYR ARG
SEQRES 31 C 568 ASP VAL GLU SER LEU ASN MET TYR ARG ILE LEU LYS GLU
SEQRES 32 C 568 ALA GLY LYS PRO GLU ALA GLU ILE ILE GLU ILE LEU LYS
SEQRES 33 C 568 ALA LYS SER ARG ASP ASN SER ARG THR PRO VAL GLN TRP
SEQRES 34 C 568 ASN GLY GLU GLU ASN ALA GLY PHE THR ALA GLY THR PRO
SEQRES 35 C 568 TRP ILE PRO VAL PRO ASP ASN TYR LYS GLU ILE ASN ALA
SEQRES 36 C 568 GLU GLU ALA LEU ASN ASP PRO ASP SER ILE PHE TYR HIS
SEQRES 37 C 568 TYR LYS LYS LEU ASN GLU LEU ARG LYS GLU PHE ASP ILE
SEQRES 38 C 568 ILE THR THR GLY ASP TYR GLN LEU ILE LEU GLU ASP ASP
SEQRES 39 C 568 GLN GLU LEU TYR ALA TYR LEU ARG ASN GLY ALA ASP GLU
SEQRES 40 C 568 LYS LEU LEU VAL ILE ASN ASN PHE TYR GLY LYS GLU THR
SEQRES 41 C 568 GLU PHE GLN LEU PRO ASP ASP ILE ASP ILE GLU GLY TYR
SEQRES 42 C 568 ASP ALA LYS VAL LEU ILE SER ASN ASP THR ASP LEU PRO
SEQRES 43 C 568 GLU SER PHE LYS ARG PHE THR VAL LYS PRO TYR GLN SER
SEQRES 44 C 568 ILE VAL TYR HIS LEU ALA LYS PRO CYS
SEQRES 1 D 568 HIS HIS HIS HIS HIS HIS MET GLU THR LYS GLU ASN PRO
SEQRES 2 D 568 TRP TRP LYS LYS ALA VAL VAL TYR GLN ILE TYR PRO LYS
SEQRES 3 D 568 SER PHE LYS ASP THR THR GLY ASN GLY VAL GLY ASP ILE
SEQRES 4 D 568 ARG GLY ILE ILE GLU LYS LEU ASP TYR ILE LYS GLU LEU
SEQRES 5 D 568 ALA CYS ASP VAL ILE TRP LEU THR PRO ILE TYR GLN SER
SEQRES 6 D 568 PRO GLN ASN ASP ASN GLY TYR ASP ILE SER ASP TYR TYR
SEQRES 7 D 568 SER ILE HIS GLU GLU TYR GLY THR MET ALA ASP PHE GLU
SEQRES 8 D 568 GLU LEU LEU GLU GLU ALA HIS LYS ARG GLY ILE LYS VAL
SEQRES 9 D 568 ILE MET ASP LEU VAL VAL ASN HIS THR SER THR GLU HIS
SEQRES 10 D 568 ARG TRP PHE LYS GLU ALA ALA SER GLY LYS GLU ASN LEU
SEQRES 11 D 568 TYR ARG ASP PHE TYR ILE TRP LYS ASP MET LYS PRO ASN
SEQRES 12 D 568 GLY ALA PRO PRO THR ASN TRP GLU SER LYS PHE GLY GLY
SEQRES 13 D 568 SER ALA TRP GLU PHE HIS ALA GLU SER GLY GLN TYR TYR
SEQRES 14 D 568 LEU HIS LEU TYR ASP VAL THR GLN ALA ASP LEU ASN TRP
SEQRES 15 D 568 GLU ASN GLU ALA VAL ARG LYS LYS VAL TYR GLU MET MET
SEQRES 16 D 568 HIS PHE TRP PHE GLU LYS GLY ILE ASP GLY PHE ARG LEU
SEQRES 17 D 568 ASP VAL ILE ASN VAL ILE SER LYS ASP GLN ARG PHE PRO
SEQRES 18 D 568 ASP ASP ASP GLU GLY ASP GLY ARG ARG PHE TYR THR ASP
SEQRES 19 D 568 GLY PRO ARG VAL HIS GLU PHE LEU ASN GLU MET ASN ARG
SEQRES 20 D 568 GLU VAL PHE SER LYS TYR ASP SER MET THR VAL GLY GLU
SEQRES 21 D 568 MET SER SER THR THR ILE ALA ASP CYS ILE ARG TYR THR
SEQRES 22 D 568 ASN PRO GLU SER ARG GLU LEU ASP MET VAL PHE ASN PHE
SEQRES 23 D 568 HIS HIS LEU LYS ALA ASP TYR PRO ASN GLY GLU LYS TRP
SEQRES 24 D 568 ALA LEU ALA ASP PHE ASP PHE LEU LYS LEU LYS LYS ILE
SEQRES 25 D 568 LEU SER GLU TRP GLN THR GLU MET ASN LYS GLY GLY GLY
SEQRES 26 D 568 TRP ASN ALA LEU PHE TRP CYS ASN HIS ASP GLN PRO ARG
SEQRES 27 D 568 ILE VAL SER ARG TYR GLY ASP ASP GLY LYS TYR ARG LYS
SEQRES 28 D 568 LYS SER ALA LYS MET LEU ALA THR ALA ILE HIS MET LEU
SEQRES 29 D 568 GLN GLY THR PRO TYR ILE TYR GLN GLY GLU GLU LEU GLY
SEQRES 30 D 568 MET THR ASN PRO LYS PHE ASP ASP ILE SER LEU TYR ARG
SEQRES 31 D 568 ASP VAL GLU SER LEU ASN MET TYR ARG ILE LEU LYS GLU
SEQRES 32 D 568 ALA GLY LYS PRO GLU ALA GLU ILE ILE GLU ILE LEU LYS
SEQRES 33 D 568 ALA LYS SER ARG ASP ASN SER ARG THR PRO VAL GLN TRP
SEQRES 34 D 568 ASN GLY GLU GLU ASN ALA GLY PHE THR ALA GLY THR PRO
SEQRES 35 D 568 TRP ILE PRO VAL PRO ASP ASN TYR LYS GLU ILE ASN ALA
SEQRES 36 D 568 GLU GLU ALA LEU ASN ASP PRO ASP SER ILE PHE TYR HIS
SEQRES 37 D 568 TYR LYS LYS LEU ASN GLU LEU ARG LYS GLU PHE ASP ILE
SEQRES 38 D 568 ILE THR THR GLY ASP TYR GLN LEU ILE LEU GLU ASP ASP
SEQRES 39 D 568 GLN GLU LEU TYR ALA TYR LEU ARG ASN GLY ALA ASP GLU
SEQRES 40 D 568 LYS LEU LEU VAL ILE ASN ASN PHE TYR GLY LYS GLU THR
SEQRES 41 D 568 GLU PHE GLN LEU PRO ASP ASP ILE ASP ILE GLU GLY TYR
SEQRES 42 D 568 ASP ALA LYS VAL LEU ILE SER ASN ASP THR ASP LEU PRO
SEQRES 43 D 568 GLU SER PHE LYS ARG PHE THR VAL LYS PRO TYR GLN SER
SEQRES 44 D 568 ILE VAL TYR HIS LEU ALA LYS PRO CYS
HET MG A 601 1
HET MG B 601 1
HET MG C 601 1
HET MG D 601 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG 4(MG 2+)
FORMUL 9 HOH *1445(H2 O)
HELIX 1 AA1 TYR A 18 PHE A 22 5 5
HELIX 2 AA2 ASP A 32 LYS A 39 1 8
HELIX 3 AA3 LYS A 39 LEU A 46 1 8
HELIX 4 AA4 GLU A 76 GLY A 79 5 4
HELIX 5 AA5 THR A 80 ARG A 94 1 15
HELIX 6 AA6 HIS A 111 SER A 119 1 9
HELIX 7 AA7 TYR A 125 TYR A 129 5 5
HELIX 8 AA8 ASN A 178 GLY A 196 1 19
HELIX 9 AA9 VAL A 204 ILE A 208 5 5
HELIX 10 AB1 GLY A 222 TYR A 226 5 5
HELIX 11 AB2 ARG A 231 VAL A 243 1 13
HELIX 12 AB3 PHE A 244 TYR A 247 5 4
HELIX 13 AB4 THR A 259 ASN A 268 1 10
HELIX 14 AB5 PRO A 269 ARG A 272 5 4
HELIX 15 AB6 PHE A 280 ALA A 285 5 6
HELIX 16 AB7 TYR A 287 GLU A 291 5 5
HELIX 17 AB8 ASP A 299 GLY A 318 1 20
HELIX 18 AB9 ARG A 332 TYR A 337 1 6
HELIX 19 AC1 TYR A 343 MET A 357 1 15
HELIX 20 AC2 GLY A 367 GLY A 371 5 5
HELIX 21 AC3 ASP A 379 TYR A 383 5 5
HELIX 22 AC4 ASP A 385 ALA A 398 1 14
HELIX 23 AC5 PRO A 401 SER A 413 1 13
HELIX 24 AC6 GLU A 426 PHE A 431 5 6
HELIX 25 AC7 PRO A 441 GLU A 446 5 6
HELIX 26 AC8 ASN A 448 ASN A 454 1 7
HELIX 27 AC9 SER A 458 PHE A 473 1 16
HELIX 28 AD1 ASP A 474 GLY A 479 1 6
HELIX 29 AD2 PRO B 7 ALA B 12 5 6
HELIX 30 AD3 TYR B 18 PHE B 22 5 5
HELIX 31 AD4 ASP B 32 LYS B 39 1 8
HELIX 32 AD5 LYS B 39 LEU B 46 1 8
HELIX 33 AD6 GLU B 76 GLY B 79 5 4
HELIX 34 AD7 THR B 80 ARG B 94 1 15
HELIX 35 AD8 HIS B 111 SER B 119 1 9
HELIX 36 AD9 TYR B 125 TYR B 129 5 5
HELIX 37 AE1 ASN B 178 GLY B 196 1 19
HELIX 38 AE2 VAL B 204 ILE B 208 5 5
HELIX 39 AE3 GLY B 222 TYR B 226 5 5
HELIX 40 AE4 ARG B 231 VAL B 243 1 13
HELIX 41 AE5 PHE B 244 TYR B 247 5 4
HELIX 42 AE6 THR B 259 ASN B 268 1 10
HELIX 43 AE7 PRO B 269 ARG B 272 5 4
HELIX 44 AE8 PHE B 280 ALA B 285 5 6
HELIX 45 AE9 TYR B 287 GLU B 291 5 5
HELIX 46 AF1 ASP B 299 GLY B 318 1 20
HELIX 47 AF2 ARG B 332 TYR B 337 1 6
HELIX 48 AF3 TYR B 343 MET B 357 1 15
HELIX 49 AF4 GLY B 367 GLY B 371 5 5
HELIX 50 AF5 ASP B 379 TYR B 383 5 5
HELIX 51 AF6 ASP B 385 ALA B 398 1 14
HELIX 52 AF7 PRO B 401 SER B 413 1 13
HELIX 53 AF8 GLU B 426 PHE B 431 5 6
HELIX 54 AF9 PRO B 441 GLU B 446 5 6
HELIX 55 AG1 ASN B 448 ASN B 454 1 7
HELIX 56 AG2 SER B 458 PHE B 473 1 16
HELIX 57 AG3 ASP B 474 GLY B 479 1 6
HELIX 58 AG4 PRO C 7 LYS C 11 5 5
HELIX 59 AG5 TYR C 18 PHE C 22 5 5
HELIX 60 AG6 ASP C 32 LYS C 39 1 8
HELIX 61 AG7 LYS C 39 LEU C 46 1 8
HELIX 62 AG8 GLU C 76 GLY C 79 5 4
HELIX 63 AG9 THR C 80 LYS C 93 1 14
HELIX 64 AH1 HIS C 111 SER C 119 1 9
HELIX 65 AH2 TYR C 125 TYR C 129 5 5
HELIX 66 AH3 ASN C 178 GLY C 196 1 19
HELIX 67 AH4 VAL C 204 ILE C 208 5 5
HELIX 68 AH5 GLY C 222 TYR C 226 5 5
HELIX 69 AH6 ARG C 231 VAL C 243 1 13
HELIX 70 AH7 PHE C 244 TYR C 247 5 4
HELIX 71 AH8 THR C 259 ASN C 268 1 10
HELIX 72 AH9 PRO C 269 ARG C 272 5 4
HELIX 73 AI1 PHE C 280 ALA C 285 5 6
HELIX 74 AI2 TYR C 287 GLU C 291 5 5
HELIX 75 AI3 ASP C 299 GLY C 318 1 20
HELIX 76 AI4 ARG C 332 TYR C 337 1 6
HELIX 77 AI5 TYR C 343 MET C 357 1 15
HELIX 78 AI6 GLY C 367 GLY C 371 5 5
HELIX 79 AI7 ASP C 379 TYR C 383 5 5
HELIX 80 AI8 ASP C 385 ALA C 398 1 14
HELIX 81 AI9 PRO C 401 SER C 413 1 13
HELIX 82 AJ1 GLU C 426 PHE C 431 5 6
HELIX 83 AJ2 PRO C 441 GLU C 446 5 6
HELIX 84 AJ3 ASN C 448 ASN C 454 1 7
HELIX 85 AJ4 SER C 458 PHE C 473 1 16
HELIX 86 AJ5 ASP C 474 GLY C 479 1 6
HELIX 87 AJ6 PRO D 7 LYS D 11 5 5
HELIX 88 AJ7 TYR D 18 PHE D 22 5 5
HELIX 89 AJ8 ASP D 32 LYS D 39 1 8
HELIX 90 AJ9 LYS D 39 LEU D 46 1 8
HELIX 91 AK1 THR D 80 ARG D 94 1 15
HELIX 92 AK2 HIS D 111 SER D 119 1 9
HELIX 93 AK3 TYR D 125 TYR D 129 5 5
HELIX 94 AK4 ASN D 178 GLY D 196 1 19
HELIX 95 AK5 VAL D 204 ILE D 208 5 5
HELIX 96 AK6 GLY D 222 TYR D 226 5 5
HELIX 97 AK7 ARG D 231 VAL D 243 1 13
HELIX 98 AK8 PHE D 244 TYR D 247 5 4
HELIX 99 AK9 THR D 259 ASN D 268 1 10
HELIX 100 AL1 PRO D 269 ARG D 272 5 4
HELIX 101 AL2 PHE D 280 ALA D 285 5 6
HELIX 102 AL3 TYR D 287 GLU D 291 5 5
HELIX 103 AL4 ASP D 299 GLY D 318 1 20
HELIX 104 AL5 ARG D 332 TYR D 337 1 6
HELIX 105 AL6 TYR D 343 MET D 357 1 15
HELIX 106 AL7 GLY D 367 GLY D 371 5 5
HELIX 107 AL8 ASP D 379 TYR D 383 5 5
HELIX 108 AL9 ASP D 385 ALA D 398 1 14
HELIX 109 AM1 PRO D 401 SER D 413 1 13
HELIX 110 AM2 GLU D 426 PHE D 431 5 6
HELIX 111 AM3 PRO D 441 GLU D 446 5 6
HELIX 112 AM4 ASN D 448 ASN D 454 1 7
HELIX 113 AM5 SER D 458 PHE D 473 1 16
HELIX 114 AM6 ASP D 474 GLY D 479 1 6
SHEET 1 AA1 8 MET A 276 PHE A 278 0
SHEET 2 AA1 8 MET A 250 GLU A 254 1 N GLY A 253 O PHE A 278
SHEET 3 AA1 8 GLY A 199 LEU A 202 1 N LEU A 202 O VAL A 252
SHEET 4 AA1 8 LYS A 97 LEU A 102 1 N LEU A 102 O ARG A 201
SHEET 5 AA1 8 VAL A 50 LEU A 53 1 N ILE A 51 O ILE A 99
SHEET 6 AA1 8 VAL A 14 ILE A 17 1 N ILE A 17 O TRP A 52
SHEET 7 AA1 8 THR A 361 TYR A 365 1 O ILE A 364 N GLN A 16
SHEET 8 AA1 8 ALA A 322 LEU A 323 1 N LEU A 323 O THR A 361
SHEET 1 AA2 2 TYR A 57 GLN A 58 0
SHEET 2 AA2 2 ASP A 70 ILE A 74 -1 O SER A 73 N GLN A 58
SHEET 1 AA3 2 HIS A 106 SER A 108 0
SHEET 2 AA3 2 GLN A 171 ASP A 173 -1 O ALA A 172 N THR A 107
SHEET 1 AA4 3 TRP A 131 LYS A 132 0
SHEET 2 AA4 3 GLN A 161 LEU A 164 -1 O TYR A 162 N LYS A 132
SHEET 3 AA4 3 TRP A 153 HIS A 156 -1 N HIS A 156 O GLN A 161
SHEET 1 AA5 5 GLN A 482 ILE A 484 0
SHEET 2 AA5 5 LEU A 491 ASN A 497 -1 O LEU A 495 N GLN A 482
SHEET 3 AA5 5 GLU A 501 ASN A 508 -1 O VAL A 505 N TYR A 494
SHEET 4 AA5 5 SER A 553 ALA A 559 -1 O TYR A 556 N LEU A 504
SHEET 5 AA5 5 ASP A 528 SER A 534 -1 N ASP A 528 O ALA A 559
SHEET 1 AA6 2 THR A 514 GLN A 517 0
SHEET 2 AA6 2 ARG A 545 VAL A 548 -1 O VAL A 548 N THR A 514
SHEET 1 AA7 8 MET B 276 PHE B 278 0
SHEET 2 AA7 8 MET B 250 GLU B 254 1 N GLY B 253 O PHE B 278
SHEET 3 AA7 8 GLY B 199 LEU B 202 1 N LEU B 202 O VAL B 252
SHEET 4 AA7 8 LYS B 97 LEU B 102 1 N MET B 100 O ARG B 201
SHEET 5 AA7 8 VAL B 50 LEU B 53 1 N ILE B 51 O ILE B 99
SHEET 6 AA7 8 VAL B 14 ILE B 17 1 N ILE B 17 O TRP B 52
SHEET 7 AA7 8 THR B 361 TYR B 365 1 O ILE B 364 N GLN B 16
SHEET 8 AA7 8 ALA B 322 LEU B 323 1 N LEU B 323 O THR B 361
SHEET 1 AA8 2 TYR B 57 GLN B 58 0
SHEET 2 AA8 2 ASP B 70 ILE B 74 -1 O SER B 73 N GLN B 58
SHEET 1 AA9 2 HIS B 106 SER B 108 0
SHEET 2 AA9 2 GLN B 171 ASP B 173 -1 O ALA B 172 N THR B 107
SHEET 1 AB1 3 TRP B 131 LYS B 132 0
SHEET 2 AB1 3 GLN B 161 LEU B 164 -1 O TYR B 162 N LYS B 132
SHEET 3 AB1 3 TRP B 153 HIS B 156 -1 N GLU B 154 O TYR B 163
SHEET 1 AB2 5 GLN B 482 ILE B 484 0
SHEET 2 AB2 5 LEU B 491 GLY B 498 -1 O LEU B 495 N GLN B 482
SHEET 3 AB2 5 GLU B 501 ASN B 508 -1 O GLU B 501 N GLY B 498
SHEET 4 AB2 5 SER B 553 ALA B 559 -1 O TYR B 556 N LEU B 504
SHEET 5 AB2 5 ASP B 528 SER B 534 -1 N ASP B 528 O ALA B 559
SHEET 1 AB3 2 THR B 514 GLN B 517 0
SHEET 2 AB3 2 ARG B 545 VAL B 548 -1 O PHE B 546 N PHE B 516
SHEET 1 AB4 8 MET C 276 PHE C 278 0
SHEET 2 AB4 8 MET C 250 GLU C 254 1 N GLY C 253 O PHE C 278
SHEET 3 AB4 8 GLY C 199 LEU C 202 1 N LEU C 202 O GLU C 254
SHEET 4 AB4 8 LYS C 97 LEU C 102 1 N LEU C 102 O ARG C 201
SHEET 5 AB4 8 VAL C 50 LEU C 53 1 N ILE C 51 O ILE C 99
SHEET 6 AB4 8 VAL C 14 ILE C 17 1 N ILE C 17 O TRP C 52
SHEET 7 AB4 8 THR C 361 TYR C 365 1 O ILE C 364 N GLN C 16
SHEET 8 AB4 8 ALA C 322 LEU C 323 1 N LEU C 323 O THR C 361
SHEET 1 AB5 2 TYR C 57 GLN C 58 0
SHEET 2 AB5 2 ASP C 70 ILE C 74 -1 O SER C 73 N GLN C 58
SHEET 1 AB6 2 HIS C 106 SER C 108 0
SHEET 2 AB6 2 GLN C 171 ASP C 173 -1 O ALA C 172 N THR C 107
SHEET 1 AB7 3 TRP C 131 LYS C 132 0
SHEET 2 AB7 3 GLN C 161 LEU C 164 -1 O TYR C 162 N LYS C 132
SHEET 3 AB7 3 TRP C 153 HIS C 156 -1 N GLU C 154 O TYR C 163
SHEET 1 AB8 5 GLN C 482 ILE C 484 0
SHEET 2 AB8 5 LEU C 491 ASN C 497 -1 O LEU C 495 N GLN C 482
SHEET 3 AB8 5 GLU C 501 ASN C 508 -1 O ASN C 507 N TYR C 492
SHEET 4 AB8 5 SER C 553 ALA C 559 -1 O LEU C 558 N LYS C 502
SHEET 5 AB8 5 ASP C 528 SER C 534 -1 N LYS C 530 O HIS C 557
SHEET 1 AB9 2 THR C 514 GLN C 517 0
SHEET 2 AB9 2 ARG C 545 VAL C 548 -1 O VAL C 548 N THR C 514
SHEET 1 AC1 8 MET D 276 PHE D 278 0
SHEET 2 AC1 8 MET D 250 GLU D 254 1 N GLY D 253 O PHE D 278
SHEET 3 AC1 8 GLY D 199 LEU D 202 1 N LEU D 202 O VAL D 252
SHEET 4 AC1 8 LYS D 97 LEU D 102 1 N LEU D 102 O ARG D 201
SHEET 5 AC1 8 VAL D 50 LEU D 53 1 N ILE D 51 O ILE D 99
SHEET 6 AC1 8 VAL D 14 ILE D 17 1 N ILE D 17 O TRP D 52
SHEET 7 AC1 8 THR D 361 TYR D 365 1 O ILE D 364 N GLN D 16
SHEET 8 AC1 8 ALA D 322 LEU D 323 1 N LEU D 323 O THR D 361
SHEET 1 AC2 2 TYR D 57 GLN D 58 0
SHEET 2 AC2 2 ASP D 70 ILE D 74 -1 O SER D 73 N GLN D 58
SHEET 1 AC3 2 HIS D 106 SER D 108 0
SHEET 2 AC3 2 GLN D 171 ASP D 173 -1 O ALA D 172 N THR D 107
SHEET 1 AC4 3 TRP D 131 ASP D 133 0
SHEET 2 AC4 3 GLN D 161 LEU D 164 -1 O TYR D 162 N LYS D 132
SHEET 3 AC4 3 TRP D 153 PHE D 155 -1 N GLU D 154 O TYR D 163
SHEET 1 AC5 5 GLN D 482 ILE D 484 0
SHEET 2 AC5 5 LEU D 491 ASN D 497 -1 O LEU D 495 N GLN D 482
SHEET 3 AC5 5 GLU D 501 ASN D 508 -1 O ASN D 507 N TYR D 492
SHEET 4 AC5 5 SER D 553 ALA D 559 -1 O LEU D 558 N LYS D 502
SHEET 5 AC5 5 ASP D 528 SER D 534 -1 N LYS D 530 O HIS D 557
SHEET 1 AC6 2 THR D 514 GLN D 517 0
SHEET 2 AC6 2 ARG D 545 VAL D 548 -1 O PHE D 546 N PHE D 516
LINK OD1 ASP A 24 MG MG A 601 1555 1555 2.30
LINK OG1 THR A 26 MG MG A 601 1555 1555 2.61
LINK OD1 ASN A 28 MG MG A 601 1555 1555 2.59
LINK O VAL A 30 MG MG A 601 1555 1555 2.38
LINK OD2 ASP A 32 MG MG A 601 1555 1555 2.42
LINK MG MG A 601 O HOH A 798 1555 1555 2.42
LINK OD1 ASP B 24 MG MG B 601 1555 1555 2.26
LINK OG1 THR B 26 MG MG B 601 1555 1555 2.60
LINK OD1 ASN B 28 MG MG B 601 1555 1555 2.37
LINK O VAL B 30 MG MG B 601 1555 1555 2.26
LINK OD2 ASP B 32 MG MG B 601 1555 1555 2.40
LINK MG MG B 601 O HOH B 727 1555 1555 2.32
LINK OD1 ASP C 24 MG MG C 601 1555 1555 2.08
LINK OG1 THR C 26 MG MG C 601 1555 1555 2.56
LINK OD1 ASN C 28 MG MG C 601 1555 1555 2.44
LINK O VAL C 30 MG MG C 601 1555 1555 2.34
LINK OD2 ASP C 32 MG MG C 601 1555 1555 2.46
LINK OD1 ASP D 24 MG MG D 601 1555 1555 2.50
LINK OG1 THR D 26 MG MG D 601 1555 1555 2.78
LINK OD1 ASN D 28 MG MG D 601 1555 1555 2.45
LINK O VAL D 30 MG MG D 601 1555 1555 2.28
LINK OD2 ASP D 32 MG MG D 601 1555 1555 2.31
CISPEP 1 GLY C 220 ASP C 221 0 -3.13
SITE 1 AC1 6 ASP A 24 THR A 26 ASN A 28 VAL A 30
SITE 2 AC1 6 ASP A 32 HOH A 798
SITE 1 AC2 6 ASP B 24 THR B 26 ASN B 28 VAL B 30
SITE 2 AC2 6 ASP B 32 HOH B 727
SITE 1 AC3 5 ASP C 24 THR C 26 ASN C 28 VAL C 30
SITE 2 AC3 5 ASP C 32
SITE 1 AC4 5 ASP D 24 THR D 26 ASN D 28 VAL D 30
SITE 2 AC4 5 ASP D 32
CRYST1 59.802 97.584 108.336 98.20 91.44 108.15 P 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 0.016722 0.005482 0.001306 0.00000
SCALE2 0.000000 0.010784 0.001729 0.00000
SCALE3 0.000000 0.000000 0.009351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
