HEADER HYDROLASE 27-MAY-09 3HLI
TITLE DIISOPROPYL FLUOROPHOSPHATASE (DFPASE), ACTIVE SITE MUTANTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIISOPROPYL-FLUOROPHOSPHATASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DFPASE;
COMPND 5 EC: 3.1.8.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LOLIGO VULGARIS;
SOURCE 3 ORGANISM_COMMON: COMMON EUROPEAN SQUID;
SOURCE 4 ORGANISM_TAXID: 6622;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRIESTERASE, BETA PROPELLER, CALCIUM BINDING, CALCIUM,
KEYWDS 2 HYDROLASE, METAL-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.-H.CHEN,M.-M.BLUM
REVDAT 4 01-NOV-23 3HLI 1 REMARK
REVDAT 3 10-NOV-21 3HLI 1 REMARK SEQADV LINK
REVDAT 2 08-DEC-09 3HLI 1 JRNL
REVDAT 1 10-NOV-09 3HLI 0
JRNL AUTH M.MELZER,J.C.CHEN,A.HEIDENREICH,J.GAB,M.KOLLER,K.KEHE,
JRNL AUTH 2 M.M.BLUM
JRNL TITL REVERSED ENANTIOSELECTIVITY OF DIISOPROPYL FLUOROPHOSPHATASE
JRNL TITL 2 AGAINST ORGANOPHOSPHORUS NERVE AGENTS BY RATIONAL DESIGN
JRNL REF J.AM.CHEM.SOC. V. 131 17226 2009
JRNL REFN ISSN 0002-7863
JRNL PMID 19894712
JRNL DOI 10.1021/JA905444G
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 213535
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 10622
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 1038
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65400
REMARK 3 B22 (A**2) : 0.91000
REMARK 3 B33 (A**2) : -0.25700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.455
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.79
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.779
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.971 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.505 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.854 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.704 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 35.21
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HLI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.007
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 213535
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : 0.05300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
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 (%) : 86.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : 0.30800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2GVW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL, 0.05M HEPES PH 7.5, 35%
REMARK 280 PENTAERYTHRIOL PROPOXYLATE (5/4 PO/OH), VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 37.24500
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, 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 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 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 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 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 MET A 1
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 MET D 1
REMARK 465 GLU D 2
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 GLU A 2 CG CD OE1 OE2
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 20 118.83 -25.28
REMARK 500 ALA A 45 44.41 -152.13
REMARK 500 THR A 145 156.45 177.60
REMARK 500 PHE A 173 66.94 61.64
REMARK 500 ASN A 175 -89.53 -130.47
REMARK 500 MET A 195 -71.17 -49.05
REMARK 500 ASP A 229 -113.86 -111.62
REMARK 500 LYS A 269 66.26 -118.62
REMARK 500 ALA B 20 120.71 -26.18
REMARK 500 ALA B 45 46.56 -152.61
REMARK 500 THR B 145 167.83 177.41
REMARK 500 LYS B 151 73.42 -111.74
REMARK 500 ALA B 170 34.83 73.45
REMARK 500 PHE B 173 68.77 62.25
REMARK 500 ASN B 175 -92.41 -129.08
REMARK 500 ASP B 229 -112.47 -110.85
REMARK 500 PRO B 266 30.13 -83.86
REMARK 500 ALA C 20 121.18 -27.52
REMARK 500 ALA C 45 46.08 -151.39
REMARK 500 THR C 145 147.62 -170.31
REMARK 500 SER C 147 37.36 -99.61
REMARK 500 ALA C 170 34.75 70.25
REMARK 500 PHE C 173 68.27 62.73
REMARK 500 ASN C 175 -90.92 -127.33
REMARK 500 ASP C 229 -113.05 -111.96
REMARK 500 PRO C 266 32.83 -83.70
REMARK 500 LYS C 269 66.62 -119.49
REMARK 500 ALA D 20 120.25 -26.99
REMARK 500 ALA D 45 44.74 -154.86
REMARK 500 PHE D 173 67.67 65.73
REMARK 500 ASN D 175 -90.67 -130.72
REMARK 500 MET D 195 -71.19 -49.59
REMARK 500 ASP D 229 -111.51 -112.24
REMARK 500 LYS D 269 64.12 -117.53
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 CA A 315 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 21 OE2
REMARK 620 2 ASN A 120 OD1 133.4
REMARK 620 3 ASN A 175 OD1 151.9 71.7
REMARK 620 4 ASP A 229 OD1 81.9 141.3 70.7
REMARK 620 5 HOH A 318 O 79.1 68.3 128.1 146.8
REMARK 620 6 HOH A 319 O 112.2 95.3 70.6 81.0 81.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 316 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 232 OD2
REMARK 620 2 LEU A 273 O 86.6
REMARK 620 3 HIS A 274 ND1 89.9 101.1
REMARK 620 4 HOH A 321 O 175.8 89.4 89.7
REMARK 620 5 HOH A 325 O 93.4 90.0 168.6 87.8
REMARK 620 6 HOH A 328 O 81.6 165.8 86.9 102.5 82.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 315 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 314 O
REMARK 620 2 GLU B 21 OE2 81.4
REMARK 620 3 ASN B 120 OD1 83.3 131.7
REMARK 620 4 ASN B 175 OD1 88.8 152.5 71.7
REMARK 620 5 ASP B 229 OD1 84.2 82.1 141.1 71.3
REMARK 620 6 HOH B 324 O 117.5 79.0 68.3 127.9 148.3
REMARK 620 7 HOH B 369 O 158.6 112.8 97.0 71.2 82.3 81.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 316 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 232 OD2
REMARK 620 2 LEU B 273 O 86.5
REMARK 620 3 HIS B 274 ND1 90.7 100.4
REMARK 620 4 HOH B 338 O 93.5 89.9 169.2
REMARK 620 5 HOH B 367 O 81.0 165.4 87.4 83.4
REMARK 620 6 HOH B 378 O 176.1 90.2 87.9 88.6 102.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 315 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 314 O
REMARK 620 2 GLU C 21 OE2 83.0
REMARK 620 3 ASN C 120 OD1 84.1 131.2
REMARK 620 4 ASN C 175 OD1 87.1 154.1 70.9
REMARK 620 5 ASP C 229 OD1 84.3 83.3 141.6 72.0
REMARK 620 6 HOH C 317 O 119.7 78.1 68.3 127.2 146.9
REMARK 620 7 HOH C 320 O 157.3 112.0 97.0 72.1 80.8 81.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 316 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 232 OD2
REMARK 620 2 LEU C 273 O 86.4
REMARK 620 3 HIS C 274 ND1 89.0 100.4
REMARK 620 4 HOH C 318 O 94.6 90.8 168.4
REMARK 620 5 HOH C 319 O 82.3 167.2 85.6 84.0
REMARK 620 6 HOH C 330 O 175.9 89.9 89.9 87.3 101.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 315 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 21 OE2
REMARK 620 2 ASN D 120 OD1 132.3
REMARK 620 3 ASN D 175 OD1 153.3 69.3
REMARK 620 4 ASP D 229 OD1 82.4 140.4 72.6
REMARK 620 5 HOH D 317 O 80.1 68.4 126.4 148.2
REMARK 620 6 HOH D 326 O 113.7 96.3 72.2 81.8 81.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 316 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 232 OD2
REMARK 620 2 LEU D 273 O 87.5
REMARK 620 3 HIS D 274 ND1 88.4 100.4
REMARK 620 4 HOH D 318 O 94.8 90.0 169.3
REMARK 620 5 HOH D 321 O 80.4 166.5 85.5 84.9
REMARK 620 6 HOH D 329 O 176.6 89.4 90.8 86.6 102.8
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 CA A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 316
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GVW RELATED DB: PDB
REMARK 900 RELATED ID: 3BYC RELATED DB: PDB
REMARK 900 RELATED ID: 2GVU RELATED DB: PDB
REMARK 900 RELATED ID: 2GVV RELATED DB: PDB
REMARK 900 RELATED ID: 2GVX RELATED DB: PDB
REMARK 900 RELATED ID: 1E1A RELATED DB: PDB
REMARK 900 RELATED ID: 3HLH RELATED DB: PDB
DBREF 3HLI A 1 314 UNP Q7SIG4 DFPA_LOLVU 1 314
DBREF 3HLI B 1 314 UNP Q7SIG4 DFPA_LOLVU 1 314
DBREF 3HLI C 1 314 UNP Q7SIG4 DFPA_LOLVU 1 314
DBREF 3HLI D 1 314 UNP Q7SIG4 DFPA_LOLVU 1 314
SEQADV 3HLI ASP A 37 UNP Q7SIG4 GLU 37 ENGINEERED MUTATION
SEQADV 3HLI ALA A 144 UNP Q7SIG4 TYR 144 ENGINEERED MUTATION
SEQADV 3HLI ALA A 146 UNP Q7SIG4 ARG 146 ENGINEERED MUTATION
SEQADV 3HLI MET A 195 UNP Q7SIG4 THR 195 ENGINEERED MUTATION
SEQADV 3HLI ASP B 37 UNP Q7SIG4 GLU 37 ENGINEERED MUTATION
SEQADV 3HLI ALA B 144 UNP Q7SIG4 TYR 144 ENGINEERED MUTATION
SEQADV 3HLI ALA B 146 UNP Q7SIG4 ARG 146 ENGINEERED MUTATION
SEQADV 3HLI MET B 195 UNP Q7SIG4 THR 195 ENGINEERED MUTATION
SEQADV 3HLI ASP C 37 UNP Q7SIG4 GLU 37 ENGINEERED MUTATION
SEQADV 3HLI ALA C 144 UNP Q7SIG4 TYR 144 ENGINEERED MUTATION
SEQADV 3HLI ALA C 146 UNP Q7SIG4 ARG 146 ENGINEERED MUTATION
SEQADV 3HLI MET C 195 UNP Q7SIG4 THR 195 ENGINEERED MUTATION
SEQADV 3HLI ASP D 37 UNP Q7SIG4 GLU 37 ENGINEERED MUTATION
SEQADV 3HLI ALA D 144 UNP Q7SIG4 TYR 144 ENGINEERED MUTATION
SEQADV 3HLI ALA D 146 UNP Q7SIG4 ARG 146 ENGINEERED MUTATION
SEQADV 3HLI MET D 195 UNP Q7SIG4 THR 195 ENGINEERED MUTATION
SEQRES 1 A 314 MET GLU ILE PRO VAL ILE GLU PRO LEU PHE THR LYS VAL
SEQRES 2 A 314 THR GLU ASP ILE PRO GLY ALA GLU GLY PRO VAL PHE ASP
SEQRES 3 A 314 LYS ASN GLY ASP PHE TYR ILE VAL ALA PRO ASP VAL GLU
SEQRES 4 A 314 VAL ASN GLY LYS PRO ALA GLY GLU ILE LEU ARG ILE ASP
SEQRES 5 A 314 LEU LYS THR GLY LYS LYS THR VAL ILE CYS LYS PRO GLU
SEQRES 6 A 314 VAL ASN GLY TYR GLY GLY ILE PRO ALA GLY CYS GLN CYS
SEQRES 7 A 314 ASP ARG ASP ALA ASN GLN LEU PHE VAL ALA ASP MET ARG
SEQRES 8 A 314 LEU GLY LEU LEU VAL VAL GLN THR ASP GLY THR PHE GLU
SEQRES 9 A 314 GLU ILE ALA LYS LYS ASP SER GLU GLY ARG ARG MET GLN
SEQRES 10 A 314 GLY CYS ASN ASP CYS ALA PHE ASP TYR GLU GLY ASN LEU
SEQRES 11 A 314 TRP ILE THR ALA PRO ALA GLY GLU VAL ALA PRO ALA ASP
SEQRES 12 A 314 ALA THR ALA SER MET GLN GLU LYS PHE GLY SER ILE TYR
SEQRES 13 A 314 CYS PHE THR THR ASP GLY GLN MET ILE GLN VAL ASP THR
SEQRES 14 A 314 ALA PHE GLN PHE PRO ASN GLY ILE ALA VAL ARG HIS MET
SEQRES 15 A 314 ASN ASP GLY ARG PRO TYR GLN LEU ILE VAL ALA GLU MET
SEQRES 16 A 314 PRO THR LYS LYS LEU TRP SER TYR ASP ILE LYS GLY PRO
SEQRES 17 A 314 ALA LYS ILE GLU ASN LYS LYS VAL TRP GLY HIS ILE PRO
SEQRES 18 A 314 GLY THR HIS GLU GLY GLY ALA ASP GLY MET ASP PHE ASP
SEQRES 19 A 314 GLU ASP ASN ASN LEU LEU VAL ALA ASN TRP GLY SER SER
SEQRES 20 A 314 HIS ILE GLU VAL PHE GLY PRO ASP GLY GLY GLN PRO LYS
SEQRES 21 A 314 MET ARG ILE ARG CYS PRO PHE GLU LYS PRO SER ASN LEU
SEQRES 22 A 314 HIS PHE LYS PRO GLN THR LYS THR ILE PHE VAL THR GLU
SEQRES 23 A 314 HIS GLU ASN ASN ALA VAL TRP LYS PHE GLU TRP GLN ARG
SEQRES 24 A 314 ASN GLY LYS LYS GLN TYR CYS GLU THR LEU LYS PHE GLY
SEQRES 25 A 314 ILE PHE
SEQRES 1 B 314 MET GLU ILE PRO VAL ILE GLU PRO LEU PHE THR LYS VAL
SEQRES 2 B 314 THR GLU ASP ILE PRO GLY ALA GLU GLY PRO VAL PHE ASP
SEQRES 3 B 314 LYS ASN GLY ASP PHE TYR ILE VAL ALA PRO ASP VAL GLU
SEQRES 4 B 314 VAL ASN GLY LYS PRO ALA GLY GLU ILE LEU ARG ILE ASP
SEQRES 5 B 314 LEU LYS THR GLY LYS LYS THR VAL ILE CYS LYS PRO GLU
SEQRES 6 B 314 VAL ASN GLY TYR GLY GLY ILE PRO ALA GLY CYS GLN CYS
SEQRES 7 B 314 ASP ARG ASP ALA ASN GLN LEU PHE VAL ALA ASP MET ARG
SEQRES 8 B 314 LEU GLY LEU LEU VAL VAL GLN THR ASP GLY THR PHE GLU
SEQRES 9 B 314 GLU ILE ALA LYS LYS ASP SER GLU GLY ARG ARG MET GLN
SEQRES 10 B 314 GLY CYS ASN ASP CYS ALA PHE ASP TYR GLU GLY ASN LEU
SEQRES 11 B 314 TRP ILE THR ALA PRO ALA GLY GLU VAL ALA PRO ALA ASP
SEQRES 12 B 314 ALA THR ALA SER MET GLN GLU LYS PHE GLY SER ILE TYR
SEQRES 13 B 314 CYS PHE THR THR ASP GLY GLN MET ILE GLN VAL ASP THR
SEQRES 14 B 314 ALA PHE GLN PHE PRO ASN GLY ILE ALA VAL ARG HIS MET
SEQRES 15 B 314 ASN ASP GLY ARG PRO TYR GLN LEU ILE VAL ALA GLU MET
SEQRES 16 B 314 PRO THR LYS LYS LEU TRP SER TYR ASP ILE LYS GLY PRO
SEQRES 17 B 314 ALA LYS ILE GLU ASN LYS LYS VAL TRP GLY HIS ILE PRO
SEQRES 18 B 314 GLY THR HIS GLU GLY GLY ALA ASP GLY MET ASP PHE ASP
SEQRES 19 B 314 GLU ASP ASN ASN LEU LEU VAL ALA ASN TRP GLY SER SER
SEQRES 20 B 314 HIS ILE GLU VAL PHE GLY PRO ASP GLY GLY GLN PRO LYS
SEQRES 21 B 314 MET ARG ILE ARG CYS PRO PHE GLU LYS PRO SER ASN LEU
SEQRES 22 B 314 HIS PHE LYS PRO GLN THR LYS THR ILE PHE VAL THR GLU
SEQRES 23 B 314 HIS GLU ASN ASN ALA VAL TRP LYS PHE GLU TRP GLN ARG
SEQRES 24 B 314 ASN GLY LYS LYS GLN TYR CYS GLU THR LEU LYS PHE GLY
SEQRES 25 B 314 ILE PHE
SEQRES 1 C 314 MET GLU ILE PRO VAL ILE GLU PRO LEU PHE THR LYS VAL
SEQRES 2 C 314 THR GLU ASP ILE PRO GLY ALA GLU GLY PRO VAL PHE ASP
SEQRES 3 C 314 LYS ASN GLY ASP PHE TYR ILE VAL ALA PRO ASP VAL GLU
SEQRES 4 C 314 VAL ASN GLY LYS PRO ALA GLY GLU ILE LEU ARG ILE ASP
SEQRES 5 C 314 LEU LYS THR GLY LYS LYS THR VAL ILE CYS LYS PRO GLU
SEQRES 6 C 314 VAL ASN GLY TYR GLY GLY ILE PRO ALA GLY CYS GLN CYS
SEQRES 7 C 314 ASP ARG ASP ALA ASN GLN LEU PHE VAL ALA ASP MET ARG
SEQRES 8 C 314 LEU GLY LEU LEU VAL VAL GLN THR ASP GLY THR PHE GLU
SEQRES 9 C 314 GLU ILE ALA LYS LYS ASP SER GLU GLY ARG ARG MET GLN
SEQRES 10 C 314 GLY CYS ASN ASP CYS ALA PHE ASP TYR GLU GLY ASN LEU
SEQRES 11 C 314 TRP ILE THR ALA PRO ALA GLY GLU VAL ALA PRO ALA ASP
SEQRES 12 C 314 ALA THR ALA SER MET GLN GLU LYS PHE GLY SER ILE TYR
SEQRES 13 C 314 CYS PHE THR THR ASP GLY GLN MET ILE GLN VAL ASP THR
SEQRES 14 C 314 ALA PHE GLN PHE PRO ASN GLY ILE ALA VAL ARG HIS MET
SEQRES 15 C 314 ASN ASP GLY ARG PRO TYR GLN LEU ILE VAL ALA GLU MET
SEQRES 16 C 314 PRO THR LYS LYS LEU TRP SER TYR ASP ILE LYS GLY PRO
SEQRES 17 C 314 ALA LYS ILE GLU ASN LYS LYS VAL TRP GLY HIS ILE PRO
SEQRES 18 C 314 GLY THR HIS GLU GLY GLY ALA ASP GLY MET ASP PHE ASP
SEQRES 19 C 314 GLU ASP ASN ASN LEU LEU VAL ALA ASN TRP GLY SER SER
SEQRES 20 C 314 HIS ILE GLU VAL PHE GLY PRO ASP GLY GLY GLN PRO LYS
SEQRES 21 C 314 MET ARG ILE ARG CYS PRO PHE GLU LYS PRO SER ASN LEU
SEQRES 22 C 314 HIS PHE LYS PRO GLN THR LYS THR ILE PHE VAL THR GLU
SEQRES 23 C 314 HIS GLU ASN ASN ALA VAL TRP LYS PHE GLU TRP GLN ARG
SEQRES 24 C 314 ASN GLY LYS LYS GLN TYR CYS GLU THR LEU LYS PHE GLY
SEQRES 25 C 314 ILE PHE
SEQRES 1 D 314 MET GLU ILE PRO VAL ILE GLU PRO LEU PHE THR LYS VAL
SEQRES 2 D 314 THR GLU ASP ILE PRO GLY ALA GLU GLY PRO VAL PHE ASP
SEQRES 3 D 314 LYS ASN GLY ASP PHE TYR ILE VAL ALA PRO ASP VAL GLU
SEQRES 4 D 314 VAL ASN GLY LYS PRO ALA GLY GLU ILE LEU ARG ILE ASP
SEQRES 5 D 314 LEU LYS THR GLY LYS LYS THR VAL ILE CYS LYS PRO GLU
SEQRES 6 D 314 VAL ASN GLY TYR GLY GLY ILE PRO ALA GLY CYS GLN CYS
SEQRES 7 D 314 ASP ARG ASP ALA ASN GLN LEU PHE VAL ALA ASP MET ARG
SEQRES 8 D 314 LEU GLY LEU LEU VAL VAL GLN THR ASP GLY THR PHE GLU
SEQRES 9 D 314 GLU ILE ALA LYS LYS ASP SER GLU GLY ARG ARG MET GLN
SEQRES 10 D 314 GLY CYS ASN ASP CYS ALA PHE ASP TYR GLU GLY ASN LEU
SEQRES 11 D 314 TRP ILE THR ALA PRO ALA GLY GLU VAL ALA PRO ALA ASP
SEQRES 12 D 314 ALA THR ALA SER MET GLN GLU LYS PHE GLY SER ILE TYR
SEQRES 13 D 314 CYS PHE THR THR ASP GLY GLN MET ILE GLN VAL ASP THR
SEQRES 14 D 314 ALA PHE GLN PHE PRO ASN GLY ILE ALA VAL ARG HIS MET
SEQRES 15 D 314 ASN ASP GLY ARG PRO TYR GLN LEU ILE VAL ALA GLU MET
SEQRES 16 D 314 PRO THR LYS LYS LEU TRP SER TYR ASP ILE LYS GLY PRO
SEQRES 17 D 314 ALA LYS ILE GLU ASN LYS LYS VAL TRP GLY HIS ILE PRO
SEQRES 18 D 314 GLY THR HIS GLU GLY GLY ALA ASP GLY MET ASP PHE ASP
SEQRES 19 D 314 GLU ASP ASN ASN LEU LEU VAL ALA ASN TRP GLY SER SER
SEQRES 20 D 314 HIS ILE GLU VAL PHE GLY PRO ASP GLY GLY GLN PRO LYS
SEQRES 21 D 314 MET ARG ILE ARG CYS PRO PHE GLU LYS PRO SER ASN LEU
SEQRES 22 D 314 HIS PHE LYS PRO GLN THR LYS THR ILE PHE VAL THR GLU
SEQRES 23 D 314 HIS GLU ASN ASN ALA VAL TRP LYS PHE GLU TRP GLN ARG
SEQRES 24 D 314 ASN GLY LYS LYS GLN TYR CYS GLU THR LEU LYS PHE GLY
SEQRES 25 D 314 ILE PHE
HET CA A 315 1
HET CA A 316 1
HET CA B 315 1
HET CA B 316 1
HET CA C 315 1
HET CA C 316 1
HET CA D 315 1
HET CA D 316 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 8(CA 2+)
FORMUL 13 HOH *1038(H2 O)
HELIX 1 1 GLN A 304 THR A 308 5 5
HELIX 2 2 GLN B 304 THR B 308 5 5
HELIX 3 3 GLN C 304 THR C 308 5 5
HELIX 4 4 GLN D 304 THR D 308 5 5
SHEET 1 A 5 VAL A 5 ILE A 6 0
SHEET 2 A 5 MET A 261 ARG A 264 1 O ARG A 264 N ILE A 6
SHEET 3 A 5 HIS A 248 PHE A 252 -1 N ILE A 249 O ILE A 263
SHEET 4 A 5 LEU A 239 TRP A 244 -1 N VAL A 241 O GLU A 250
SHEET 5 A 5 GLY A 227 PHE A 233 -1 N ASP A 232 O LEU A 240
SHEET 1 B 4 THR A 11 THR A 14 0
SHEET 2 B 4 ALA A 291 GLU A 296 -1 O VAL A 292 N VAL A 13
SHEET 3 B 4 THR A 281 GLU A 286 -1 N ILE A 282 O PHE A 295
SHEET 4 B 4 PRO A 270 PHE A 275 -1 N HIS A 274 O PHE A 283
SHEET 1 C 4 GLU A 21 PHE A 25 0
SHEET 2 C 4 PHE A 31 ALA A 35 -1 O TYR A 32 N VAL A 24
SHEET 3 C 4 GLU A 47 ILE A 51 -1 O LEU A 49 N ILE A 33
SHEET 4 C 4 LYS A 58 CYS A 62 -1 O THR A 59 N ARG A 50
SHEET 1 D 2 GLU A 39 VAL A 40 0
SHEET 2 D 2 LYS A 43 PRO A 44 -1 O LYS A 43 N VAL A 40
SHEET 1 E 2 GLU A 65 VAL A 66 0
SHEET 2 E 2 TYR A 69 GLY A 70 -1 O TYR A 69 N VAL A 66
SHEET 1 F 4 PRO A 73 CYS A 78 0
SHEET 2 F 4 GLN A 84 ASP A 89 -1 O ALA A 88 N ALA A 74
SHEET 3 F 4 GLY A 93 GLN A 98 -1 O GLY A 93 N ASP A 89
SHEET 4 F 4 PHE A 103 GLU A 105 -1 O GLU A 104 N VAL A 96
SHEET 1 G 4 CYS A 122 PHE A 124 0
SHEET 2 G 4 LEU A 130 ALA A 134 -1 O TRP A 131 N ALA A 123
SHEET 3 G 4 GLY A 153 PHE A 158 -1 O TYR A 156 N ILE A 132
SHEET 4 G 4 MET A 164 PHE A 171 -1 O PHE A 171 N GLY A 153
SHEET 1 H 4 PRO A 174 HIS A 181 0
SHEET 2 H 4 PRO A 187 GLU A 194 -1 O GLN A 189 N ARG A 180
SHEET 3 H 4 LYS A 199 GLY A 207 -1 O TRP A 201 N VAL A 192
SHEET 4 H 4 LYS A 210 HIS A 219 -1 O LYS A 210 N LYS A 206
SHEET 1 I 5 VAL B 5 ILE B 6 0
SHEET 2 I 5 MET B 261 ARG B 264 1 O ARG B 262 N ILE B 6
SHEET 3 I 5 HIS B 248 PHE B 252 -1 N VAL B 251 O MET B 261
SHEET 4 I 5 LEU B 239 TRP B 244 -1 N LEU B 239 O PHE B 252
SHEET 5 I 5 GLY B 227 PHE B 233 -1 N ASP B 232 O LEU B 240
SHEET 1 J 4 THR B 11 THR B 14 0
SHEET 2 J 4 ALA B 291 GLU B 296 -1 O VAL B 292 N VAL B 13
SHEET 3 J 4 THR B 281 GLU B 286 -1 N ILE B 282 O PHE B 295
SHEET 4 J 4 PRO B 270 PHE B 275 -1 N HIS B 274 O PHE B 283
SHEET 1 K 4 GLU B 21 PHE B 25 0
SHEET 2 K 4 PHE B 31 ALA B 35 -1 O TYR B 32 N VAL B 24
SHEET 3 K 4 GLU B 47 ILE B 51 -1 O GLU B 47 N ALA B 35
SHEET 4 K 4 LYS B 58 CYS B 62 -1 O THR B 59 N ARG B 50
SHEET 1 L 2 GLU B 39 VAL B 40 0
SHEET 2 L 2 LYS B 43 PRO B 44 -1 O LYS B 43 N VAL B 40
SHEET 1 M 2 GLU B 65 VAL B 66 0
SHEET 2 M 2 TYR B 69 GLY B 70 -1 O TYR B 69 N VAL B 66
SHEET 1 N 4 PRO B 73 CYS B 78 0
SHEET 2 N 4 GLN B 84 ASP B 89 -1 O PHE B 86 N GLN B 77
SHEET 3 N 4 GLY B 93 GLN B 98 -1 O GLY B 93 N ASP B 89
SHEET 4 N 4 PHE B 103 GLU B 105 -1 O GLU B 104 N VAL B 96
SHEET 1 O 4 ASP B 121 PHE B 124 0
SHEET 2 O 4 LEU B 130 ALA B 134 -1 O TRP B 131 N ALA B 123
SHEET 3 O 4 GLY B 153 PHE B 158 -1 O SER B 154 N ALA B 134
SHEET 4 O 4 MET B 164 PHE B 171 -1 O ASP B 168 N ILE B 155
SHEET 1 P 4 PRO B 174 HIS B 181 0
SHEET 2 P 4 PRO B 187 GLU B 194 -1 O GLN B 189 N ARG B 180
SHEET 3 P 4 LYS B 199 GLY B 207 -1 O TRP B 201 N VAL B 192
SHEET 4 P 4 LYS B 210 HIS B 219 -1 O LYS B 215 N SER B 202
SHEET 1 Q 5 VAL C 5 ILE C 6 0
SHEET 2 Q 5 MET C 261 ARG C 264 1 O ARG C 264 N ILE C 6
SHEET 3 Q 5 HIS C 248 PHE C 252 -1 N ILE C 249 O ILE C 263
SHEET 4 Q 5 LEU C 239 TRP C 244 -1 N VAL C 241 O GLU C 250
SHEET 5 Q 5 GLY C 227 PHE C 233 -1 N ASP C 232 O LEU C 240
SHEET 1 R 4 THR C 11 THR C 14 0
SHEET 2 R 4 ALA C 291 GLU C 296 -1 O VAL C 292 N VAL C 13
SHEET 3 R 4 THR C 281 GLU C 286 -1 N ILE C 282 O PHE C 295
SHEET 4 R 4 PRO C 270 PHE C 275 -1 N HIS C 274 O PHE C 283
SHEET 1 S 4 GLU C 21 PHE C 25 0
SHEET 2 S 4 PHE C 31 ALA C 35 -1 O TYR C 32 N VAL C 24
SHEET 3 S 4 GLU C 47 ILE C 51 -1 O LEU C 49 N ILE C 33
SHEET 4 S 4 LYS C 58 CYS C 62 -1 O ILE C 61 N ILE C 48
SHEET 1 T 2 GLU C 39 VAL C 40 0
SHEET 2 T 2 LYS C 43 PRO C 44 -1 O LYS C 43 N VAL C 40
SHEET 1 U 2 GLU C 65 VAL C 66 0
SHEET 2 U 2 TYR C 69 GLY C 70 -1 O TYR C 69 N VAL C 66
SHEET 1 V 4 PRO C 73 CYS C 78 0
SHEET 2 V 4 GLN C 84 ASP C 89 -1 O ALA C 88 N ALA C 74
SHEET 3 V 4 GLY C 93 GLN C 98 -1 O GLY C 93 N ASP C 89
SHEET 4 V 4 PHE C 103 GLU C 105 -1 O GLU C 104 N VAL C 96
SHEET 1 W 4 CYS C 122 PHE C 124 0
SHEET 2 W 4 LEU C 130 ALA C 134 -1 O TRP C 131 N ALA C 123
SHEET 3 W 4 GLY C 153 PHE C 158 -1 O SER C 154 N ALA C 134
SHEET 4 W 4 MET C 164 PHE C 171 -1 O PHE C 171 N GLY C 153
SHEET 1 X 4 PRO C 174 HIS C 181 0
SHEET 2 X 4 PRO C 187 GLU C 194 -1 O GLN C 189 N ARG C 180
SHEET 3 X 4 LYS C 199 GLY C 207 -1 O TRP C 201 N VAL C 192
SHEET 4 X 4 LYS C 210 HIS C 219 -1 O TRP C 217 N LEU C 200
SHEET 1 Y 5 VAL D 5 ILE D 6 0
SHEET 2 Y 5 MET D 261 ARG D 264 1 O ARG D 264 N ILE D 6
SHEET 3 Y 5 HIS D 248 PHE D 252 -1 N ILE D 249 O ILE D 263
SHEET 4 Y 5 LEU D 239 TRP D 244 -1 N VAL D 241 O GLU D 250
SHEET 5 Y 5 GLY D 227 PHE D 233 -1 N ASP D 232 O LEU D 240
SHEET 1 Z 4 THR D 11 THR D 14 0
SHEET 2 Z 4 ALA D 291 GLU D 296 -1 O VAL D 292 N VAL D 13
SHEET 3 Z 4 THR D 281 GLU D 286 -1 N ILE D 282 O PHE D 295
SHEET 4 Z 4 PRO D 270 PHE D 275 -1 N HIS D 274 O PHE D 283
SHEET 1 AA 4 GLU D 21 PHE D 25 0
SHEET 2 AA 4 PHE D 31 ALA D 35 -1 O TYR D 32 N VAL D 24
SHEET 3 AA 4 GLU D 47 ILE D 51 -1 O LEU D 49 N ILE D 33
SHEET 4 AA 4 LYS D 58 CYS D 62 -1 O THR D 59 N ARG D 50
SHEET 1 AB 2 GLU D 39 VAL D 40 0
SHEET 2 AB 2 LYS D 43 PRO D 44 -1 O LYS D 43 N VAL D 40
SHEET 1 AC 2 GLU D 65 VAL D 66 0
SHEET 2 AC 2 TYR D 69 GLY D 70 -1 O TYR D 69 N VAL D 66
SHEET 1 AD 4 PRO D 73 CYS D 78 0
SHEET 2 AD 4 GLN D 84 ASP D 89 -1 O ALA D 88 N ALA D 74
SHEET 3 AD 4 GLY D 93 GLN D 98 -1 O GLY D 93 N ASP D 89
SHEET 4 AD 4 PHE D 103 GLU D 105 -1 O GLU D 104 N VAL D 96
SHEET 1 AE 4 CYS D 122 PHE D 124 0
SHEET 2 AE 4 LEU D 130 ALA D 134 -1 O TRP D 131 N ALA D 123
SHEET 3 AE 4 GLY D 153 PHE D 158 -1 O PHE D 158 N LEU D 130
SHEET 4 AE 4 MET D 164 PHE D 171 -1 O PHE D 171 N GLY D 153
SHEET 1 AF 4 PRO D 174 HIS D 181 0
SHEET 2 AF 4 PRO D 187 GLU D 194 -1 O GLN D 189 N ARG D 180
SHEET 3 AF 4 LYS D 199 GLY D 207 -1 O TRP D 201 N VAL D 192
SHEET 4 AF 4 LYS D 210 HIS D 219 -1 O LYS D 210 N LYS D 206
LINK OE2 GLU A 21 CA CA A 315 1555 1555 2.29
LINK OD1 ASN A 120 CA CA A 315 1555 1555 2.44
LINK OD1 ASN A 175 CA CA A 315 1555 1555 2.33
LINK OD1 ASP A 229 CA CA A 315 1555 1555 2.37
LINK OD2 ASP A 232 CA CA A 316 1555 1555 2.22
LINK O LEU A 273 CA CA A 316 1555 1555 2.32
LINK ND1 HIS A 274 CA CA A 316 1555 1555 2.49
LINK O PHE A 314 CA CA B 315 1555 1555 2.37
LINK CA CA A 315 O HOH A 318 1555 1555 2.45
LINK CA CA A 315 O HOH A 319 1555 1555 2.43
LINK CA CA A 316 O HOH A 321 1555 1555 2.33
LINK CA CA A 316 O HOH A 325 1555 1555 2.30
LINK CA CA A 316 O HOH A 328 1555 1555 2.37
LINK OE2 GLU B 21 CA CA B 315 1555 1555 2.30
LINK OD1 ASN B 120 CA CA B 315 1555 1555 2.48
LINK OD1 ASN B 175 CA CA B 315 1555 1555 2.30
LINK OD1 ASP B 229 CA CA B 315 1555 1555 2.38
LINK OD2 ASP B 232 CA CA B 316 1555 1555 2.19
LINK O LEU B 273 CA CA B 316 1555 1555 2.34
LINK ND1 HIS B 274 CA CA B 316 1555 1555 2.46
LINK O PHE B 314 CA CA C 315 1555 1555 2.33
LINK CA CA B 315 O HOH B 324 1555 1555 2.48
LINK CA CA B 315 O HOH B 369 1555 1555 2.40
LINK CA CA B 316 O HOH B 338 1555 1555 2.28
LINK CA CA B 316 O HOH B 367 1555 1555 2.38
LINK CA CA B 316 O HOH B 378 1555 1555 2.30
LINK OE2 GLU C 21 CA CA C 315 1555 1555 2.29
LINK OD1 ASN C 120 CA CA C 315 1555 1555 2.42
LINK OD1 ASN C 175 CA CA C 315 1555 1555 2.35
LINK OD1 ASP C 229 CA CA C 315 1555 1555 2.36
LINK OD2 ASP C 232 CA CA C 316 1555 1555 2.20
LINK O LEU C 273 CA CA C 316 1555 1555 2.33
LINK ND1 HIS C 274 CA CA C 316 1555 1555 2.48
LINK CA CA C 315 O HOH C 317 1555 1555 2.45
LINK CA CA C 315 O HOH C 320 1555 1555 2.39
LINK CA CA C 316 O HOH C 318 1555 1555 2.28
LINK CA CA C 316 O HOH C 319 1555 1555 2.41
LINK CA CA C 316 O HOH C 330 1555 1555 2.32
LINK OE2 GLU D 21 CA CA D 315 1555 1555 2.29
LINK OD1 ASN D 120 CA CA D 315 1555 1555 2.45
LINK OD1 ASN D 175 CA CA D 315 1555 1555 2.32
LINK OD1 ASP D 229 CA CA D 315 1555 1555 2.37
LINK OD2 ASP D 232 CA CA D 316 1555 1555 2.19
LINK O LEU D 273 CA CA D 316 1555 1555 2.34
LINK ND1 HIS D 274 CA CA D 316 1555 1555 2.46
LINK CA CA D 315 O HOH D 317 1555 1555 2.47
LINK CA CA D 315 O HOH D 326 1555 1555 2.39
LINK CA CA D 316 O HOH D 318 1555 1555 2.23
LINK CA CA D 316 O HOH D 321 1555 1555 2.40
LINK CA CA D 316 O HOH D 329 1555 1555 2.33
CISPEP 1 ALA A 140 PRO A 141 0 0.32
CISPEP 2 ALA B 140 PRO B 141 0 0.27
CISPEP 3 ALA C 140 PRO C 141 0 0.31
CISPEP 4 ALA D 140 PRO D 141 0 0.32
SITE 1 AC1 6 GLU A 21 ASN A 120 ASN A 175 ASP A 229
SITE 2 AC1 6 HOH A 318 HOH A 319
SITE 1 AC2 6 ASP A 232 LEU A 273 HIS A 274 HOH A 321
SITE 2 AC2 6 HOH A 325 HOH A 328
SITE 1 AC3 7 PHE A 314 GLU B 21 ASN B 120 ASN B 175
SITE 2 AC3 7 ASP B 229 HOH B 324 HOH B 369
SITE 1 AC4 6 ASP B 232 LEU B 273 HIS B 274 HOH B 338
SITE 2 AC4 6 HOH B 367 HOH B 378
SITE 1 AC5 7 PHE B 314 GLU C 21 ASN C 120 ASN C 175
SITE 2 AC5 7 ASP C 229 HOH C 317 HOH C 320
SITE 1 AC6 6 ASP C 232 LEU C 273 HIS C 274 HOH C 318
SITE 2 AC6 6 HOH C 319 HOH C 330
SITE 1 AC7 6 GLU D 21 ASN D 120 ASN D 175 ASP D 229
SITE 2 AC7 6 HOH D 317 HOH D 326
SITE 1 AC8 6 ASP D 232 LEU D 273 HIS D 274 HOH D 318
SITE 2 AC8 6 HOH D 321 HOH D 329
CRYST1 66.950 74.490 118.950 90.00 100.00 90.00 P 1 21 1 8
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 0.014937 0.000000 0.002634 0.00000
SCALE2 0.000000 0.013425 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008537 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
