HEADER HYDROLASE 19-OCT-01 1K7I
TITLE PRTC FROM ERWINIA CHRYSANTHEMI: Y228F MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SECRETED PROTEASE C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROC;
COMPND 5 EC: 3.4.24.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERWINIA CHRYSANTHEMI;
SOURCE 3 ORGANISM_TAXID: 556;
SOURCE 4 GENE: PRTC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METALLOPROTEASE, HYDROLASE, PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.BAUMANN,T.HEGE
REVDAT 4 07-FEB-24 1K7I 1 REMARK
REVDAT 3 27-OCT-21 1K7I 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1K7I 1 VERSN
REVDAT 1 19-OCT-02 1K7I 0
JRNL AUTH T.HEGE,U.BAUMANN
JRNL TITL PROTEASE C OF ERWINIA CHRYSANTHEMI: THE CRYSTAL STRUCTURE
JRNL TITL 2 AND ROLE OF AMINO ACIDS Y228 AND E189
JRNL REF J.MOL.BIOL. V. 314 187 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11718553
JRNL DOI 10.1006/JMBI.2001.5124
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.98
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) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 98323
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) : 0.197
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2024
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6337
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3519
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 521
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.95000
REMARK 3 B22 (A**2) : 0.95000
REMARK 3 B33 (A**2) : -1.90000
REMARK 3 B12 (A**2) : 0.51000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 49.82
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014657.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 577315
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 14.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, PH 6.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.76600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.53200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.53200
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.76600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 GLY A 2
REMARK 465 LYS A 3
REMARK 465 ASN A 4
REMARK 465 LEU A 5
REMARK 465 SER A 6
REMARK 465 LEU A 7
REMARK 465 ARG A 8
REMARK 465 GLN A 9
REMARK 465 ASP A 10
REMARK 465 ASP A 11
REMARK 465 ALA A 12
REMARK 465 GLN A 13
REMARK 465 HIS A 14
REMARK 465 ALA A 15
REMARK 465 LEU A 16
REMARK 465 SER A 17
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 ASP A 38 -134.19 55.90
REMARK 500 ASN A 355 -162.19 -124.29
REMARK 500 ALA A 400 61.03 -155.32
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 ZN A 486 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 HIS A 192 NE2 103.2
REMARK 620 3 HIS A 198 NE2 111.9 99.1
REMARK 620 4 HOH A 798 O 111.6 114.3 115.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 480 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 265 O
REMARK 620 2 GLY A 267 O 97.0
REMARK 620 3 SER A 269 OG 84.9 79.9
REMARK 620 4 ASP A 297 OD1 79.7 154.6 124.4
REMARK 620 5 ASP A 297 OD2 90.4 154.1 76.1 51.2
REMARK 620 6 GLY A 299 O 85.9 79.8 156.6 74.8 125.6
REMARK 620 7 ASP A 302 OD1 143.2 114.3 118.1 63.7 70.1 81.3
REMARK 620 8 ASP A 302 OD2 169.3 85.2 85.1 102.8 83.3 104.8 41.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 481 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 300 O
REMARK 620 2 ASP A 302 OD1 87.1
REMARK 620 3 THR A 339 O 167.5 93.3
REMARK 620 4 GLU A 341 OE2 85.6 87.2 81.9
REMARK 620 5 GLU A 341 OE1 87.2 136.9 84.0 49.8
REMARK 620 6 HOH A 653 O 102.0 75.1 90.2 160.3 147.6
REMARK 620 7 HOH A 797 O 88.1 146.2 98.4 125.7 76.1 73.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 482 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 346 O
REMARK 620 2 GLY A 348 O 101.8
REMARK 620 3 ASP A 350 OD2 86.7 86.5
REMARK 620 4 GLY A 363 O 82.7 174.7 91.1
REMARK 620 5 ALA A 365 O 76.7 80.9 156.6 102.9
REMARK 620 6 ASP A 368 OD1 170.8 78.0 84.1 97.1 112.2
REMARK 620 7 ASP A 368 OD2 138.9 109.4 120.5 67.9 82.5 47.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 483 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 355 O
REMARK 620 2 ALA A 357 O 88.4
REMARK 620 3 ASN A 359 OD1 82.4 82.6
REMARK 620 4 GLY A 372 O 86.6 168.9 87.0
REMARK 620 5 ALA A 374 O 84.4 89.5 164.7 99.9
REMARK 620 6 ASP A 377 OD2 149.0 119.8 111.8 67.7 83.4
REMARK 620 7 ASP A 377 OD1 161.3 82.2 80.4 99.7 111.5 47.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 484 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 364 O
REMARK 620 2 GLY A 366 O 108.0
REMARK 620 3 ASP A 368 OD2 80.2 81.1
REMARK 620 4 GLY A 381 O 79.5 169.6 93.5
REMARK 620 5 ALA A 383 O 82.3 75.3 144.5 113.3
REMARK 620 6 ASP A 386 OD1 154.7 82.6 79.0 87.7 122.9
REMARK 620 7 ASP A 386 OD2 139.1 109.4 121.3 65.9 91.7 47.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 487 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 373 O
REMARK 620 2 GLY A 375 O 109.8
REMARK 620 3 ASP A 377 OD2 90.4 88.2
REMARK 620 4 ASP A 395 O 83.0 89.1 171.5
REMARK 620 5 ASP A 402 OD1 164.4 85.7 88.7 99.1
REMARK 620 6 HOH A 534 O 80.4 168.9 87.4 96.7 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 485 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 382 O
REMARK 620 2 GLY A 384 O 109.3
REMARK 620 3 ASP A 386 OD2 78.2 86.8
REMARK 620 4 GLN A 408 OE1 91.2 85.1 163.8
REMARK 620 5 ASP A 412 OD1 162.3 83.8 91.1 102.0
REMARK 620 6 ASP A 412 OD2 131.0 118.4 113.2 83.0 41.3
REMARK 620 7 HOH A 505 O 83.2 166.5 91.0 100.0 82.9 50.7
REMARK 620 N 1 2 3 4 5 6
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 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 487
DBREF 1K7I A 1 479 UNP P16317 PRTC_ERWCH 1 479
SEQADV 1K7I PHE A 228 UNP P16317 TYR 228 ENGINEERED MUTATION
SEQRES 1 A 479 MET GLY LYS ASN LEU SER LEU ARG GLN ASP ASP ALA GLN
SEQRES 2 A 479 HIS ALA LEU SER ALA ASN THR SER SER ALA TYR ASN SER
SEQRES 3 A 479 VAL TYR ASP PHE LEU ARG TYR HIS ASP ARG GLY ASP GLY
SEQRES 4 A 479 LEU THR VAL ASN GLY LYS THR SER TYR SER ILE ASP GLN
SEQRES 5 A 479 ALA ALA ALA GLN ILE THR ARG GLU ASN VAL SER TRP ASN
SEQRES 6 A 479 GLY THR ASN VAL PHE GLY LYS SER ALA ASN LEU THR PHE
SEQRES 7 A 479 LYS PHE LEU GLN SER VAL SER SER ILE PRO SER GLY ASP
SEQRES 8 A 479 THR GLY PHE VAL LYS PHE ASN ALA GLU GLN ILE GLU GLN
SEQRES 9 A 479 ALA LYS LEU SER LEU GLN SER TRP SER ASP VAL ALA ASN
SEQRES 10 A 479 LEU THR PHE THR GLU VAL THR GLY ASN LYS SER ALA ASN
SEQRES 11 A 479 ILE THR PHE GLY ASN TYR THR ARG ASP ALA SER GLY ASN
SEQRES 12 A 479 LEU ASP TYR GLY THR GLN ALA TYR ALA TYR TYR PRO GLY
SEQRES 13 A 479 ASN TYR GLN GLY ALA GLY SER SER TRP TYR ASN TYR ASN
SEQRES 14 A 479 GLN SER ASN ILE ARG ASN PRO GLY SER GLU GLU TYR GLY
SEQRES 15 A 479 ARG GLN THR PHE THR HIS GLU ILE GLY HIS ALA LEU GLY
SEQRES 16 A 479 LEU ALA HIS PRO GLY GLU TYR ASN ALA GLY GLU GLY ASP
SEQRES 17 A 479 PRO SER TYR ASN ASP ALA VAL TYR ALA GLU ASP SER TYR
SEQRES 18 A 479 GLN PHE SER ILE MET SER PHE TRP GLY GLU ASN GLU THR
SEQRES 19 A 479 GLY ALA ASP TYR ASN GLY HIS TYR GLY GLY ALA PRO MET
SEQRES 20 A 479 ILE ASP ASP ILE ALA ALA ILE GLN ARG LEU TYR GLY ALA
SEQRES 21 A 479 ASN MET THR THR ARG THR GLY ASP SER VAL TYR GLY PHE
SEQRES 22 A 479 ASN SER ASN THR ASP ARG ASP PHE TYR THR ALA THR ASP
SEQRES 23 A 479 SER SER LYS ALA LEU ILE PHE SER VAL TRP ASP ALA GLY
SEQRES 24 A 479 GLY THR ASP THR PHE ASP PHE SER GLY TYR SER ASN ASN
SEQRES 25 A 479 GLN ARG ILE ASN LEU ASN GLU GLY SER PHE SER ASP VAL
SEQRES 26 A 479 GLY GLY LEU LYS GLY ASN VAL SER ILE ALA HIS GLY VAL
SEQRES 27 A 479 THR ILE GLU ASN ALA ILE GLY GLY SER GLY ASN ASP ILE
SEQRES 28 A 479 LEU VAL GLY ASN SER ALA ASP ASN ILE LEU GLN GLY GLY
SEQRES 29 A 479 ALA GLY ASN ASP VAL LEU TYR GLY GLY ALA GLY ALA ASP
SEQRES 30 A 479 THR LEU TYR GLY GLY ALA GLY ARG ASP THR PHE VAL TYR
SEQRES 31 A 479 GLY SER GLY GLN ASP SER THR VAL ALA ALA TYR ASP TRP
SEQRES 32 A 479 ILE ALA ASP PHE GLN LYS GLY ILE ASP LYS ILE ASP LEU
SEQRES 33 A 479 SER ALA PHE ARG ASN GLU GLY GLN LEU SER PHE VAL GLN
SEQRES 34 A 479 ASP GLN PHE THR GLY LYS GLY GLN GLU VAL MET LEU GLN
SEQRES 35 A 479 TRP ASP ALA ALA ASN SER ILE THR ASN LEU TRP LEU HIS
SEQRES 36 A 479 GLU ALA GLY HIS SER SER VAL ASP PHE LEU VAL ARG ILE
SEQRES 37 A 479 VAL GLY GLN ALA ALA GLN SER ASP ILE ILE VAL
HET CA A 480 1
HET CA A 481 1
HET CA A 482 1
HET CA A 483 1
HET CA A 484 1
HET CA A 485 1
HET ZN A 486 1
HET CA A 487 1
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 2 CA 7(CA 2+)
FORMUL 8 ZN ZN 2+
FORMUL 10 HOH *521(H2 O)
HELIX 1 1 SER A 21 LEU A 31 1 11
HELIX 2 2 SER A 49 THR A 58 1 10
HELIX 3 3 ASN A 98 ASP A 114 1 17
HELIX 4 4 GLN A 170 ASN A 175 1 6
HELIX 5 5 GLU A 179 LEU A 194 1 16
HELIX 6 6 SER A 210 ALA A 214 5 5
HELIX 7 7 GLY A 230 GLY A 235 5 6
HELIX 8 8 MET A 247 GLY A 259 1 13
HELIX 9 9 ARG A 279 THR A 283 5 5
HELIX 10 10 SER A 392 SER A 396 5 5
HELIX 11 11 THR A 397 TYR A 401 5 5
HELIX 12 12 SER A 417 GLY A 423 5 7
HELIX 13 13 ALA A 473 SER A 475 5 3
SHEET 1 A 2 THR A 41 VAL A 42 0
SHEET 2 A 2 LYS A 45 THR A 46 -1 O LYS A 45 N VAL A 42
SHEET 1 B 2 VAL A 62 SER A 63 0
SHEET 2 B 2 GLY A 66 THR A 67 -1 O GLY A 66 N SER A 63
SHEET 1 C 5 LEU A 118 GLU A 122 0
SHEET 2 C 5 ALA A 74 PHE A 80 1 N LEU A 76 O THR A 119
SHEET 3 C 5 ILE A 131 TYR A 136 1 O PHE A 133 N LYS A 79
SHEET 4 C 5 SER A 163 ASN A 167 1 O TYR A 166 N TYR A 136
SHEET 5 C 5 ALA A 150 ALA A 152 -1 N TYR A 151 O TRP A 165
SHEET 1 D10 VAL A 270 GLY A 272 0
SHEET 2 D10 THR A 303 ASP A 305 1 O THR A 303 N TYR A 271
SHEET 3 D10 ASN A 342 ILE A 344 1 O ILE A 344 N PHE A 304
SHEET 4 D10 ILE A 360 GLN A 362 1 O GLN A 362 N ALA A 343
SHEET 5 D10 THR A 378 TYR A 380 1 O TYR A 380 N LEU A 361
SHEET 6 D10 ASP A 402 ILE A 404 1 O TRP A 403 N LEU A 379
SHEET 7 D10 PHE A 464 VAL A 469 1 O ARG A 467 N ASP A 402
SHEET 8 D10 ILE A 449 HIS A 455 -1 N LEU A 452 O VAL A 466
SHEET 9 D10 GLU A 438 ASP A 444 -1 N GLN A 442 O ASN A 451
SHEET 10 D10 SER A 426 PHE A 427 1 N SER A 426 O VAL A 439
SHEET 1 E 3 PHE A 293 VAL A 295 0
SHEET 2 E 3 VAL A 332 ILE A 334 1 O SER A 333 N VAL A 295
SHEET 3 E 3 PHE A 322 SER A 323 -1 N SER A 323 O VAL A 332
SHEET 1 F 6 ARG A 314 ASN A 316 0
SHEET 2 F 6 ILE A 351 VAL A 353 1 O VAL A 353 N ILE A 315
SHEET 3 F 6 VAL A 369 TYR A 371 1 O VAL A 369 N LEU A 352
SHEET 4 F 6 THR A 387 VAL A 389 1 O VAL A 389 N LEU A 370
SHEET 5 F 6 LYS A 413 ASP A 415 1 O LYS A 413 N PHE A 388
SHEET 6 F 6 ILE A 477 ILE A 478 1 O ILE A 478 N ILE A 414
LINK NE2 HIS A 188 ZN ZN A 486 1555 1555 2.09
LINK NE2 HIS A 192 ZN ZN A 486 1555 1555 2.14
LINK NE2 HIS A 198 ZN ZN A 486 1555 1555 2.08
LINK O ARG A 265 CA CA A 480 1555 1555 2.43
LINK O GLY A 267 CA CA A 480 1555 1555 2.45
LINK OG SER A 269 CA CA A 480 1555 1555 2.64
LINK OD1 ASP A 297 CA CA A 480 1555 1555 2.56
LINK OD2 ASP A 297 CA CA A 480 1555 1555 2.55
LINK O GLY A 299 CA CA A 480 1555 1555 2.37
LINK O GLY A 300 CA CA A 481 1555 1555 2.42
LINK OD1 ASP A 302 CA CA A 480 1555 1555 3.29
LINK OD2 ASP A 302 CA CA A 480 1555 1555 2.41
LINK OD1 ASP A 302 CA CA A 481 1555 1555 2.49
LINK O THR A 339 CA CA A 481 1555 1555 2.43
LINK OE2 GLU A 341 CA CA A 481 1555 1555 2.62
LINK OE1 GLU A 341 CA CA A 481 1555 1555 2.62
LINK O GLY A 346 CA CA A 482 1555 1555 2.54
LINK O GLY A 348 CA CA A 482 1555 1555 2.51
LINK OD2 ASP A 350 CA CA A 482 1555 1555 2.55
LINK O ASN A 355 CA CA A 483 1555 1555 2.41
LINK O ALA A 357 CA CA A 483 1555 1555 2.48
LINK OD1 ASN A 359 CA CA A 483 1555 1555 2.48
LINK O GLY A 363 CA CA A 482 1555 1555 2.42
LINK O GLY A 364 CA CA A 484 1555 1555 2.48
LINK O ALA A 365 CA CA A 482 1555 1555 2.46
LINK O GLY A 366 CA CA A 484 1555 1555 2.47
LINK OD1 ASP A 368 CA CA A 482 1555 1555 2.54
LINK OD2 ASP A 368 CA CA A 482 1555 1555 2.83
LINK OD2 ASP A 368 CA CA A 484 1555 1555 2.58
LINK O GLY A 372 CA CA A 483 1555 1555 2.49
LINK O GLY A 373 CA CA A 487 1555 1555 2.45
LINK O ALA A 374 CA CA A 483 1555 1555 2.42
LINK O GLY A 375 CA CA A 487 1555 1555 2.48
LINK OD2 ASP A 377 CA CA A 483 1555 1555 2.89
LINK OD1 ASP A 377 CA CA A 483 1555 1555 2.52
LINK OD2 ASP A 377 CA CA A 487 1555 1555 2.46
LINK O GLY A 381 CA CA A 484 1555 1555 2.47
LINK O GLY A 382 CA CA A 485 1555 1555 2.53
LINK O ALA A 383 CA CA A 484 1555 1555 2.54
LINK O GLY A 384 CA CA A 485 1555 1555 2.55
LINK OD1 ASP A 386 CA CA A 484 1555 1555 2.60
LINK OD2 ASP A 386 CA CA A 484 1555 1555 2.78
LINK OD2 ASP A 386 CA CA A 485 1555 1555 2.53
LINK O ASP A 395 CA CA A 487 1555 1555 2.41
LINK OD1 ASP A 402 CA CA A 487 1555 1555 2.52
LINK OE1 GLN A 408 CA CA A 485 1555 1555 2.58
LINK OD1 ASP A 412 CA CA A 485 1555 1555 2.60
LINK OD2 ASP A 412 CA CA A 485 1555 1555 3.33
LINK CA CA A 481 O HOH A 653 1555 1555 2.51
LINK CA CA A 481 O HOH A 797 1555 1555 2.60
LINK CA CA A 485 O HOH A 505 1555 1555 2.62
LINK ZN ZN A 486 O HOH A 798 1555 1555 2.32
LINK CA CA A 487 O HOH A 534 1555 1555 2.57
SITE 1 AC1 6 ARG A 265 GLY A 267 SER A 269 ASP A 297
SITE 2 AC1 6 GLY A 299 ASP A 302
SITE 1 AC2 6 GLY A 300 ASP A 302 THR A 339 GLU A 341
SITE 2 AC2 6 HOH A 653 HOH A 797
SITE 1 AC3 6 GLY A 346 GLY A 348 ASP A 350 GLY A 363
SITE 2 AC3 6 ALA A 365 ASP A 368
SITE 1 AC4 6 ASN A 355 ALA A 357 ASN A 359 GLY A 372
SITE 2 AC4 6 ALA A 374 ASP A 377
SITE 1 AC5 6 GLY A 364 GLY A 366 ASP A 368 GLY A 381
SITE 2 AC5 6 ALA A 383 ASP A 386
SITE 1 AC6 6 GLY A 382 GLY A 384 ASP A 386 GLN A 408
SITE 2 AC6 6 ASP A 412 HOH A 505
SITE 1 AC7 4 HIS A 188 HIS A 192 HIS A 198 HOH A 798
SITE 1 AC8 6 GLY A 373 GLY A 375 ASP A 377 ASP A 395
SITE 2 AC8 6 ASP A 402 HOH A 534
CRYST1 101.967 101.967 122.298 90.00 90.00 120.00 P 31 2 1 6
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 0.009807 0.005662 0.000000 0.00000
SCALE2 0.000000 0.011324 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
