HEADER HYDROLASE (SERINE PROTEASE) 04-JUL-94 1SAT
TITLE CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERRATIA PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SERRALYSIN, MAJOR METALLO PROTEASE FROM SERRATIA MARCESCENS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA MARCESCENS;
SOURCE 3 ORGANISM_TAXID: 615
KEYWDS PARALLEL BETA HELIX, PARALLEL BETA ROLL, HYDROLASE (SERINE PROTEASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR U.BAUMANN
REVDAT 4 14-FEB-24 1SAT 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1SAT 1 VERSN
REVDAT 2 01-APR-03 1SAT 1 JRNL
REVDAT 1 31-JUL-95 1SAT 0
JRNL AUTH U.BAUMANN
JRNL TITL CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM
JRNL TITL 2 SERRATIA MARCESCENS.
JRNL REF J.MOL.BIOL. V. 242 244 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8089845
JRNL DOI 10.1006/JMBI.1994.1576
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH U.BAUMANN,S.WU,K.M.FLAHERTY,D.B.MCKAY
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE FROM
REMARK 1 TITL 2 PS. AERUGINOSA: A TWO-DOMAIN PROTEIN WITH A CALCIUM BINDING
REMARK 1 TITL 3 PARALLEL BETA ROLL MOTIF
REMARK 1 REF EMBO J. V. 12 3357 1993
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 60167
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3539
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.44
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.450
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.46
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.180
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) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.200 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.400 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.700 ; 2.500
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81141
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 75.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 21.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 75.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.60000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 ALA A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
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 GLN A 111 CG CD OE1 NE2
REMARK 470 LYS A 112 CG CD CE NZ
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 PRO A 187 0.01 -66.04
REMARK 500 TYR A 190 128.41 -172.99
REMARK 500 ASP A 225 105.10 -160.73
REMARK 500 ASN A 343 -166.44 -126.34
REMARK 500 SER A 379 10.61 -140.40
REMARK 500 ALA A 388 46.95 -154.22
REMARK 500 ASP A 394 40.79 -152.17
REMARK 500 ILE A 399 -57.12 -120.52
REMARK 500 PHE A 416 -70.32 -62.18
REMARK 500 SER A 424 5.13 -150.96
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 472 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 176 NE2
REMARK 620 2 HIS A 180 NE2 101.6
REMARK 620 3 HIS A 186 NE2 114.7 102.4
REMARK 620 4 TYR A 216 OH 76.1 167.9 89.2
REMARK 620 5 HOH A 510 O 107.4 98.5 127.3 71.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 473 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 253 O
REMARK 620 2 GLY A 255 O 94.8
REMARK 620 3 THR A 257 OG1 91.4 80.7
REMARK 620 4 ASP A 285 OD2 89.6 156.6 76.3
REMARK 620 5 ASP A 285 OD1 80.4 152.6 126.2 50.8
REMARK 620 6 GLY A 287 O 84.8 81.6 161.5 121.7 71.1
REMARK 620 7 ASP A 290 OD1 172.5 89.7 83.4 84.0 98.4 101.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 474 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 288 O
REMARK 620 2 ASP A 290 OD2 81.9
REMARK 620 3 THR A 327 O 163.9 95.8
REMARK 620 4 GLU A 329 OE1 82.7 84.1 81.2
REMARK 620 5 GLU A 329 OE2 87.7 133.4 82.4 49.5
REMARK 620 6 HOH A 541 O 110.7 74.4 83.7 152.2 150.0
REMARK 620 7 HOH A 543 O 90.2 147.3 99.9 126.4 77.3 79.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 475 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 334 O
REMARK 620 2 GLY A 336 O 97.5
REMARK 620 3 ASP A 338 OD2 86.5 85.9
REMARK 620 4 GLY A 351 O 88.2 173.3 91.0
REMARK 620 5 ALA A 353 O 84.1 86.0 166.6 98.1
REMARK 620 6 ASP A 356 OD1 168.3 78.9 82.2 94.9 106.6
REMARK 620 7 ASP A 356 OD2 144.4 111.6 114.7 64.4 78.2 45.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 476 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 343 O
REMARK 620 2 ALA A 345 O 89.3
REMARK 620 3 ASN A 347 OD1 85.0 83.1
REMARK 620 4 GLY A 360 O 85.2 170.1 88.3
REMARK 620 5 GLY A 362 O 91.6 86.9 169.5 101.4
REMARK 620 6 ASP A 365 OD2 145.6 121.1 112.2 66.7 75.9
REMARK 620 7 ASP A 365 OD1 167.1 82.3 84.3 101.6 97.7 46.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 477 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 352 O
REMARK 620 2 GLY A 354 O 108.3
REMARK 620 3 ASP A 356 OD2 80.5 80.0
REMARK 620 4 GLY A 369 O 79.1 170.7 96.1
REMARK 620 5 ALA A 371 O 87.5 80.5 152.6 105.9
REMARK 620 6 ASP A 374 OD1 153.9 82.0 77.7 88.9 118.3
REMARK 620 7 ASP A 374 OD2 140.5 107.5 121.9 67.4 82.5 48.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 479 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 361 O
REMARK 620 2 GLY A 362 O 62.2
REMARK 620 3 GLY A 363 O 122.5 67.0
REMARK 620 4 ASP A 365 OD2 84.8 67.3 99.3
REMARK 620 5 ASP A 383 O 94.1 128.2 96.9 161.4
REMARK 620 6 ASP A 390 OD1 152.0 137.6 85.3 87.6 84.7
REMARK 620 7 HOH A 561 O 65.2 117.5 171.5 76.9 85.8 86.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 478 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 370 O
REMARK 620 2 GLY A 372 O 111.1
REMARK 620 3 ASP A 374 OD2 81.4 84.0
REMARK 620 4 ASP A 400 OD1 164.3 82.3 92.4
REMARK 620 5 ASP A 400 OD2 132.2 111.5 123.5 41.9
REMARK 620 6 HOH A 566 O 87.5 159.6 91.1 78.2 55.5
REMARK 620 7 HOH A 629 O 98.0 90.8 174.2 89.6 61.0 94.7
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 ZN A 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 479
DBREF 1SAT A 1 471 UNP P23694 PRZN_SERMA 17 487
SEQADV 1SAT ASP A 196 UNP P23694 ASN 212 CONFLICT
SEQADV 1SAT ALA A 200 UNP P23694 ASN 216 CONFLICT
SEQADV 1SAT LEU A 250 UNP P23694 PRO 266 CONFLICT
SEQADV 1SAT ASP A 408 UNP P23694 ASN 424 CONFLICT
SEQADV 1SAT SER A 415 UNP P23694 ASP 431 CONFLICT
SEQADV 1SAT ALA A 451 UNP P23694 GLN 467 CONFLICT
SEQRES 1 A 471 ALA ALA THR THR GLY TYR ASP ALA VAL ASP ASP LEU LEU
SEQRES 2 A 471 HIS TYR HIS GLU ARG GLY ASN GLY ILE GLN ILE ASN GLY
SEQRES 3 A 471 LYS ASP SER PHE SER ASN GLU GLN ALA GLY LEU PHE ILE
SEQRES 4 A 471 THR ARG GLU ASN GLN THR TRP ASN GLY TYR LYS VAL PHE
SEQRES 5 A 471 GLY GLN PRO VAL LYS LEU THR PHE SER PHE PRO ASP TYR
SEQRES 6 A 471 LYS PHE SER SER THR ASN VAL ALA GLY ASP THR GLY LEU
SEQRES 7 A 471 SER LYS PHE SER ALA GLU GLN GLN GLN GLN ALA LYS LEU
SEQRES 8 A 471 SER LEU GLN SER TRP ALA ASP VAL ALA ASN ILE THR PHE
SEQRES 9 A 471 THR GLU VAL ALA ALA GLY GLN LYS ALA ASN ILE THR PHE
SEQRES 10 A 471 GLY ASN TYR SER GLN ASP ARG PRO GLY HIS TYR ASP TYR
SEQRES 11 A 471 GLY THR GLN ALA TYR ALA PHE LEU PRO ASN THR ILE TRP
SEQRES 12 A 471 GLN GLY GLN ASP LEU GLY GLY GLN THR TRP TYR ASN VAL
SEQRES 13 A 471 ASN GLN SER ASN VAL LYS HIS PRO ALA THR GLU ASP TYR
SEQRES 14 A 471 GLY ARG GLN THR PHE THR HIS GLU ILE GLY HIS ALA LEU
SEQRES 15 A 471 GLY LEU SER HIS PRO GLY ASP TYR ASN ALA GLY GLU GLY
SEQRES 16 A 471 ASP PRO THR TYR ALA ASP VAL THR TYR ALA GLU ASP THR
SEQRES 17 A 471 ARG GLN PHE SER LEU MET SER TYR TRP SER GLU THR ASN
SEQRES 18 A 471 THR GLY GLY ASP ASN GLY GLY HIS TYR ALA ALA ALA PRO
SEQRES 19 A 471 LEU LEU ASP ASP ILE ALA ALA ILE GLN HIS LEU TYR GLY
SEQRES 20 A 471 ALA ASN LEU SER THR ARG THR GLY ASP THR VAL TYR GLY
SEQRES 21 A 471 PHE ASN SER ASN THR GLY ARG ASP PHE LEU SER THR THR
SEQRES 22 A 471 SER ASN SER GLN LYS VAL ILE PHE ALA ALA TRP ASP ALA
SEQRES 23 A 471 GLY GLY ASN ASP THR PHE ASP PHE SER GLY TYR THR ALA
SEQRES 24 A 471 ASN GLN ARG ILE ASN LEU ASN GLU LYS SER PHE SER ASP
SEQRES 25 A 471 VAL GLY GLY LEU LYS GLY ASN VAL SER ILE ALA ALA GLY
SEQRES 26 A 471 VAL THR ILE GLU ASN ALA ILE GLY GLY SER GLY ASN ASP
SEQRES 27 A 471 VAL ILE VAL GLY ASN ALA ALA ASN ASN VAL LEU LYS GLY
SEQRES 28 A 471 GLY ALA GLY ASN ASP VAL LEU PHE GLY GLY GLY GLY ALA
SEQRES 29 A 471 ASP GLU LEU TRP GLY GLY ALA GLY LYS ASP ILE PHE VAL
SEQRES 30 A 471 PHE SER ALA ALA SER ASP SER ALA PRO GLY ALA SER ASP
SEQRES 31 A 471 TRP ILE ARG ASP PHE GLN LYS GLY ILE ASP LYS ILE ASP
SEQRES 32 A 471 LEU SER PHE PHE ASP LYS GLU ALA ASN SER SER SER PHE
SEQRES 33 A 471 ILE HIS PHE VAL ASP HIS PHE SER GLY THR ALA GLY GLU
SEQRES 34 A 471 ALA LEU LEU SER TYR ASN ALA SER SER ASN VAL THR ASP
SEQRES 35 A 471 LEU SER VAL ASN ILE GLY GLY HIS ALA ALA PRO ASP PHE
SEQRES 36 A 471 LEU VAL LYS ILE VAL GLY GLN VAL ASP VAL ALA THR ASP
SEQRES 37 A 471 PHE ILE VAL
HET ZN A 472 1
HET CA A 473 1
HET CA A 474 1
HET CA A 475 1
HET CA A 476 1
HET CA A 477 1
HET CA A 478 1
HET CA A 479 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CA 7(CA 2+)
FORMUL 10 HOH *194(H2 O)
HELIX 1 1 GLY A 5 LEU A 13 1 9
HELIX 2 2 ASN A 32 ILE A 39 1 8
HELIX 3 3 ALA A 83 VAL A 99 1 17
HELIX 4 4 SER A 159 LYS A 162 1 4
HELIX 5 5 ASP A 168 LEU A 182 1 15
HELIX 6 6 TYR A 199 ASP A 201 5 3
HELIX 7 7 GLU A 219 THR A 222 5 4
HELIX 8 8 LEU A 236 TYR A 246 1 11
HELIX 9 9 ASP A 268 LEU A 270 5 3
HELIX 10 10 ALA A 381 SER A 384 5 4
HELIX 11 11 SER A 405 ALA A 411 1 7
SHEET 1 A 2 VAL A 56 PHE A 60 0
SHEET 2 A 2 ILE A 102 GLU A 106 1 N THR A 103 O VAL A 56
SHEET 1 B 3 THR A 116 TYR A 120 0
SHEET 2 B 3 GLN A 151 ASN A 155 1 N THR A 152 O THR A 116
SHEET 3 B 3 ALA A 134 ALA A 136 -1 N TYR A 135 O TRP A 153
SHEET 1 C 3 VAL A 258 GLY A 260 0
SHEET 2 C 3 THR A 291 ASP A 293 1 N THR A 291 O TYR A 259
SHEET 3 C 3 ASN A 330 ILE A 332 1 N ASN A 330 O PHE A 292
SHEET 1 D 2 PHE A 281 ALA A 283 0
SHEET 2 D 2 VAL A 320 ILE A 322 1 N SER A 321 O PHE A 281
SHEET 1 E 5 ARG A 302 ASN A 304 0
SHEET 2 E 5 VAL A 339 VAL A 341 1 N VAL A 339 O ILE A 303
SHEET 3 E 5 VAL A 357 PHE A 359 1 N VAL A 357 O ILE A 340
SHEET 4 E 5 ILE A 375 VAL A 377 1 N ILE A 375 O LEU A 358
SHEET 5 E 5 LYS A 401 ASP A 403 1 N LYS A 401 O PHE A 376
SHEET 1 F 2 VAL A 348 LYS A 350 0
SHEET 2 F 2 GLU A 366 TRP A 368 1 N GLU A 366 O LEU A 349
SHEET 1 G 4 ASP A 390 ILE A 392 0
SHEET 2 G 4 PHE A 455 VAL A 460 1 N LYS A 458 O ASP A 390
SHEET 3 G 4 VAL A 440 VAL A 445 -1 N VAL A 445 O PHE A 455
SHEET 4 G 4 ALA A 430 ASN A 435 -1 N ASN A 435 O VAL A 440
LINK NE2 HIS A 176 ZN ZN A 472 1555 1555 2.08
LINK NE2 HIS A 180 ZN ZN A 472 1555 1555 2.13
LINK NE2 HIS A 186 ZN ZN A 472 1555 1555 1.99
LINK OH TYR A 216 ZN ZN A 472 1555 1555 2.77
LINK O ARG A 253 CA CA A 473 1555 1555 2.30
LINK O GLY A 255 CA CA A 473 1555 1555 2.36
LINK OG1 THR A 257 CA CA A 473 1555 1555 2.44
LINK OD2 ASP A 285 CA CA A 473 1555 1555 2.57
LINK OD1 ASP A 285 CA CA A 473 1555 1555 2.55
LINK O GLY A 287 CA CA A 473 1555 1555 2.31
LINK O GLY A 288 CA CA A 474 1555 1555 2.38
LINK OD1 ASP A 290 CA CA A 473 1555 1555 2.41
LINK OD2 ASP A 290 CA CA A 474 1555 1555 2.44
LINK O THR A 327 CA CA A 474 1555 1555 2.36
LINK OE1 GLU A 329 CA CA A 474 1555 1555 2.62
LINK OE2 GLU A 329 CA CA A 474 1555 1555 2.58
LINK O GLY A 334 CA CA A 475 1555 1555 2.33
LINK O GLY A 336 CA CA A 475 1555 1555 2.38
LINK OD2 ASP A 338 CA CA A 475 1555 1555 2.50
LINK O ASN A 343 CA CA A 476 1555 1555 2.31
LINK O ALA A 345 CA CA A 476 1555 1555 2.37
LINK OD1 ASN A 347 CA CA A 476 1555 1555 2.39
LINK O GLY A 351 CA CA A 475 1555 1555 2.32
LINK O GLY A 352 CA CA A 477 1555 1555 2.32
LINK O ALA A 353 CA CA A 475 1555 1555 2.38
LINK O GLY A 354 CA CA A 477 1555 1555 2.43
LINK OD1 ASP A 356 CA CA A 475 1555 1555 2.47
LINK OD2 ASP A 356 CA CA A 475 1555 1555 3.01
LINK OD2 ASP A 356 CA CA A 477 1555 1555 2.46
LINK O GLY A 360 CA CA A 476 1555 1555 2.40
LINK O GLY A 361 CA CA A 479 1555 1555 2.40
LINK O GLY A 362 CA CA A 476 1555 1555 2.33
LINK O GLY A 362 CA CA A 479 1555 1555 3.30
LINK O GLY A 363 CA CA A 479 1555 1555 2.35
LINK OD2 ASP A 365 CA CA A 476 1555 1555 2.90
LINK OD1 ASP A 365 CA CA A 476 1555 1555 2.49
LINK OD2 ASP A 365 CA CA A 479 1555 1555 2.40
LINK O GLY A 369 CA CA A 477 1555 1555 2.40
LINK O GLY A 370 CA CA A 478 1555 1555 2.47
LINK O ALA A 371 CA CA A 477 1555 1555 2.27
LINK O GLY A 372 CA CA A 478 1555 1555 2.46
LINK OD1 ASP A 374 CA CA A 477 1555 1555 2.48
LINK OD2 ASP A 374 CA CA A 477 1555 1555 2.77
LINK OD2 ASP A 374 CA CA A 478 1555 1555 2.44
LINK O ASP A 383 CA CA A 479 1555 1555 2.21
LINK OD1 ASP A 390 CA CA A 479 1555 1555 2.54
LINK OD1 ASP A 400 CA CA A 478 1555 1555 2.55
LINK OD2 ASP A 400 CA CA A 478 1555 1555 3.31
LINK ZN ZN A 472 O HOH A 510 1555 1555 1.84
LINK CA CA A 474 O HOH A 541 1555 1555 2.38
LINK CA CA A 474 O HOH A 543 1555 1555 2.45
LINK CA CA A 478 O HOH A 566 1555 1555 2.66
LINK CA CA A 478 O HOH A 629 1555 1555 2.29
LINK CA CA A 479 O HOH A 561 1555 1555 2.81
SITE 1 AC1 5 HIS A 176 HIS A 180 HIS A 186 TYR A 216
SITE 2 AC1 5 HOH A 510
SITE 1 AC2 6 ARG A 253 GLY A 255 THR A 257 ASP A 285
SITE 2 AC2 6 GLY A 287 ASP A 290
SITE 1 AC3 6 GLY A 288 ASP A 290 THR A 327 GLU A 329
SITE 2 AC3 6 HOH A 541 HOH A 543
SITE 1 AC4 6 GLY A 334 GLY A 336 ASP A 338 GLY A 351
SITE 2 AC4 6 ALA A 353 ASP A 356
SITE 1 AC5 6 ASN A 343 ALA A 345 ASN A 347 GLY A 360
SITE 2 AC5 6 GLY A 362 ASP A 365
SITE 1 AC6 6 GLY A 352 GLY A 354 ASP A 356 GLY A 369
SITE 2 AC6 6 ALA A 371 ASP A 374
SITE 1 AC7 6 GLY A 370 GLY A 372 ASP A 374 ASP A 400
SITE 2 AC7 6 HOH A 566 HOH A 629
SITE 1 AC8 7 GLY A 361 GLY A 362 GLY A 363 ASP A 365
SITE 2 AC8 7 ASP A 383 ASP A 390 HOH A 561
CRYST1 151.000 109.200 42.600 90.00 90.00 90.00 P 21 21 21 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 0.006623 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023474 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
