HEADER HYDROLASE 22-APR-12 4AR9
TITLE CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE T FROM
TITLE 2 CLOSTRIDIUM TETANI AT 1.69 ANGSTROM RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLLAGENASE COLT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PEPTIDASE DOMAIN, RESIDUES 340-730;
COMPND 5 SYNONYM: COLLAGENASE T;
COMPND 6 EC: 3.4.24.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM TETANI;
SOURCE 3 ORGANISM_TAXID: 1513;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-15B
KEYWDS HYDROLASE, COLLAGEN, METALLOPROTEASE, PEPTIDASE, COLLAGENOLYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR U.ECKHARD,H.BRANDSTETTER
REVDAT 3 20-DEC-23 4AR9 1 REMARK LINK
REVDAT 2 31-JUL-13 4AR9 1 JRNL
REVDAT 1 05-JUN-13 4AR9 0
JRNL AUTH U.ECKHARD,E.SCHONAUER,H.BRANDSTETTER
JRNL TITL STRUCTURAL BASIS FOR ACTIVITY REGULATION AND SUBSTRATE
JRNL TITL 2 PREFERENCE OF CLOSTRIDIAL COLLAGENASES G, H, AND T.
JRNL REF J.BIOL.CHEM. V. 288 20184 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23703618
JRNL DOI 10.1074/JBC.M112.448548
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 84407
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 + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4451
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5690
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 323
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6325
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 569
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.15000
REMARK 3 B22 (A**2) : -1.52000
REMARK 3 B33 (A**2) : 0.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.168
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.314
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6526 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4421 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8818 ; 1.393 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10686 ; 1.130 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 792 ; 5.127 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 335 ;33.325 ;25.075
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1094 ;13.632 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;22.562 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 920 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7370 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1383 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 10947 ; 2.935 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 196 ;26.888 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 11148 ; 7.004 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 339 A 730
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6431 4.7357 -25.4257
REMARK 3 T TENSOR
REMARK 3 T11: 0.0066 T22: 0.0359
REMARK 3 T33: 0.0310 T12: -0.0043
REMARK 3 T13: -0.0027 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.8105 L22: 1.4931
REMARK 3 L33: 1.1143 L12: 0.2903
REMARK 3 L13: -0.1767 L23: 0.1717
REMARK 3 S TENSOR
REMARK 3 S11: 0.0250 S12: -0.0210 S13: -0.0252
REMARK 3 S21: -0.0663 S22: -0.0282 S23: 0.0088
REMARK 3 S31: 0.0093 S32: 0.0371 S33: 0.0032
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 339 B 730
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4912 12.2537 -25.7698
REMARK 3 T TENSOR
REMARK 3 T11: 0.0365 T22: 0.0368
REMARK 3 T33: 0.0430 T12: -0.0113
REMARK 3 T13: 0.0040 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.9877 L22: 1.2017
REMARK 3 L33: 1.4211 L12: -0.3458
REMARK 3 L13: 0.2951 L23: 0.2744
REMARK 3 S TENSOR
REMARK 3 S11: 0.1161 S12: 0.0574 S13: 0.0494
REMARK 3 S21: -0.0273 S22: -0.0629 S23: -0.1047
REMARK 3 S31: 0.1503 S32: -0.0051 S33: -0.0532
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4AR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1290052163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88975
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 39.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2Y3U
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 100MM NACL, 0.1M MES PH
REMARK 280 6.5
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 38.44500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.37500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.05500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.37500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.44500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.05500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 GLY A 337
REMARK 465 GLY A 338
REMARK 465 GLY B 337
REMARK 465 GLY B 338
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 350 CE NZ
REMARK 470 LYS A 355 CE NZ
REMARK 470 LYS A 363 NZ
REMARK 470 LYS A 371 CE NZ
REMARK 470 LYS A 399 CE NZ
REMARK 470 GLU A 419 CD OE1 OE2
REMARK 470 LYS A 425 CE NZ
REMARK 470 ILE A 456 CD1
REMARK 470 LYS A 528 CG CD CE NZ
REMARK 470 LYS A 540 CD CE NZ
REMARK 470 LYS A 549 CD CE NZ
REMARK 470 LYS A 579 CD CE NZ
REMARK 470 LYS A 590 CD CE NZ
REMARK 470 LYS A 593 NZ
REMARK 470 LYS A 596 CE NZ
REMARK 470 GLU A 599 CD OE1 OE2
REMARK 470 ASN A 607 CG OD1 ND2
REMARK 470 MET A 622 CG SD CE
REMARK 470 LYS A 623 CE NZ
REMARK 470 GLN A 647 CD OE1 NE2
REMARK 470 TYR A 655 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 662 NZ
REMARK 470 LYS A 690 NZ
REMARK 470 LYS B 343 CD CE NZ
REMARK 470 LEU B 344 CD1 CD2
REMARK 470 GLU B 346 CD OE1 OE2
REMARK 470 LYS B 350 CD CE NZ
REMARK 470 LYS B 355 CE NZ
REMARK 470 LYS B 363 NZ
REMARK 470 LYS B 371 CE NZ
REMARK 470 GLU B 373 OE1 OE2
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 LYS B 422 NZ
REMARK 470 LYS B 425 CD CE NZ
REMARK 470 GLN B 453 CG CD OE1 NE2
REMARK 470 ILE B 456 CD1
REMARK 470 LYS B 483 CE NZ
REMARK 470 LYS B 528 CD CE NZ
REMARK 470 LYS B 540 CE NZ
REMARK 470 LYS B 579 CE NZ
REMARK 470 LYS B 590 CD CE NZ
REMARK 470 LYS B 596 CD CE NZ
REMARK 470 LYS B 623 NZ
REMARK 470 GLN B 624 CD OE1 NE2
REMARK 470 ASP B 642 OD1 OD2
REMARK 470 LYS B 644 CE NZ
REMARK 470 GLN B 647 CD OE1 NE2
REMARK 470 TYR B 655 OH
REMARK 470 LYS B 662 NZ
REMARK 470 GLU B 673 CD OE1 OE2
REMARK 470 LYS B 683 CE NZ
REMARK 470 GLU B 686 CD OE1 OE2
REMARK 470 ASN B 715 OD1 ND2
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 OG SER A 389 O HOH A 2037 1.91
REMARK 500 ND2 ASN B 595 O HOH B 2189 1.91
REMARK 500 CD ARG B 516 O HOH B 2092 2.05
REMARK 500 OE1 GLU A 499 O HOH A 2107 2.09
REMARK 500 OG SER B 389 O HOH B 2031 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2168 O HOH B 2207 3654 1.44
REMARK 500 O HOH A 2170 O HOH A 2255 3544 1.45
REMARK 500 O HOH B 2165 O HOH B 2253 3654 2.01
REMARK 500 OD2 ASP B 636 O HOH B 2168 3644 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 465 CG HIS A 465 CD2 0.068
REMARK 500 HIS B 392 CG HIS B 392 CD2 0.054
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 615 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO A 615 C - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG B 516 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 516 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
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 THR A 447 -159.96 -159.09
REMARK 500 THR A 509 -167.48 -121.87
REMARK 500 PRO A 615 44.67 -62.47
REMARK 500 THR B 509 -167.31 -118.87
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 A1732 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 440 OE2
REMARK 620 2 GLY A 473 O 81.4
REMARK 620 3 ILE A 477 O 162.9 93.6
REMARK 620 4 GLY A 479 O 90.2 162.9 98.5
REMARK 620 5 HOH A2055 O 100.1 81.7 95.3 85.2
REMARK 620 6 HOH A2089 O 78.9 106.8 87.0 85.9 171.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1731 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 465 NE2
REMARK 620 2 HIS A 469 NE2 101.6
REMARK 620 3 GLU A 499 OE1 120.7 100.7
REMARK 620 4 HOH A2107 O 67.4 106.5 53.6
REMARK 620 5 HOH A2108 O 96.2 106.8 127.9 145.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1732 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 440 OE2
REMARK 620 2 GLY B 473 O 83.4
REMARK 620 3 ILE B 477 O 164.2 92.6
REMARK 620 4 GLY B 479 O 87.9 161.7 99.8
REMARK 620 5 HOH B2052 O 100.3 80.7 94.0 85.0
REMARK 620 6 HOH B2082 O 78.0 108.5 88.9 85.3 170.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1731 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 465 NE2
REMARK 620 2 HIS B 469 NE2 101.2
REMARK 620 3 GLU B 499 OE1 112.5 102.7
REMARK 620 4 HOH B2093 O 109.0 110.0 119.7
REMARK 620 N 1 2 3
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 1731
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1732
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1731
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1732
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AR8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE T FROM
REMARK 900 CLOSTRIDIUM TETANI COMPLEXED WITH THE PEPTIDIC INHIBITOR ISOAMYL-
REMARK 900 PHOSPHONYL-GLY-PRO-ALA AT 2.05 ANGSTROM RESOLUTION.
REMARK 900 RELATED ID: 4ARE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COLLAGENASE UNIT OF COLLAGENASE G FROM
REMARK 900 CLOSTRIDIUM HISTOLYTICUM AT 2.19 ANGSTROM RESOLUTION.
REMARK 900 RELATED ID: 4ARF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM
REMARK 900 CLOSTRIDIUM HISTOLYTICUM IN COMPLEX WITH THE PEPTIDIC INHIBITOR
REMARK 900 ISOAMYLPHOSPHONYL-GLY-PRO-ALA AT 1. 77 ANGSTROM RESOLUTION.
DBREF 4AR9 A 340 730 UNP Q899Y1 Q899Y1_CLOTE 340 730
DBREF 4AR9 B 340 730 UNP Q899Y1 Q899Y1_CLOTE 340 730
SEQADV 4AR9 GLY A 337 UNP Q899Y1 EXPRESSION TAG
SEQADV 4AR9 GLY A 338 UNP Q899Y1 EXPRESSION TAG
SEQADV 4AR9 THR A 339 UNP Q899Y1 EXPRESSION TAG
SEQADV 4AR9 GLY B 337 UNP Q899Y1 EXPRESSION TAG
SEQADV 4AR9 GLY B 338 UNP Q899Y1 EXPRESSION TAG
SEQADV 4AR9 THR B 339 UNP Q899Y1 EXPRESSION TAG
SEQRES 1 A 394 GLY GLY THR ASP ILE ASN LYS LEU ILE GLU GLU GLY LYS
SEQRES 2 A 394 LYS HIS TYR LEU PRO LYS THR TYR THR PHE ASP ASN GLY
SEQRES 3 A 394 LYS ILE ILE ILE LYS ALA GLY ASP LYS VAL GLU GLU SER
SEQRES 4 A 394 LYS ILE GLN LYS LEU TYR TRP ALA SER LYS GLU VAL LYS
SEQRES 5 A 394 SER GLN PHE HIS ARG ILE ILE GLY ASN ASP LYS PRO LEU
SEQRES 6 A 394 GLU VAL GLY ASN ALA ASP ASP ILE LEU THR ILE VAL ILE
SEQRES 7 A 394 TYR ASN ASN PRO GLU GLU TYR LYS LEU ASN LYS THR LEU
SEQRES 8 A 394 TYR GLY TYR SER VAL ASP ASN GLY GLY ILE TYR ILE GLU
SEQRES 9 A 394 GLY ILE GLY THR PHE PHE THR TYR GLU ARG THR PRO GLN
SEQRES 10 A 394 GLU SER ILE TYR SER LEU GLU GLU LEU PHE ARG HIS GLU
SEQRES 11 A 394 PHE THR HIS TYR LEU GLN GLY ARG TYR LEU ILE PRO GLY
SEQRES 12 A 394 LEU PHE ASN LYS GLY ASP PHE TYR LYS GLY ASN ASN GLY
SEQRES 13 A 394 ARG ILE THR TRP PHE GLU GLU GLY SER ALA GLU PHE PHE
SEQRES 14 A 394 ALA GLY SER THR ARG THR SER VAL LEU PRO ARG LYS SER
SEQRES 15 A 394 MET VAL GLY GLY LEU SER LYS ASN PRO LYS GLU ARG PHE
SEQRES 16 A 394 ASN ALA ASP LYS LEU LEU HIS SER LYS TYR SER ASP GLY
SEQRES 17 A 394 TRP ASP PHE TYR LYS TYR GLY TYR ALA PHE SER ASP TYR
SEQRES 18 A 394 MET TYR ASN ASN ASN LYS LYS LEU PHE SER ASP LEU VAL
SEQRES 19 A 394 SER THR MET LYS ASN ASN ASP VAL LYS GLY TYR GLU ALA
SEQRES 20 A 394 LEU ILE GLU GLU SER SER LYS ASP SER LYS ILE ASN LYS
SEQRES 21 A 394 ASP TYR GLU TYR HIS MET GLU ASN LEU VAL ASN ASN TYR
SEQRES 22 A 394 ASP ASN TYR THR ILE PRO LEU VAL SER ASP ASP TYR MET
SEQRES 23 A 394 LYS GLN TYR ASP ASN LYS SER LEU HIS GLU ILE LYS SER
SEQRES 24 A 394 ASP ILE GLU LYS ALA MET ASP VAL LYS ASN SER GLN ILE
SEQRES 25 A 394 THR LYS GLU SER SER GLN TYR PHE ASP THR TYR ASN LEU
SEQRES 26 A 394 LYS ALA THR TYR THR LEU SER SER ASN LYS GLY GLU ILE
SEQRES 27 A 394 SER ASN TRP ASN TYR MET ASN ASN LYS ILE ASN GLU ALA
SEQRES 28 A 394 LEU ASN LYS LEU ASP ASN LEU SER TRP GLY GLY TYR LYS
SEQRES 29 A 394 THR VAL THR ALA TYR PHE SER ASN PRO ARG LEU ASN SER
SEQRES 30 A 394 ASN ASN GLU VAL VAL TYR ASP ILE VAL PHE HIS GLY LEU
SEQRES 31 A 394 LEU SER HIS ASN
SEQRES 1 B 394 GLY GLY THR ASP ILE ASN LYS LEU ILE GLU GLU GLY LYS
SEQRES 2 B 394 LYS HIS TYR LEU PRO LYS THR TYR THR PHE ASP ASN GLY
SEQRES 3 B 394 LYS ILE ILE ILE LYS ALA GLY ASP LYS VAL GLU GLU SER
SEQRES 4 B 394 LYS ILE GLN LYS LEU TYR TRP ALA SER LYS GLU VAL LYS
SEQRES 5 B 394 SER GLN PHE HIS ARG ILE ILE GLY ASN ASP LYS PRO LEU
SEQRES 6 B 394 GLU VAL GLY ASN ALA ASP ASP ILE LEU THR ILE VAL ILE
SEQRES 7 B 394 TYR ASN ASN PRO GLU GLU TYR LYS LEU ASN LYS THR LEU
SEQRES 8 B 394 TYR GLY TYR SER VAL ASP ASN GLY GLY ILE TYR ILE GLU
SEQRES 9 B 394 GLY ILE GLY THR PHE PHE THR TYR GLU ARG THR PRO GLN
SEQRES 10 B 394 GLU SER ILE TYR SER LEU GLU GLU LEU PHE ARG HIS GLU
SEQRES 11 B 394 PHE THR HIS TYR LEU GLN GLY ARG TYR LEU ILE PRO GLY
SEQRES 12 B 394 LEU PHE ASN LYS GLY ASP PHE TYR LYS GLY ASN ASN GLY
SEQRES 13 B 394 ARG ILE THR TRP PHE GLU GLU GLY SER ALA GLU PHE PHE
SEQRES 14 B 394 ALA GLY SER THR ARG THR SER VAL LEU PRO ARG LYS SER
SEQRES 15 B 394 MET VAL GLY GLY LEU SER LYS ASN PRO LYS GLU ARG PHE
SEQRES 16 B 394 ASN ALA ASP LYS LEU LEU HIS SER LYS TYR SER ASP GLY
SEQRES 17 B 394 TRP ASP PHE TYR LYS TYR GLY TYR ALA PHE SER ASP TYR
SEQRES 18 B 394 MET TYR ASN ASN ASN LYS LYS LEU PHE SER ASP LEU VAL
SEQRES 19 B 394 SER THR MET LYS ASN ASN ASP VAL LYS GLY TYR GLU ALA
SEQRES 20 B 394 LEU ILE GLU GLU SER SER LYS ASP SER LYS ILE ASN LYS
SEQRES 21 B 394 ASP TYR GLU TYR HIS MET GLU ASN LEU VAL ASN ASN TYR
SEQRES 22 B 394 ASP ASN TYR THR ILE PRO LEU VAL SER ASP ASP TYR MET
SEQRES 23 B 394 LYS GLN TYR ASP ASN LYS SER LEU HIS GLU ILE LYS SER
SEQRES 24 B 394 ASP ILE GLU LYS ALA MET ASP VAL LYS ASN SER GLN ILE
SEQRES 25 B 394 THR LYS GLU SER SER GLN TYR PHE ASP THR TYR ASN LEU
SEQRES 26 B 394 LYS ALA THR TYR THR LEU SER SER ASN LYS GLY GLU ILE
SEQRES 27 B 394 SER ASN TRP ASN TYR MET ASN ASN LYS ILE ASN GLU ALA
SEQRES 28 B 394 LEU ASN LYS LEU ASP ASN LEU SER TRP GLY GLY TYR LYS
SEQRES 29 B 394 THR VAL THR ALA TYR PHE SER ASN PRO ARG LEU ASN SER
SEQRES 30 B 394 ASN ASN GLU VAL VAL TYR ASP ILE VAL PHE HIS GLY LEU
SEQRES 31 B 394 LEU SER HIS ASN
HET ZN A1731 1
HET CA A1732 1
HET ZN B1731 1
HET CA B1732 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 7 HOH *569(H2 O)
HELIX 1 1 ASP A 340 LEU A 353 1 14
HELIX 2 2 GLU A 373 GLY A 396 1 24
HELIX 3 3 ASN A 405 ILE A 409 5 5
HELIX 4 4 ASN A 417 LYS A 422 1 6
HELIX 5 5 LEU A 423 TYR A 428 1 6
HELIX 6 6 GLU A 440 ILE A 442 5 3
HELIX 7 7 SER A 458 LEU A 476 1 19
HELIX 8 8 GLY A 484 LYS A 488 5 5
HELIX 9 9 ILE A 494 ALA A 506 1 13
HELIX 10 10 ARG A 516 GLY A 521 1 6
HELIX 11 11 ASN A 526 ARG A 530 5 5
HELIX 12 12 ASN A 532 HIS A 538 1 7
HELIX 13 13 LYS A 540 GLY A 544 5 5
HELIX 14 14 ASP A 546 ASN A 562 1 17
HELIX 15 15 ASN A 562 ASN A 575 1 14
HELIX 16 16 ASP A 577 LYS A 590 1 14
HELIX 17 17 ASP A 591 ASN A 608 1 18
HELIX 18 18 TYR A 609 TYR A 612 5 4
HELIX 19 19 SER A 618 LYS A 623 5 6
HELIX 20 20 SER A 629 ASP A 642 1 14
HELIX 21 21 GLY A 672 ASN A 693 1 22
HELIX 22 22 TRP A 696 VAL A 702 5 7
HELIX 23 23 ASP B 340 LEU B 353 1 14
HELIX 24 24 GLU B 373 GLY B 396 1 24
HELIX 25 25 ASN B 405 ILE B 409 5 5
HELIX 26 26 ASN B 417 LYS B 422 1 6
HELIX 27 27 LEU B 423 TYR B 428 1 6
HELIX 28 28 GLU B 440 ILE B 442 5 3
HELIX 29 29 SER B 458 LEU B 476 1 19
HELIX 30 30 GLY B 484 LYS B 488 5 5
HELIX 31 31 ILE B 494 ALA B 506 1 13
HELIX 32 32 ARG B 516 GLY B 521 1 6
HELIX 33 33 ASN B 526 ARG B 530 5 5
HELIX 34 34 ASN B 532 HIS B 538 1 7
HELIX 35 35 LYS B 540 GLY B 544 5 5
HELIX 36 36 TRP B 545 ASN B 562 1 18
HELIX 37 37 ASN B 562 ASN B 575 1 14
HELIX 38 38 ASP B 577 LYS B 590 1 14
HELIX 39 39 ASP B 591 ASN B 608 1 18
HELIX 40 40 TYR B 609 TYR B 612 5 4
HELIX 41 41 SER B 618 MET B 622 5 5
HELIX 42 42 SER B 629 ASP B 642 1 14
HELIX 43 43 GLY B 672 ASN B 693 1 22
HELIX 44 44 TRP B 696 VAL B 702 5 7
SHEET 1 AA 5 LYS A 355 PHE A 359 0
SHEET 2 AA 5 ILE A 364 ALA A 368 -1 O ILE A 364 N PHE A 359
SHEET 3 AA 5 LEU A 410 TYR A 415 1 O LEU A 410 N ILE A 365
SHEET 4 AA 5 THR A 444 TYR A 448 1 O PHE A 445 N VAL A 413
SHEET 5 AA 5 GLY A 436 ILE A 439 -1 O ILE A 437 N PHE A 446
SHEET 1 AB 4 GLN A 647 SER A 652 0
SHEET 2 AB 4 PHE A 656 THR A 666 -1 O THR A 658 N GLU A 651
SHEET 3 AB 4 VAL A 717 HIS A 729 -1 O TYR A 719 N TYR A 665
SHEET 4 AB 4 THR A 703 LEU A 711 -1 O THR A 703 N HIS A 724
SHEET 1 BA 5 LYS B 355 PHE B 359 0
SHEET 2 BA 5 ILE B 364 ALA B 368 -1 O ILE B 364 N PHE B 359
SHEET 3 BA 5 LEU B 410 TYR B 415 1 O LEU B 410 N ILE B 365
SHEET 4 BA 5 THR B 444 TYR B 448 1 O PHE B 445 N VAL B 413
SHEET 5 BA 5 GLY B 436 ILE B 439 -1 O ILE B 437 N PHE B 446
SHEET 1 BB 4 GLN B 647 SER B 652 0
SHEET 2 BB 4 PHE B 656 THR B 666 -1 O THR B 658 N GLU B 651
SHEET 3 BB 4 VAL B 717 HIS B 729 -1 O TYR B 719 N TYR B 665
SHEET 4 BB 4 THR B 703 LEU B 711 -1 O THR B 703 N HIS B 724
LINK OE2 GLU A 440 CA CA A1732 1555 1555 2.32
LINK NE2 HIS A 465 ZN ZN A1731 1555 1555 2.04
LINK NE2 HIS A 469 ZN ZN A1731 1555 1555 2.03
LINK O GLY A 473 CA CA A1732 1555 1555 2.35
LINK O ILE A 477 CA CA A1732 1555 1555 2.35
LINK O GLY A 479 CA CA A1732 1555 1555 2.35
LINK OE1 GLU A 499 ZN ZN A1731 1555 1555 2.00
LINK ZN ZN A1731 O HOH A2107 1555 1555 2.52
LINK ZN ZN A1731 O HOH A2108 1555 1555 2.03
LINK CA CA A1732 O HOH A2055 1555 1555 2.36
LINK CA CA A1732 O HOH A2089 1555 1555 2.40
LINK OE2 GLU B 440 CA CA B1732 1555 1555 2.31
LINK NE2 HIS B 465 ZN ZN B1731 1555 1555 2.04
LINK NE2 HIS B 469 ZN ZN B1731 1555 1555 2.03
LINK O GLY B 473 CA CA B1732 1555 1555 2.35
LINK O ILE B 477 CA CA B1732 1555 1555 2.34
LINK O GLY B 479 CA CA B1732 1555 1555 2.35
LINK OE1 GLU B 499 ZN ZN B1731 1555 1555 1.99
LINK ZN ZN B1731 O HOH B2093 1555 1555 2.02
LINK CA CA B1732 O HOH B2052 1555 1555 2.40
LINK CA CA B1732 O HOH B2082 1555 1555 2.39
SITE 1 AC1 6 HIS A 465 GLU A 466 HIS A 469 GLU A 499
SITE 2 AC1 6 HOH A2107 HOH A2108
SITE 1 AC2 6 GLU A 440 GLY A 473 ILE A 477 GLY A 479
SITE 2 AC2 6 HOH A2055 HOH A2089
SITE 1 AC3 4 HIS B 465 HIS B 469 GLU B 499 HOH B2093
SITE 1 AC4 6 GLU B 440 GLY B 473 ILE B 477 GLY B 479
SITE 2 AC4 6 HOH B2052 HOH B2082
CRYST1 76.890 102.110 104.750 90.00 90.00 90.00 P 21 21 21 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 0.013006 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009793 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009547 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
