HEADER HYDROLASE 01-NOV-09 3KI9
TITLE CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE
TITLE 2 (SAPEP/DAPE) IN THE MN2+ BOUND FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIPEPTIDASE SACOL1801;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: METALLOPEPTIDASE, DAPE;
COMPND 5 EC: 3.4.13.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 93062;
SOURCE 4 STRAIN: COL;
SOURCE 5 GENE: DIPEPTIDASE PEPV(SACOL1801);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS MN+2 BOUND FORM-DIPEPTIDASE (DAPE), METALLOPEPTIDASE, SAPEP, M20
KEYWDS 2 PEPTIDASE, DIPEPTIDASE, HYDROLASE, METAL-BINDING, METALLOPROTEASE,
KEYWDS 3 PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.GIRISH,B.GOPAL
REVDAT 3 01-NOV-23 3KI9 1 REMARK SEQADV LINK
REVDAT 2 28-SEP-11 3KI9 1 JRNL VERSN
REVDAT 1 07-JUL-10 3KI9 0
JRNL AUTH T.S.GIRISH,B.GOPAL
JRNL TITL CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE
JRNL TITL 2 (SAPEP) REVEALS LARGE DOMAIN MOTIONS BETWEEN THE
JRNL TITL 3 MANGANESE-BOUND AND APO-STATES
JRNL REF J.BIOL.CHEM. V. 285 29406 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20610394
JRNL DOI 10.1074/JBC.M110.147579
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13998
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 745
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3662
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 26
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.56
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.398
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.040
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3735 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5064 ; 0.937 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 464 ; 4.845 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 190 ;39.888 ;25.316
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 603 ;15.345 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;20.690 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 547 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2902 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2311 ; 0.304 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3707 ; 0.577 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1424 ; 0.695 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1357 ; 1.232 ; 4.500
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 3
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 4 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9904 -29.5587 5.0527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0527 T22: 0.0144
REMARK 3 T33: 0.0179 T12: -0.0088
REMARK 3 T13: 0.0266 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.9700 L22: 1.1052
REMARK 3 L33: 0.6626 L12: 0.0010
REMARK 3 L13: -0.2067 L23: -0.1197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0872 S12: 0.0660 S13: 0.0835
REMARK 3 S21: 0.0618 S22: -0.0837 S23: 0.0483
REMARK 3 S31: -0.0637 S32: -0.0210 S33: -0.0035
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 : A 184 A 383
REMARK 3 ORIGIN FOR THE GROUP (A): 57.6076 -61.0212 18.0286
REMARK 3 T TENSOR
REMARK 3 T11: 0.0187 T22: 0.0320
REMARK 3 T33: 0.0259 T12: -0.0199
REMARK 3 T13: -0.0096 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 0.8130 L22: 1.7722
REMARK 3 L33: 1.0627 L12: -0.3473
REMARK 3 L13: -0.1268 L23: 0.2276
REMARK 3 S TENSOR
REMARK 3 S11: 0.0334 S12: -0.1002 S13: -0.0834
REMARK 3 S21: 0.0864 S22: -0.0556 S23: -0.1233
REMARK 3 S31: 0.0040 S32: 0.0794 S33: 0.0222
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 385 A 464
REMARK 3 ORIGIN FOR THE GROUP (A): 38.9555 -33.0048 12.7438
REMARK 3 T TENSOR
REMARK 3 T11: 0.0252 T22: 0.0290
REMARK 3 T33: 0.0541 T12: -0.0137
REMARK 3 T13: 0.0332 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.8729 L22: 1.3261
REMARK 3 L33: 1.3201 L12: -0.8301
REMARK 3 L13: -0.3076 L23: -0.2748
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: -0.0565 S13: -0.0097
REMARK 3 S21: 0.0544 S22: 0.0549 S23: 0.1598
REMARK 3 S31: -0.0504 S32: -0.1069 S33: -0.0824
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3KI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14758
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.11500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : 0.56300
REMARK 200 R SYM FOR SHELL (I) : 0.60400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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 3KHX, INDEPENDENT DOMAINS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MEGNESIUM ACETATE TETRAHYDRATE,
REMARK 280 0.1M SODIUM CACODYLATE PH 6.8, 22.0% POLYETHYLENE GLYCOL 8000,
REMARK 280 MICROBATCH METHOD UNDER OIL, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 79.07500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 79.07500
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 79.07500
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 79.07500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 79.07500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 79.07500
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 79.07500
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 79.07500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 79.07500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 79.07500
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 79.07500
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 79.07500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 79.07500
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 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 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 -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 LEU A -9
REMARK 465 VAL A -8
REMARK 465 PRO A -7
REMARK 465 ARG A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 THR A 196
REMARK 465 GLU A 197
REMARK 465 ASP A 198
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 4 CG CD OE1 OE2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 LEU A 195 CG CD1 CD2
REMARK 470 GLU A 201 CG CD OE1 OE2
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 GLN A 237 CG CD OE1 NE2
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 LYS A 379 CG CD CE NZ
REMARK 470 THR A 404 OG1 CG2
REMARK 470 SER A 433 OG
REMARK 470 GLU A 469 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 5 CD CE NZ
REMARK 480 GLU A 201 C
REMARK 480 GLN A 394 CG CD OE1 NE2
REMARK 480 LYS A 424 CE NZ
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 OE2 GLU A 149 O3 PO4 A 472 2.01
REMARK 500 OE2 GLU A 150 O2 PO4 A 472 2.19
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 GLU A 175 CG GLU A 175 CD -0.102
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 ALA A 72 -52.60 -132.20
REMARK 500 ALA A 110 145.59 166.24
REMARK 500 SER A 151 -64.05 -129.32
REMARK 500 ASP A 173 35.14 -175.31
REMARK 500 ALA A 174 -115.27 -125.86
REMARK 500 GLU A 230 -75.83 -139.30
REMARK 500 ASN A 405 -7.77 71.26
REMARK 500 ALA A 430 -90.99 94.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 173 ALA A 174 120.57
REMARK 500 GLY A 429 ALA A 430 -144.05
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 MN A 471 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 84 NE2
REMARK 620 2 ASP A 115 OD2 69.3
REMARK 620 3 ASP A 173 OD2 81.0 133.6
REMARK 620 4 ASP A 173 OD1 96.4 94.9 52.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 470 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 115 OD1
REMARK 620 2 GLU A 150 OE2 142.3
REMARK 620 3 GLU A 150 OE1 91.4 55.2
REMARK 620 4 HIS A 440 NE2 108.7 79.2 119.6
REMARK 620 5 PO4 A 472 O2 146.6 66.7 103.2 90.1
REMARK 620 N 1 2 3 4
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 472
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KHX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE (SAPEP/
REMARK 900 DAPE) IN THE APO-FORM
REMARK 900 RELATED ID: 3KHZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF R350A MUTANT OF STAPHYLOCOCCUS AUREUS
REMARK 900 METALLOPEPTIDASE (SAPEP/DAPE) IN THE APO-FORM
DBREF 3KI9 A 1 469 UNP Q5HF23 PEPVL_STAAC 1 469
SEQADV 3KI9 MET A -22 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 GLY A -21 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 SER A -20 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 SER A -19 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -18 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -17 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -16 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -15 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -14 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -13 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 SER A -12 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 SER A -11 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 GLY A -10 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 LEU A -9 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 VAL A -8 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 PRO A -7 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 ARG A -6 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 GLY A -5 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 SER A -4 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 HIS A -3 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 MET A -2 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 ALA A -1 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KI9 SER A 0 UNP Q5HF23 EXPRESSION TAG
SEQRES 1 A 492 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 492 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET TRP LYS
SEQRES 3 A 492 GLU LYS VAL GLN GLN TYR GLU ASP GLN ILE ILE ASN ASP
SEQRES 4 A 492 LEU LYS GLY LEU LEU ALA ILE GLU SER VAL ARG ASP ASP
SEQRES 5 A 492 ALA LYS ALA SER GLU ASP ALA PRO VAL GLY PRO GLY PRO
SEQRES 6 A 492 ARG LYS ALA LEU ASP TYR MET TYR GLU ILE ALA HIS ARG
SEQRES 7 A 492 ASP GLY PHE THR THR HIS ASP VAL ASP HIS ILE ALA GLY
SEQRES 8 A 492 ARG ILE GLU ALA GLY LYS GLY ASN ASP VAL LEU GLY ILE
SEQRES 9 A 492 LEU CYS HIS VAL ASP VAL VAL PRO ALA GLY ASP GLY TRP
SEQRES 10 A 492 ASP SER ASN PRO PHE GLU PRO VAL VAL THR GLU ASP ALA
SEQRES 11 A 492 ILE ILE ALA ARG GLY THR LEU ASP ASP LYS GLY PRO THR
SEQRES 12 A 492 ILE ALA ALA TYR TYR ALA ILE LYS ILE LEU GLU ASP MET
SEQRES 13 A 492 ASN VAL ASP TRP LYS LYS ARG ILE HIS MET ILE ILE GLY
SEQRES 14 A 492 THR ASP GLU GLU SER ASP TRP LYS CYS THR ASP ARG TYR
SEQRES 15 A 492 PHE LYS THR GLU GLU MET PRO THR LEU GLY PHE ALA PRO
SEQRES 16 A 492 ASP ALA GLU PHE PRO CYS ILE HIS GLY GLU LYS GLY ILE
SEQRES 17 A 492 THR THR PHE ASP LEU VAL GLN ASN LYS LEU THR GLU ASP
SEQRES 18 A 492 GLN ASP GLU PRO ASP TYR GLU LEU ILE THR PHE LYS SER
SEQRES 19 A 492 GLY GLU ARG TYR ASN MET VAL PRO ASP HIS ALA GLU ALA
SEQRES 20 A 492 ARG VAL LEU VAL LYS GLU ASN MET THR ASP VAL ILE GLN
SEQRES 21 A 492 ASP PHE GLU TYR PHE LEU GLU GLN ASN HIS LEU GLN GLY
SEQRES 22 A 492 ASP SER THR VAL ASP SER GLY ILE LEU VAL LEU THR VAL
SEQRES 23 A 492 GLU GLY LYS ALA VAL HIS GLY MET ASP PRO SER ILE GLY
SEQRES 24 A 492 VAL ASN ALA GLY LEU TYR LEU LEU LYS PHE LEU ALA SER
SEQRES 25 A 492 LEU ASN LEU ASP ASN ASN ALA GLN ALA PHE VAL ALA PHE
SEQRES 26 A 492 SER ASN ARG TYR LEU PHE ASN SER ASP PHE GLY GLU LYS
SEQRES 27 A 492 MET GLY MET LYS PHE HIS THR ASP VAL MET GLY ASP VAL
SEQRES 28 A 492 THR THR ASN ILE GLY VAL ILE THR TYR ASP ASN GLU ASN
SEQRES 29 A 492 ALA GLY LEU PHE GLY ILE ASN LEU ARG TYR PRO GLU GLY
SEQRES 30 A 492 PHE GLU PHE GLU LYS ALA MET ASP ARG PHE ALA ASN GLU
SEQRES 31 A 492 ILE GLN GLN TYR GLY PHE GLU VAL LYS LEU GLY LYS VAL
SEQRES 32 A 492 GLN PRO PRO HIS TYR VAL ASP LYS ASN ASP PRO PHE VAL
SEQRES 33 A 492 GLN LYS LEU VAL THR ALA TYR ARG ASN GLN THR ASN ASP
SEQRES 34 A 492 MET THR GLU PRO TYR THR ILE GLY GLY GLY THR TYR ALA
SEQRES 35 A 492 ARG ASN LEU ASP LYS GLY VAL ALA PHE GLY ALA MET PHE
SEQRES 36 A 492 SER ASP SER GLU ASP LEU MET HIS GLN LYS ASN GLU TYR
SEQRES 37 A 492 ILE THR LYS LYS GLN LEU PHE ASN ALA THR SER ILE TYR
SEQRES 38 A 492 LEU GLU ALA ILE TYR SER LEU CYS VAL GLU GLU
HET MN A 470 1
HET MN A 471 1
HET PO4 A 472 5
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 MN 2(MN 2+)
FORMUL 4 PO4 O4 P 3-
FORMUL 5 HOH *26(H2 O)
HELIX 1 1 MET A 1 GLN A 7 1 7
HELIX 2 2 GLU A 10 LEU A 21 1 12
HELIX 3 3 PRO A 40 ARG A 55 1 16
HELIX 4 4 LYS A 117 ASP A 132 1 16
HELIX 5 5 LYS A 154 THR A 162 1 9
HELIX 6 6 THR A 233 ASN A 246 1 14
HELIX 7 7 ALA A 279 LEU A 287 1 9
HELIX 8 8 ASN A 294 TYR A 306 1 13
HELIX 9 9 PHE A 357 GLN A 369 1 13
HELIX 10 10 PRO A 391 THR A 404 1 14
HELIX 11 11 LYS A 448 CYS A 466 1 19
SHEET 1 1 1 THR A 59 VAL A 63 0
SHEET 1 2 1 ALA A 67 GLU A 71 0
SHEET 1 3 1 VAL A 78 HIS A 84 0
SHEET 1 4 1 VAL A 102 VAL A 103 0
SHEET 1 5 1 ALA A 107 ILE A 109 0
SHEET 1 6 1 ARG A 140 GLY A 146 0
SHEET 1 7 1 LEU A 168 ALA A 171 0
SHEET 1 8 1 ALA A 174 GLU A 175 0
SHEET 1 9 1 ILE A 179 GLU A 182 0
SHEET 1 10 1 GLY A 184 GLN A 192 0
SHEET 1 11 1 TYR A 204 SER A 211 0
SHEET 1 12 1 HIS A 221 VAL A 228 0
SHEET 1 13 1 GLN A 249 VAL A 254 0
SHEET 1 14 1 LEU A 259 GLU A 264 0
SHEET 1 15 1 HIS A 321 THR A 322 0
SHEET 1 16 1 GLY A 326 ASP A 327 0
SHEET 1 17 1 THR A 329 ASP A 338 0
SHEET 1 18 1 LEU A 344 TYR A 351 0
SHEET 1 19 1 PHE A 373 GLN A 381 0
SHEET 1 20 1 HIS A 384 TYR A 385 0
SHEET 1 21 1 TYR A 411 ILE A 413 0
SHEET 1 22 1 VAL A 426 ALA A 427 0
SHEET 1 23 1 ALA A 430 MET A 431 0
SHEET 1 24 1 TYR A 445 THR A 447 0
LINK NE2 HIS A 84 MN MN A 471 1555 1555 2.36
LINK OD1 ASP A 115 MN MN A 470 1555 1555 1.97
LINK OD2 ASP A 115 MN MN A 471 1555 1555 2.19
LINK OE2 GLU A 150 MN MN A 470 1555 1555 2.04
LINK OE1 GLU A 150 MN MN A 470 1555 1555 2.59
LINK OD2 ASP A 173 MN MN A 471 1555 1555 2.72
LINK OD1 ASP A 173 MN MN A 471 1555 1555 1.95
LINK NE2 HIS A 440 MN MN A 470 1555 1555 2.36
LINK MN MN A 470 O2 PO4 A 472 1555 1555 1.94
CISPEP 1 ASP A 115 ASP A 116 0 3.46
CISPEP 2 PHE A 176 PRO A 177 0 12.65
CISPEP 3 ALA A 342 GLY A 343 0 0.35
SITE 1 AC1 5 ASP A 115 GLU A 150 HIS A 440 MN A 471
SITE 2 AC1 5 PO4 A 472
SITE 1 AC2 6 HIS A 84 ASP A 115 GLU A 149 ASP A 173
SITE 2 AC2 6 MN A 470 PO4 A 472
SITE 1 AC3 8 GLU A 149 GLU A 150 HIS A 269 GLY A 415
SITE 2 AC3 8 GLY A 416 HIS A 440 MN A 470 MN A 471
CRYST1 158.150 158.150 158.150 90.00 90.00 90.00 I 2 3 24
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 0.006323 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006323 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006323 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
