HEADER HYDROLASE 31-OCT-09 3KHZ
TITLE CRYSTAL STRUCTURE OF R350A MUTANT OF STAPHYLOCOCCUS AUREUS
TITLE 2 METALLOPEPTIDASE (SAPEP/DAPE) IN THE APO-FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIPEPTIDASE SACOL1801;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: METALLOPEPTIDASE (DAPE);
COMPND 5 EC: 3.4.13.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 R350A MUTANT-DIPEPTIDASE, DAPE, METALLOPEPTIDASE, DIPEPTIDASE,
KEYWDS 2 HYDROLASE, METAL-BINDING, METALLOPROTEASE, PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.GIRISH,B.GOPAL
REVDAT 3 01-NOV-23 3KHZ 1 SEQADV
REVDAT 2 28-SEP-11 3KHZ 1 JRNL VERSN
REVDAT 1 07-JUL-10 3KHZ 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. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 37576
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1984
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2739
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 141
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6767
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 113
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : -2.31000
REMARK 3 B33 (A**2) : 2.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.75000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.440
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.212
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.762
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6934 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9418 ; 1.350 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 870 ; 6.386 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 341 ;38.307 ;25.367
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1122 ;18.953 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;22.597 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1033 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5367 ; 0.006 ; 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): 4315 ; 0.588 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6929 ; 1.111 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2619 ; 1.627 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2486 ; 2.619 ; 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 : 6
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 1 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5403 11.9060 -2.0170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0647 T22: 0.0225
REMARK 3 T33: 0.0901 T12: 0.0039
REMARK 3 T13: -0.0613 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.4892 L22: 2.8434
REMARK 3 L33: 4.2805 L12: -0.9400
REMARK 3 L13: 0.6346 L23: -0.5497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: 0.0726 S13: 0.0989
REMARK 3 S21: -0.3304 S22: -0.1574 S23: 0.3393
REMARK 3 S31: 0.1845 S32: -0.1005 S33: 0.1385
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 389 A 465
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0190 11.7764 -16.4336
REMARK 3 T TENSOR
REMARK 3 T11: 0.4932 T22: 0.4511
REMARK 3 T33: 0.2331 T12: 0.0391
REMARK 3 T13: -0.1672 T23: -0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 0.8964 L22: 5.5865
REMARK 3 L33: 2.9055 L12: 0.8315
REMARK 3 L13: -0.0863 L23: -1.1001
REMARK 3 S TENSOR
REMARK 3 S11: -0.1056 S12: 0.4138 S13: -0.0880
REMARK 3 S21: -0.6310 S22: 0.0059 S23: 0.4621
REMARK 3 S31: 0.3504 S32: -0.4722 S33: 0.0996
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 : B 1 B 182
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5053 42.5170 -28.3301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0370 T22: 0.0193
REMARK 3 T33: 0.1561 T12: 0.0164
REMARK 3 T13: -0.0110 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 2.2666 L22: 3.9593
REMARK 3 L33: 1.6974 L12: -0.7306
REMARK 3 L13: -0.1478 L23: 0.8674
REMARK 3 S TENSOR
REMARK 3 S11: -0.1121 S12: -0.0766 S13: -0.2312
REMARK 3 S21: 0.2803 S22: 0.1228 S23: 0.3513
REMARK 3 S31: 0.1250 S32: -0.0679 S33: -0.0107
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 389 B 465
REMARK 3 ORIGIN FOR THE GROUP (A): -47.9823 41.6839 -26.7571
REMARK 3 T TENSOR
REMARK 3 T11: 0.1765 T22: 0.4428
REMARK 3 T33: 0.6532 T12: -0.0554
REMARK 3 T13: 0.0658 T23: -0.0998
REMARK 3 L TENSOR
REMARK 3 L11: 2.4061 L22: 6.4520
REMARK 3 L33: 0.3424 L12: -0.6934
REMARK 3 L13: -0.7419 L23: -0.4368
REMARK 3 S TENSOR
REMARK 3 S11: -0.1246 S12: -0.1807 S13: -0.1959
REMARK 3 S21: 0.6485 S22: 0.0718 S23: 0.9198
REMARK 3 S31: -0.0023 S32: -0.0813 S33: 0.0529
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 183 A 388
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3106 61.6462 -9.2944
REMARK 3 T TENSOR
REMARK 3 T11: 0.0148 T22: 0.0420
REMARK 3 T33: 0.0234 T12: 0.0048
REMARK 3 T13: -0.0065 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.2764 L22: 5.6686
REMARK 3 L33: 1.0561 L12: 0.8585
REMARK 3 L13: 0.5167 L23: -0.7831
REMARK 3 S TENSOR
REMARK 3 S11: 0.0596 S12: -0.1676 S13: 0.0689
REMARK 3 S21: 0.0974 S22: -0.0033 S23: 0.2137
REMARK 3 S31: 0.0795 S32: 0.0104 S33: -0.0563
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 183 B 388
REMARK 3 ORIGIN FOR THE GROUP (A): -39.8939 91.9475 -23.9293
REMARK 3 T TENSOR
REMARK 3 T11: 0.0233 T22: 0.0613
REMARK 3 T33: 0.0806 T12: 0.0113
REMARK 3 T13: 0.0221 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 1.5683 L22: 6.2198
REMARK 3 L33: 1.3007 L12: 0.0041
REMARK 3 L13: -0.3656 L23: -0.9811
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: 0.1131 S13: 0.0731
REMARK 3 S21: 0.3478 S22: 0.1572 S23: 0.3260
REMARK 3 S31: -0.1016 S32: 0.0298 S33: -0.1805
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 3KHZ 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_1000056016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39597
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 60.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41400
REMARK 200 R SYM FOR SHELL (I) : 0.44200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
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
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M MES, 30.0%
REMARK 280 PEG MONO-METHYL-ETHER 5000, PH 6.5, MICROBATCH METHOD UNDER OIL,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 66.76000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 ASN A 405
REMARK 465 ASP A 406
REMARK 465 MET A 407
REMARK 465 THR A 408
REMARK 465 GLU A 409
REMARK 465 PRO A 410
REMARK 465 TYR A 411
REMARK 465 THR A 412
REMARK 465 ILE A 413
REMARK 465 GLY A 414
REMARK 465 GLY A 415
REMARK 465 GLY A 416
REMARK 465 THR A 417
REMARK 465 TYR A 418
REMARK 465 ALA A 419
REMARK 465 ARG A 420
REMARK 465 ASN A 421
REMARK 465 LEU A 422
REMARK 465 ASP A 423
REMARK 465 LYS A 424
REMARK 465 GLY A 425
REMARK 465 VAL A 426
REMARK 465 ALA A 427
REMARK 465 PHE A 428
REMARK 465 GLY A 429
REMARK 465 ALA A 430
REMARK 465 MET A 431
REMARK 465 PHE A 432
REMARK 465 SER A 433
REMARK 465 ASP A 434
REMARK 465 SER A 435
REMARK 465 GLU A 436
REMARK 465 ASP A 437
REMARK 465 LEU A 438
REMARK 465 MET A 439
REMARK 465 GLU A 468
REMARK 465 GLU A 469
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 LEU B -9
REMARK 465 VAL B -8
REMARK 465 PRO B -7
REMARK 465 ARG B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 ASN B 405
REMARK 465 ASP B 406
REMARK 465 MET B 407
REMARK 465 THR B 408
REMARK 465 GLU B 409
REMARK 465 PRO B 410
REMARK 465 TYR B 411
REMARK 465 THR B 412
REMARK 465 ILE B 413
REMARK 465 GLY B 414
REMARK 465 GLY B 415
REMARK 465 GLY B 416
REMARK 465 THR B 417
REMARK 465 TYR B 418
REMARK 465 ALA B 419
REMARK 465 ARG B 420
REMARK 465 ASN B 421
REMARK 465 LEU B 422
REMARK 465 ASP B 423
REMARK 465 LYS B 424
REMARK 465 GLY B 425
REMARK 465 VAL B 426
REMARK 465 ALA B 427
REMARK 465 PHE B 428
REMARK 465 GLY B 429
REMARK 465 ALA B 430
REMARK 465 MET B 431
REMARK 465 PHE B 432
REMARK 465 SER B 433
REMARK 465 ASP B 434
REMARK 465 SER B 435
REMARK 465 GLU B 436
REMARK 465 ASP B 437
REMARK 465 LEU B 438
REMARK 465 MET B 439
REMARK 465 GLU B 469
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 ASP A 92 CG OD1 OD2
REMARK 470 GLU A 105 CG CD OE1 OE2
REMARK 470 ASP A 106 CG OD1 OD2
REMARK 470 ASN A 134 CG OD1 ND2
REMARK 470 ASP A 152 CG OD1 OD2
REMARK 470 ASP A 173 CG OD1 OD2
REMARK 470 ASP A 198 CG OD1 OD2
REMARK 470 GLU A 213 CG CD OE1 OE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 MET A 325 CG SD CE
REMARK 470 GLU A 340 CG CD OE1 OE2
REMARK 470 LYS A 379 CG CD CE NZ
REMARK 470 LYS A 388 CG CD CE NZ
REMARK 470 THR A 404 OG1 CG2
REMARK 470 HIS A 440 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 449 CG CD CE NZ
REMARK 470 GLN B 8 CG CD OE1 NE2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 ASN B 134 CG OD1 ND2
REMARK 470 ASP B 173 CG OD1 OD2
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 ASP B 198 CG OD1 OD2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 GLU B 244 CG CD OE1 OE2
REMARK 470 GLN B 249 CG CD OE1 NE2
REMARK 470 ASP B 255 CG OD1 OD2
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 LYS B 379 CG CD CE NZ
REMARK 470 ARG B 401 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 440 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 449 CG CD CE NZ
REMARK 470 GLU B 468 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 GLU A 4 CG CD OE1 OE2
REMARK 480 LYS A 5 CE NZ
REMARK 480 LYS A 395 CD CE NZ
REMARK 480 ARG A 401 NE CZ NH1 NH2
REMARK 480 LYS A 442 CG CD CE NZ
REMARK 480 LYS B 442 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 GLU A 230 -163.53 -105.46
REMARK 500 ASP A 272 99.20 -163.22
REMARK 500 VAL A 324 -34.25 -137.79
REMARK 500 ALA A 342 -134.86 61.64
REMARK 500 ALA B 110 152.71 174.17
REMARK 500 ALA B 342 -138.17 60.37
REMARK 500 GLN B 441 -155.50 -36.87
REMARK 500 VAL B 467 -65.14 -132.96
REMARK 500
REMARK 500 REMARK: NULL
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: 3KI9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE (SAPEP/
REMARK 900 DAPE) IN THE MN2+ BOUND FORM
DBREF 3KHZ A 1 469 UNP Q5HF23 PEPVL_STAAC 1 469
DBREF 3KHZ B 1 469 UNP Q5HF23 PEPVL_STAAC 1 469
SEQADV 3KHZ MET A -22 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ GLY A -21 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER A -20 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER A -19 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -18 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -17 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -16 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -15 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -14 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -13 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER A -12 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER A -11 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ GLY A -10 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ LEU A -9 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ VAL A -8 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ PRO A -7 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ ARG A -6 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ GLY A -5 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER A -4 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS A -3 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ MET A -2 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ ALA A -1 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER A 0 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ ALA A 350 UNP Q5HF23 ARG 350 ENGINEERED MUTATION
SEQADV 3KHZ MET B -22 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ GLY B -21 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER B -20 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER B -19 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -18 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -17 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -16 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -15 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -14 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -13 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER B -12 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER B -11 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ GLY B -10 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ LEU B -9 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ VAL B -8 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ PRO B -7 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ ARG B -6 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ GLY B -5 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER B -4 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ HIS B -3 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ MET B -2 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ ALA B -1 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ SER B 0 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHZ ALA B 350 UNP Q5HF23 ARG 350 ENGINEERED MUTATION
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 ALA 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
SEQRES 1 B 492 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 492 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET TRP LYS
SEQRES 3 B 492 GLU LYS VAL GLN GLN TYR GLU ASP GLN ILE ILE ASN ASP
SEQRES 4 B 492 LEU LYS GLY LEU LEU ALA ILE GLU SER VAL ARG ASP ASP
SEQRES 5 B 492 ALA LYS ALA SER GLU ASP ALA PRO VAL GLY PRO GLY PRO
SEQRES 6 B 492 ARG LYS ALA LEU ASP TYR MET TYR GLU ILE ALA HIS ARG
SEQRES 7 B 492 ASP GLY PHE THR THR HIS ASP VAL ASP HIS ILE ALA GLY
SEQRES 8 B 492 ARG ILE GLU ALA GLY LYS GLY ASN ASP VAL LEU GLY ILE
SEQRES 9 B 492 LEU CYS HIS VAL ASP VAL VAL PRO ALA GLY ASP GLY TRP
SEQRES 10 B 492 ASP SER ASN PRO PHE GLU PRO VAL VAL THR GLU ASP ALA
SEQRES 11 B 492 ILE ILE ALA ARG GLY THR LEU ASP ASP LYS GLY PRO THR
SEQRES 12 B 492 ILE ALA ALA TYR TYR ALA ILE LYS ILE LEU GLU ASP MET
SEQRES 13 B 492 ASN VAL ASP TRP LYS LYS ARG ILE HIS MET ILE ILE GLY
SEQRES 14 B 492 THR ASP GLU GLU SER ASP TRP LYS CYS THR ASP ARG TYR
SEQRES 15 B 492 PHE LYS THR GLU GLU MET PRO THR LEU GLY PHE ALA PRO
SEQRES 16 B 492 ASP ALA GLU PHE PRO CYS ILE HIS GLY GLU LYS GLY ILE
SEQRES 17 B 492 THR THR PHE ASP LEU VAL GLN ASN LYS LEU THR GLU ASP
SEQRES 18 B 492 GLN ASP GLU PRO ASP TYR GLU LEU ILE THR PHE LYS SER
SEQRES 19 B 492 GLY GLU ARG TYR ASN MET VAL PRO ASP HIS ALA GLU ALA
SEQRES 20 B 492 ARG VAL LEU VAL LYS GLU ASN MET THR ASP VAL ILE GLN
SEQRES 21 B 492 ASP PHE GLU TYR PHE LEU GLU GLN ASN HIS LEU GLN GLY
SEQRES 22 B 492 ASP SER THR VAL ASP SER GLY ILE LEU VAL LEU THR VAL
SEQRES 23 B 492 GLU GLY LYS ALA VAL HIS GLY MET ASP PRO SER ILE GLY
SEQRES 24 B 492 VAL ASN ALA GLY LEU TYR LEU LEU LYS PHE LEU ALA SER
SEQRES 25 B 492 LEU ASN LEU ASP ASN ASN ALA GLN ALA PHE VAL ALA PHE
SEQRES 26 B 492 SER ASN ARG TYR LEU PHE ASN SER ASP PHE GLY GLU LYS
SEQRES 27 B 492 MET GLY MET LYS PHE HIS THR ASP VAL MET GLY ASP VAL
SEQRES 28 B 492 THR THR ASN ILE GLY VAL ILE THR TYR ASP ASN GLU ASN
SEQRES 29 B 492 ALA GLY LEU PHE GLY ILE ASN LEU ALA TYR PRO GLU GLY
SEQRES 30 B 492 PHE GLU PHE GLU LYS ALA MET ASP ARG PHE ALA ASN GLU
SEQRES 31 B 492 ILE GLN GLN TYR GLY PHE GLU VAL LYS LEU GLY LYS VAL
SEQRES 32 B 492 GLN PRO PRO HIS TYR VAL ASP LYS ASN ASP PRO PHE VAL
SEQRES 33 B 492 GLN LYS LEU VAL THR ALA TYR ARG ASN GLN THR ASN ASP
SEQRES 34 B 492 MET THR GLU PRO TYR THR ILE GLY GLY GLY THR TYR ALA
SEQRES 35 B 492 ARG ASN LEU ASP LYS GLY VAL ALA PHE GLY ALA MET PHE
SEQRES 36 B 492 SER ASP SER GLU ASP LEU MET HIS GLN LYS ASN GLU TYR
SEQRES 37 B 492 ILE THR LYS LYS GLN LEU PHE ASN ALA THR SER ILE TYR
SEQRES 38 B 492 LEU GLU ALA ILE TYR SER LEU CYS VAL GLU GLU
FORMUL 3 HOH *113(H2 O)
HELIX 1 1 SER A 0 GLN A 8 1 9
HELIX 2 2 TYR A 9 ALA A 22 1 14
HELIX 3 3 GLY A 39 ASP A 56 1 18
HELIX 4 4 ASP A 116 MET A 133 1 18
HELIX 5 5 ASP A 157 GLU A 163 1 7
HELIX 6 6 MET A 232 ASN A 246 1 15
HELIX 7 7 ASN A 278 ALA A 288 1 11
HELIX 8 8 ASP A 293 LEU A 307 1 15
HELIX 9 9 GLY A 313 GLY A 317 5 5
HELIX 10 10 GLU A 356 GLN A 370 1 15
HELIX 11 11 VAL A 386 ASN A 389 5 4
HELIX 12 12 ASP A 390 GLN A 403 1 14
HELIX 13 13 LYS A 448 VAL A 467 1 20
HELIX 14 14 SER B 0 GLN B 8 1 9
HELIX 15 15 TYR B 9 ALA B 22 1 14
HELIX 16 16 GLY B 39 GLY B 57 1 19
HELIX 17 17 ASP B 116 MET B 133 1 18
HELIX 18 18 ASP B 157 GLU B 163 1 7
HELIX 19 19 MET B 232 ASN B 246 1 15
HELIX 20 20 ASP B 272 GLY B 276 5 5
HELIX 21 21 ASN B 278 ALA B 288 1 11
HELIX 22 22 ASP B 293 LEU B 307 1 15
HELIX 23 23 GLY B 313 GLY B 317 5 5
HELIX 24 24 GLU B 356 ILE B 368 1 13
HELIX 25 25 GLN B 369 TYR B 371 5 3
HELIX 26 26 VAL B 386 ASN B 389 5 4
HELIX 27 27 ASP B 390 THR B 404 1 15
HELIX 28 28 LYS B 448 VAL B 467 1 20
SHEET 1 A 5 THR A 60 VAL A 63 0
SHEET 2 A 5 ALA A 67 GLY A 73 -1 O ALA A 67 N VAL A 63
SHEET 3 A 5 ARG A 140 GLY A 146 -1 O ILE A 145 N GLY A 68
SHEET 4 A 5 VAL A 78 HIS A 84 1 N LEU A 79 O ARG A 140
SHEET 5 A 5 LEU A 168 PHE A 170 1 O LEU A 168 N GLY A 80
SHEET 1 B 3 VAL A 102 VAL A 103 0
SHEET 2 B 3 ALA A 107 ILE A 109 -1 O ILE A 109 N VAL A 102
SHEET 3 B 3 TYR A 445 THR A 447 -1 O ILE A 446 N ILE A 108
SHEET 1 C 8 GLY A 250 ASP A 255 0
SHEET 2 C 8 ILE A 258 GLU A 264 -1 O VAL A 260 N THR A 253
SHEET 3 C 8 HIS A 221 VAL A 228 -1 N ALA A 224 O LEU A 261
SHEET 4 C 8 TYR A 204 GLY A 212 -1 N ILE A 207 O ARG A 225
SHEET 5 C 8 THR A 329 ASP A 338 -1 O ILE A 335 N SER A 211
SHEET 6 C 8 ALA A 342 TYR A 351 -1 O GLY A 346 N VAL A 334
SHEET 7 C 8 GLY A 184 GLN A 192 -1 N PHE A 188 O ILE A 347
SHEET 8 C 8 PHE A 373 GLN A 381 -1 O LYS A 376 N ASP A 189
SHEET 1 D 2 HIS A 321 THR A 322 0
SHEET 2 D 2 GLY A 326 ASP A 327 -1 O GLY A 326 N THR A 322
SHEET 1 E 5 THR B 60 VAL B 63 0
SHEET 2 E 5 ALA B 67 GLY B 73 -1 O ARG B 69 N HIS B 61
SHEET 3 E 5 ARG B 140 GLY B 146 -1 O MET B 143 N ILE B 70
SHEET 4 E 5 VAL B 78 HIS B 84 1 N CYS B 83 O ILE B 144
SHEET 5 E 5 LEU B 168 PHE B 170 1 O LEU B 168 N GLY B 80
SHEET 1 F 3 VAL B 102 VAL B 103 0
SHEET 2 F 3 ALA B 107 ILE B 109 -1 O ILE B 109 N VAL B 102
SHEET 3 F 3 TYR B 445 THR B 447 -1 O ILE B 446 N ILE B 108
SHEET 1 G 8 GLY B 250 ASP B 255 0
SHEET 2 G 8 ILE B 258 GLU B 264 -1 O VAL B 260 N THR B 253
SHEET 3 G 8 HIS B 221 VAL B 228 -1 N ALA B 224 O LEU B 261
SHEET 4 G 8 TYR B 204 SER B 211 -1 N GLU B 205 O LEU B 227
SHEET 5 G 8 THR B 329 ASP B 338 -1 O TYR B 337 N PHE B 209
SHEET 6 G 8 ALA B 342 TYR B 351 -1 O ASN B 348 N ASN B 331
SHEET 7 G 8 GLY B 184 GLN B 192 -1 N GLY B 184 O TYR B 351
SHEET 8 G 8 PHE B 373 GLN B 381 -1 O GLN B 381 N ILE B 185
SSBOND 1 CYS A 155 CYS A 178 1555 1555 2.04
SSBOND 2 CYS B 155 CYS B 178 1555 1555 2.05
CISPEP 1 ASP A 115 ASP A 116 0 2.89
CISPEP 2 GLU A 353 GLY A 354 0 -5.00
CISPEP 3 ASP B 92 GLY B 93 0 -1.97
CISPEP 4 ASP B 115 ASP B 116 0 4.67
CISPEP 5 GLU B 353 GLY B 354 0 -16.99
CRYST1 64.750 133.520 67.710 90.00 95.59 90.00 P 1 21 1 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 0.015444 0.000000 0.001512 0.00000
SCALE2 0.000000 0.007490 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
