HEADER STRUCTURAL PROTEIN 19-APR-14 4CZI
TITLE C. CRESCENTUS MREB, SINGLE FILAMENT, EMPTY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ROD SHAPE-DETERMINING PROTEIN MREB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 9-347;
COMPND 5 SYNONYM: MREB;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: M-I9-CCMREB(F102S, V103G)-A347-GSHHHHHH
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAULOBACTER VIBRIOIDES;
SOURCE 3 ORGANISM_TAXID: 155892;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHIS17
KEYWDS STRUCTURAL PROTEIN, BACTERIAL ACTIN, BACTERIAL CYTOSKELETON
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LOWE,F.VANDENENT
REVDAT 3 20-DEC-23 4CZI 1 REMARK
REVDAT 2 25-JUN-14 4CZI 1 JRNL ATOM MASTER
REVDAT 1 11-JUN-14 4CZI 0
JRNL AUTH F.VAN DEN ENT,T.IZORE,T.A.BHARAT,C.M.JOHNSON,J.LOWE
JRNL TITL BACTERIAL ACTIN MREB FORMS ANTIPARALLEL DOUBLE FILAMENTS.
JRNL REF ELIFE V. 3 02634 2014
JRNL REFN ESSN 2050-084X
JRNL PMID 24843005
JRNL DOI 10.7554/ELIFE.02634
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML3
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 33573
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3159
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.1929 - 5.1160 0.97 2678 128 0.1955 0.2272
REMARK 3 2 5.1160 - 4.0618 0.98 2706 114 0.1544 0.1748
REMARK 3 3 4.0618 - 3.5487 0.97 2688 142 0.1731 0.1730
REMARK 3 4 3.5487 - 3.2244 0.98 2661 142 0.1824 0.2173
REMARK 3 5 3.2244 - 2.9934 0.97 2664 144 0.1837 0.2060
REMARK 3 6 2.9934 - 2.8169 0.97 2668 165 0.1878 0.2028
REMARK 3 7 2.8169 - 2.6759 0.97 2631 140 0.1831 0.2408
REMARK 3 8 2.6759 - 2.5594 0.96 2690 123 0.1734 0.1932
REMARK 3 9 2.5594 - 2.4609 0.96 2618 121 0.1734 0.2577
REMARK 3 10 2.4609 - 2.3760 0.95 2609 144 0.1699 0.2167
REMARK 3 11 2.3760 - 2.3017 0.95 2641 119 0.1867 0.2365
REMARK 3 12 2.3017 - 2.2359 0.95 2623 123 0.1819 0.2320
REMARK 3 13 2.2359 - 2.1770 0.95 2584 124 0.1874 0.2361
REMARK 3 14 2.1770 - 2.1239 0.94 2642 154 0.1858 0.2444
REMARK 3 15 2.1239 - 2.0757 0.95 2544 150 0.1934 0.2362
REMARK 3 16 2.0757 - 2.0315 0.94 2589 127 0.1930 0.2531
REMARK 3 17 2.0315 - 1.9908 0.94 2560 145 0.1995 0.2429
REMARK 3 18 1.9908 - 1.9533 0.94 2542 178 0.1942 0.2385
REMARK 3 19 1.9533 - 1.9184 0.93 2509 99 0.1994 0.2521
REMARK 3 20 1.9184 - 1.8859 0.93 2625 144 0.2091 0.2189
REMARK 3 21 1.8859 - 1.8555 0.93 2503 152 0.2347 0.2535
REMARK 3 22 1.8555 - 1.8269 0.92 2556 153 0.2477 0.2503
REMARK 3 23 1.8269 - 1.8000 0.92 2492 128 0.2608 0.2782
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 38.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 120.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.68670
REMARK 3 B22 (A**2) : 2.93410
REMARK 3 B33 (A**2) : 3.75270
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.21870
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 2360
REMARK 3 ANGLE : 1.298 3186
REMARK 3 CHIRALITY : 0.075 381
REMARK 3 PLANARITY : 0.006 416
REMARK 3 DIHEDRAL : 13.322 894
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4CZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1290060399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33485
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
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 1JCE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 34.61900
REMARK 290 SMTRY3 2 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 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 8
REMARK 465 VAL A 44
REMARK 465 GLY A 45
REMARK 465 GLY A 46
REMARK 465 ARG A 47
REMARK 465 GLY A 114
REMARK 465 ALA A 115
REMARK 465 ALA A 226
REMARK 465 ASP A 227
REMARK 465 GLY A 228
REMARK 465 GLU A 229
REMARK 465 PRO A 335
REMARK 465 LYS A 336
REMARK 465 TRP A 337
REMARK 465 MET A 338
REMARK 465 LYS A 339
REMARK 465 GLY A 340
REMARK 465 VAL A 341
REMARK 465 LEU A 342
REMARK 465 GLU A 343
REMARK 465 SER A 344
REMARK 465 THR A 345
REMARK 465 LEU A 346
REMARK 465 ALA A 347
REMARK 465 GLY A 348
REMARK 465 SER A 349
REMARK 465 HIS A 350
REMARK 465 HIS A 351
REMARK 465 HIS A 352
REMARK 465 HIS A 353
REMARK 465 HIS A 354
REMARK 465 HIS A 355
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 O HOH A 2012 O HOH A 2198 1.92
REMARK 500 OE1 GLU A 275 O HOH A 2265 1.94
REMARK 500 OE1 GLU A 69 O HOH A 2099 1.94
REMARK 500 O HOH A 2169 O HOH A 2305 1.96
REMARK 500 O HOH A 2228 O HOH A 2229 1.97
REMARK 500 O HOH A 2301 O HOH A 2302 1.99
REMARK 500 SG CYS A 110 O HOH A 2011 2.02
REMARK 500 O HOH A 2037 O HOH A 2066 2.06
REMARK 500 N THR A 116 O HOH A 2162 2.09
REMARK 500 O HOH A 2010 O HOH A 2019 2.09
REMARK 500 O HOH A 2139 O HOH A 2142 2.10
REMARK 500 OG SER A 232 NH1 ARG A 249 2.10
REMARK 500 OD1 ASP A 16 O HOH A 2011 2.11
REMARK 500 O HOH A 2014 O HOH A 2196 2.14
REMARK 500 O HOH A 2167 O HOH A 2168 2.15
REMARK 500 O HOH A 2170 O HOH A 2308 2.16
REMARK 500 O HOH A 2045 O HOH A 2146 2.18
REMARK 500 NH2 ARG A 120 O HOH A 2165 2.18
REMARK 500 OE1 GLU A 268 O HOH A 2263 2.19
REMARK 500 O HOH A 2020 O HOH A 2200 2.19
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 A 2069 O HOH A 2278 2555 1.84
REMARK 500 O HOH A 2152 O HOH A 2184 2555 2.06
REMARK 500 O HOH A 2148 O HOH A 2278 2555 2.15
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 VAL A 78 -167.88 -122.06
REMARK 500 ALA A 80 -78.02 -85.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2307 DISTANCE = 7.28 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CZE RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, DOUBLE FILAMENT, EMPTY
REMARK 900 RELATED ID: 4CZF RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, SINGLE FILAMENT, ADP
REMARK 900 RELATED ID: 4CZG RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, SINGLE FILAMENT, ADP, A22 INHIBITOR
REMARK 900 RELATED ID: 4CZH RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, SINGLE FILAMENT, ADP, MP265 INHIBITOR
REMARK 900 RELATED ID: 4CZJ RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, DOUBLE FILAMENT, AMPPNP
REMARK 900 RELATED ID: 4CZK RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, SINGLE FILAMENT, AMPPNP, MP265 INHIBITOR
REMARK 900 RELATED ID: 4CZL RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, MONOMERIC, ADP
REMARK 900 RELATED ID: 4CZM RELATED DB: PDB
REMARK 900 C. CRESCENTUS MREB, MONOMERIC, AMPPNP
DBREF 4CZI A 9 347 UNP B8H609 B8H609_CAUCN 9 347
SEQADV 4CZI MET A 8 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI GLY A 348 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI SER A 349 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI HIS A 350 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI HIS A 351 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI HIS A 352 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI HIS A 353 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI HIS A 354 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI HIS A 355 UNP B8H609 EXPRESSION TAG
SEQADV 4CZI SER A 102 UNP B8H609 PHE 102 ENGINEERED MUTATION
SEQADV 4CZI GLY A 103 UNP B8H609 VAL 103 ENGINEERED MUTATION
SEQRES 1 A 348 MET ILE SER ASN ASP ILE ALA ILE ASP LEU GLY THR ALA
SEQRES 2 A 348 ASN THR LEU ILE TYR GLN LYS GLY LYS GLY ILE VAL LEU
SEQRES 3 A 348 ASN GLU PRO SER VAL VAL ALA LEU ARG ASN VAL GLY GLY
SEQRES 4 A 348 ARG LYS VAL VAL HIS ALA VAL GLY ILE GLU ALA LYS GLN
SEQRES 5 A 348 MET LEU GLY ARG THR PRO GLY HIS MET GLU ALA ILE ARG
SEQRES 6 A 348 PRO MET ARG ASP GLY VAL ILE ALA ASP PHE GLU VAL ALA
SEQRES 7 A 348 GLU GLU MET ILE LYS TYR PHE ILE ARG LYS VAL HIS ASN
SEQRES 8 A 348 ARG LYS GLY SER GLY ASN PRO LYS VAL ILE VAL CYS VAL
SEQRES 9 A 348 PRO SER GLY ALA THR ALA VAL GLU ARG ARG ALA ILE ASN
SEQRES 10 A 348 ASP SER CYS LEU ASN ALA GLY ALA ARG ARG VAL GLY LEU
SEQRES 11 A 348 ILE ASP GLU PRO MET ALA ALA ALA ILE GLY ALA GLY LEU
SEQRES 12 A 348 PRO ILE HIS GLU PRO THR GLY SER MET VAL VAL ASP ILE
SEQRES 13 A 348 GLY GLY GLY THR THR GLU VAL ALA VAL LEU SER LEU SER
SEQRES 14 A 348 GLY ILE VAL TYR SER ARG SER VAL ARG VAL GLY GLY ASP
SEQRES 15 A 348 LYS MET ASP GLU ALA ILE ILE SER TYR MET ARG ARG HIS
SEQRES 16 A 348 HIS ASN LEU LEU ILE GLY GLU THR THR ALA GLU ARG ILE
SEQRES 17 A 348 LYS LYS GLU ILE GLY THR ALA ARG ALA PRO ALA ASP GLY
SEQRES 18 A 348 GLU GLY LEU SER ILE ASP VAL LYS GLY ARG ASP LEU MET
SEQRES 19 A 348 GLN GLY VAL PRO ARG GLU VAL ARG ILE SER GLU LYS GLN
SEQRES 20 A 348 ALA ALA ASP ALA LEU ALA GLU PRO VAL GLY GLN ILE VAL
SEQRES 21 A 348 GLU ALA VAL LYS VAL ALA LEU GLU ALA THR PRO PRO GLU
SEQRES 22 A 348 LEU ALA SER ASP ILE ALA ASP LYS GLY ILE MET LEU THR
SEQRES 23 A 348 GLY GLY GLY ALA LEU LEU ARG GLY LEU ASP ALA GLU ILE
SEQRES 24 A 348 ARG ASP HIS THR GLY LEU PRO VAL THR VAL ALA ASP ASP
SEQRES 25 A 348 PRO LEU SER CYS VAL ALA LEU GLY CYS GLY LYS VAL LEU
SEQRES 26 A 348 GLU HIS PRO LYS TRP MET LYS GLY VAL LEU GLU SER THR
SEQRES 27 A 348 LEU ALA GLY SER HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *308(H2 O)
HELIX 1 1 ILE A 55 LEU A 61 5 7
HELIX 2 2 ASP A 81 HIS A 97 1 17
HELIX 3 3 THR A 116 ASN A 129 1 14
HELIX 4 4 GLU A 140 ALA A 148 1 9
HELIX 5 5 GLY A 187 ASN A 204 1 18
HELIX 6 6 GLY A 208 GLY A 220 1 13
HELIX 7 7 GLU A 252 ALA A 276 1 25
HELIX 8 8 PRO A 278 GLY A 289 1 12
HELIX 9 9 GLY A 294 LEU A 299 5 6
HELIX 10 10 GLY A 301 GLY A 311 1 11
HELIX 11 11 ASP A 319 LEU A 321 5 3
HELIX 12 12 SER A 322 HIS A 334 1 13
SHEET 1 AA 5 GLY A 30 PRO A 36 0
SHEET 2 AA 5 ASN A 21 GLN A 26 -1 O THR A 22 N GLU A 35
SHEET 3 AA 5 ILE A 13 LEU A 17 -1 O ALA A 14 N TYR A 25
SHEET 4 AA 5 LYS A 106 VAL A 111 1 O LYS A 106 N ILE A 13
SHEET 5 AA 5 ARG A 134 ASP A 139 1 O ARG A 134 N VAL A 107
SHEET 1 AB 3 VAL A 49 VAL A 53 0
SHEET 2 AB 3 VAL A 39 ARG A 42 -1 O ALA A 40 N HIS A 51
SHEET 3 AB 3 MET A 68 ILE A 71 -1 O GLU A 69 N LEU A 41
SHEET 1 AC 2 MET A 74 ARG A 75 0
SHEET 2 AC 2 VAL A 78 ILE A 79 -1 O VAL A 78 N ARG A 75
SHEET 1 AD 5 GLY A 177 VAL A 184 0
SHEET 2 AD 5 THR A 168 SER A 174 -1 O THR A 168 N VAL A 184
SHEET 3 AD 5 SER A 158 ILE A 163 -1 O SER A 158 N LEU A 173
SHEET 4 AD 5 ILE A 290 THR A 293 1 O MET A 291 N VAL A 161
SHEET 5 AD 5 VAL A 314 VAL A 316 1 O THR A 315 N LEU A 292
SHEET 1 AE 3 LEU A 205 LEU A 206 0
SHEET 2 AE 3 SER A 232 ASP A 239 -1 O ARG A 238 N LEU A 206
SHEET 3 AE 3 PRO A 245 SER A 251 -1 O ARG A 246 N GLY A 237
CRYST1 51.951 69.238 52.183 90.00 99.56 90.00 P 1 21 1 2
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 0.019249 0.000000 0.003242 0.00000
SCALE2 0.000000 0.014443 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019433 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
