HEADER HYDROLASE 27-FEB-14 4PPR
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS D,D-PEPTIDASE RV3330
TITLE 2 IN COMPLEX WITH MEROPENEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLIN-BINDING PROTEIN DACB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 38-368;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV3330, RVBD_3330;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC,
KEYWDS 3 PENICILLIN-BINDING PROTEIN, PEPTIDOGLYCAN D, D-PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.PRIGOZHIN,J.P.HUIZAR,D.MAVRICI,T.ALBER,TB STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (TBSGC)
REVDAT 4 20-SEP-23 4PPR 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK
REVDAT 3 11-MAR-15 4PPR 1 JRNL
REVDAT 2 04-MAR-15 4PPR 1 JRNL
REVDAT 1 05-NOV-14 4PPR 0
JRNL AUTH D.M.PRIGOZHIN,I.V.KRIEGER,J.P.HUIZAR,D.MAVRICI,G.S.WALDO,
JRNL AUTH 2 L.W.HUNG,J.C.SACCHETTINI,T.C.TERWILLIGER,T.ALBER
JRNL TITL SUBFAMILY-SPECIFIC ADAPTATIONS IN THE STRUCTURES OF TWO
JRNL TITL 2 PENICILLIN-BINDING PROTEINS FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF PLOS ONE V. 9 16249 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 25551456
JRNL DOI 10.1371/JOURNAL.PONE.0116249
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20594
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 : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1031
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 47.5000 - 3.8250 1.00 2981 157 0.1667 0.1739
REMARK 3 2 3.8250 - 3.0362 1.00 2826 151 0.1706 0.1984
REMARK 3 3 3.0362 - 2.6524 1.00 2786 146 0.2058 0.2343
REMARK 3 4 2.6524 - 2.4099 1.00 2764 144 0.2060 0.2509
REMARK 3 5 2.4099 - 2.2372 1.00 2746 144 0.2040 0.2429
REMARK 3 6 2.2372 - 2.1053 1.00 2731 146 0.2031 0.2405
REMARK 3 7 2.1053 - 2.0000 0.99 2729 143 0.2207 0.2907
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 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 : 0.004 2297
REMARK 3 ANGLE : 0.876 3143
REMARK 3 CHIRALITY : 0.034 355
REMARK 3 PLANARITY : 0.004 419
REMARK 3 DIHEDRAL : 13.980 824
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 4PPR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.23
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1158
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20630
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.80400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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 2BCF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NACL, 0.1 M HEPES, 1.7 M
REMARK 280 AMMONIUM SULFATE, PH 7.23, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 49.98900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.99450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.98350
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.98900
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.98350
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 24.99450
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 501 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 536 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 568 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 577 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 586 LIES ON A SPECIAL POSITION.
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 35
REMARK 465 HIS A 36
REMARK 465 MET A 37
REMARK 465 PRO A 38
REMARK 465 TYR A 39
REMARK 465 LYS A 40
REMARK 465 VAL A 41
REMARK 465 SER A 42
REMARK 465 THR A 43
REMARK 465 PRO A 44
REMARK 465 PRO A 45
REMARK 465 ALA A 46
REMARK 465 VAL A 47
REMARK 465 ASP A 48
REMARK 465 SER A 49
REMARK 465 SER A 50
REMARK 465 GLU A 51
REMARK 465 VAL A 52
REMARK 465 PRO A 53
REMARK 465 ALA A 54
REMARK 465 ALA A 55
REMARK 465 GLY A 56
REMARK 465 GLU A 57
REMARK 465 PRO A 58
REMARK 465 ASN A 354
REMARK 465 PRO A 355
REMARK 465 ALA A 356
REMARK 465 ASP A 357
REMARK 465 ARG A 358
REMARK 465 GLN A 359
REMARK 465 ALA A 365
REMARK 465 ALA A 366
REMARK 465 ALA A 367
REMARK 465 ARG A 368
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 120 -144.28 48.56
REMARK 500 GLN A 337 117.94 -160.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MER A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS D,D-PEPTIDASE
REMARK 900 RV2911 IN COMPLEX WITH PMSF
DBREF 4PPR A 38 368 UNP O53380 O53380_MYCTU 38 368
SEQADV 4PPR GLY A 35 UNP O53380 EXPRESSION TAG
SEQADV 4PPR HIS A 36 UNP O53380 EXPRESSION TAG
SEQADV 4PPR MET A 37 UNP O53380 EXPRESSION TAG
SEQRES 1 A 334 GLY HIS MET PRO TYR LYS VAL SER THR PRO PRO ALA VAL
SEQRES 2 A 334 ASP SER SER GLU VAL PRO ALA ALA GLY GLU PRO PRO LEU
SEQRES 3 A 334 PRO LEU VAL VAL PRO PRO THR PRO VAL GLY GLY ASN ALA
SEQRES 4 A 334 LEU GLY GLY CYS GLY ILE ILE THR ALA PRO GLY SER ALA
SEQRES 5 A 334 PRO ALA PRO GLY ASP VAL SER ALA GLU ALA TRP LEU VAL
SEQRES 6 A 334 ALA ASP LEU ASP SER GLY ALA VAL ILE ALA ALA ARG ASP
SEQRES 7 A 334 PRO HIS GLY ARG HIS ARG PRO ALA SER VAL ILE LYS VAL
SEQRES 8 A 334 LEU VAL ALA MET ALA SER ILE ASN THR LEU THR LEU ASN
SEQRES 9 A 334 LYS SER VAL ALA GLY THR ALA ASP ASP ALA ALA VAL GLU
SEQRES 10 A 334 GLY THR LYS VAL GLY VAL ASN THR GLY GLY THR TYR THR
SEQRES 11 A 334 VAL ASN GLN LEU LEU HIS GLY LEU LEU MET HIS SER GLY
SEQRES 12 A 334 ASN ASP ALA ALA TYR ALA LEU ALA ARG GLN LEU GLY GLY
SEQRES 13 A 334 MET PRO ALA ALA LEU GLU LYS ILE ASN LEU LEU ALA ALA
SEQRES 14 A 334 LYS LEU GLY GLY ARG ASP THR ARG VAL ALA THR PRO SER
SEQRES 15 A 334 GLY LEU ASP GLY PRO GLY MET SER THR SER ALA TYR ASP
SEQRES 16 A 334 ILE GLY LEU PHE TYR ARG TYR ALA TRP GLN ASN PRO VAL
SEQRES 17 A 334 PHE ALA ASP ILE VAL ALA THR ARG THR PHE ASP PHE PRO
SEQRES 18 A 334 GLY HIS GLY ASP HIS PRO GLY TYR GLU LEU GLU ASN ASP
SEQRES 19 A 334 ASN GLN LEU LEU TYR ASN TYR PRO GLY ALA LEU GLY GLY
SEQRES 20 A 334 LYS THR GLY TYR THR ASP ASP ALA GLY GLN THR PHE VAL
SEQRES 21 A 334 GLY ALA ALA ASN ARG ASP GLY ARG ARG LEU MET THR VAL
SEQRES 22 A 334 LEU LEU HIS GLY THR ARG GLN PRO ILE PRO PRO TRP GLU
SEQRES 23 A 334 GLN ALA ALA HIS LEU LEU ASP TYR GLY PHE ASN THR PRO
SEQRES 24 A 334 ALA GLY THR GLN ILE GLY THR LEU ILE GLU PRO ASP PRO
SEQRES 25 A 334 SER LEU MET SER THR ASP ARG ASN PRO ALA ASP ARG GLN
SEQRES 26 A 334 ARG VAL ASP PRO GLN ALA ALA ALA ARG
HET MER A 400 26
HETNAM MER (4R,5S)-3-{[(3S,5S)-5-(DIMETHYLCARBAMOYL)PYRROLIDIN-3-
HETNAM 2 MER YL]SULFANYL}-5-[(2S,3R)-3-HYDROXY-1-OXOBUTAN-2-YL]-4-
HETNAM 3 MER METHYL-4,5-D IHYDRO-1H-PYRROLE-2-CARBOXYLIC ACID
HETSYN MER MEROPENEM, BOUND FORM
FORMUL 2 MER C17 H27 N3 O5 S
FORMUL 3 HOH *144(H2 O)
HELIX 1 1 GLY A 71 GLY A 76 5 6
HELIX 2 2 PRO A 119 VAL A 122 5 4
HELIX 3 3 ILE A 123 LEU A 135 1 13
HELIX 4 4 THR A 144 VAL A 150 1 7
HELIX 5 5 VAL A 165 HIS A 175 1 11
HELIX 6 6 GLY A 177 LEU A 188 1 12
HELIX 7 7 GLY A 190 LEU A 205 1 16
HELIX 8 8 SER A 226 GLN A 239 1 14
HELIX 9 9 ASN A 240 ALA A 248 1 9
HELIX 10 10 ASN A 269 TYR A 275 1 7
HELIX 11 11 PRO A 317 THR A 332 1 16
HELIX 12 12 ASP A 345 SER A 350 5 6
SHEET 1 A 6 ILE A 79 THR A 81 0
SHEET 2 A 6 ALA A 106 ARG A 111 -1 O ALA A 110 N ILE A 80
SHEET 3 A 6 ALA A 96 ASP A 101 -1 N TRP A 97 O ARG A 111
SHEET 4 A 6 ARG A 302 GLY A 311 -1 O MET A 305 N ALA A 100
SHEET 5 A 6 GLY A 290 ARG A 299 -1 N PHE A 293 O LEU A 308
SHEET 6 A 6 ALA A 278 THR A 286 -1 N LYS A 282 O VAL A 294
SHEET 1 B 3 ILE A 79 THR A 81 0
SHEET 2 B 3 ALA A 106 ARG A 111 -1 O ALA A 110 N ILE A 80
SHEET 3 B 3 GLY A 339 THR A 340 -1 O GLY A 339 N VAL A 107
SHEET 1 C 2 SER A 140 ALA A 142 0
SHEET 2 C 2 THR A 162 THR A 164 -1 O TYR A 163 N VAL A 141
SHEET 1 D 2 THR A 251 PHE A 254 0
SHEET 2 D 2 TYR A 263 GLU A 266 -1 O LEU A 265 N PHE A 252
SSBOND 1 CYS A 77 CYS A 77 1555 7554 2.02
LINK OG SER A 121 C1 MER A 400 1555 1555 1.38
CISPEP 1 GLN A 314 PRO A 315 0 1.86
SITE 1 AC1 14 ALA A 120 SER A 121 THR A 153 SER A 176
SITE 2 AC1 14 ASN A 178 GLY A 217 LEU A 218 LYS A 282
SITE 3 AC1 14 THR A 283 GLY A 284 TYR A 285 GLN A 291
SITE 4 AC1 14 ARG A 313 HOH A 553
CRYST1 76.291 76.291 99.978 90.00 90.00 90.00 P 41 2 2 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 0.013108 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013108 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010002 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
