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HEADER HYDROLASE 26-FEB-22 7X2P
TITLE LEGIONELLA PNEUMOPHILA EFFECTOR RAVL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RAVL;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR.
SOURCE 3 PHILADELPHIA 1;
SOURCE 4 ORGANISM_TAXID: 272624;
SOURCE 5 STRAIN: PHILADELPHIA 1 / ATCC 33152 / DSM 7513;
SOURCE 6 GENE: LPG1108;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LEGIONELLA PNEUMOPHILA EFFECTOR RAVL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHENG,Z.LU,S.CHEN
REVDAT 2 29-NOV-23 7X2P 1 REMARK
REVDAT 1 01-MAR-23 7X2P 0
JRNL AUTH J.ZHENG,Z.LU
JRNL TITL LEGIONELLA PNEUMOPHILA EFFECTOR RAVL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 9974
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.289
REMARK 3 R VALUE (WORKING SET) : 0.284
REMARK 3 FREE R VALUE : 0.337
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.920
REMARK 3 FREE R VALUE TEST SET COUNT : 989
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 33.1500 - 5.5300 0.99 1541 169 0.2680 0.2902
REMARK 3 2 5.5300 - 4.3900 1.00 1501 170 0.2523 0.2927
REMARK 3 3 4.3900 - 3.8400 1.00 1487 162 0.2589 0.3526
REMARK 3 4 3.8400 - 3.4900 1.00 1501 159 0.3277 0.3920
REMARK 3 5 3.4900 - 3.2400 0.98 1464 173 0.3220 0.3614
REMARK 3 6 3.2400 - 3.0500 0.65 958 102 0.3061 0.4185
REMARK 3 7 3.0500 - 2.8900 0.36 533 54 0.3531 0.3715
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) : 0.447
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.99
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 : 0.006 3487
REMARK 3 ANGLE : 1.062 4717
REMARK 3 CHIRALITY : 0.071 512
REMARK 3 PLANARITY : 0.007 616
REMARK 3 DIHEDRAL : 17.705 459
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7872 -4.4828 33.7573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1412 T22: 0.4907
REMARK 3 T33: 0.0408 T12: 0.0823
REMARK 3 T13: -0.0052 T23: -0.1622
REMARK 3 L TENSOR
REMARK 3 L11: 2.4921 L22: 1.5727
REMARK 3 L33: 1.8300 L12: -0.2127
REMARK 3 L13: -0.0129 L23: 0.3565
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: 1.6922 S13: 0.4402
REMARK 3 S21: -0.3919 S22: 0.2185 S23: -0.0038
REMARK 3 S31: -0.0977 S32: 0.5277 S33: 0.1072
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and resid 11 through 241)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "B"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7X2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1300027930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : SYNCHROTRON RADIATION
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9974
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 33.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 0.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 10.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 7A16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES SODIUM PH 7.5, 0.8M
REMARK 280 POTASSIUM TARTATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 27.12350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 THR A 1
REMARK 465 GLY A 2
REMARK 465 ILE A 3
REMARK 465 PHE A 4
REMARK 465 ALA A 5
REMARK 465 HIS A 6
REMARK 465 THR A 7
REMARK 465 TYR A 8
REMARK 465 SER A 142
REMARK 465 TYR A 143
REMARK 465 LEU A 144
REMARK 465 ALA A 145
REMARK 465 VAL A 146
REMARK 465 LYS A 147
REMARK 465 PRO A 148
REMARK 465 LEU A 149
REMARK 465 SER A 150
REMARK 465 TRP A 151
REMARK 465 PHE A 152
REMARK 465 SER A 153
REMARK 465 ASP A 154
REMARK 465 SER A 155
REMARK 465 ILE A 156
REMARK 465 ARG A 157
REMARK 465 GLU A 158
REMARK 465 MET A 159
REMARK 465 TYR A 242
REMARK 465 GLN A 243
REMARK 465 ASN A 244
REMARK 465 ASP A 245
REMARK 465 THR A 246
REMARK 465 GLU A 247
REMARK 465 GLU A 248
REMARK 465 VAL A 249
REMARK 465 LYS A 250
REMARK 465 ILE A 251
REMARK 465 SER A 252
REMARK 465 THR B 1
REMARK 465 GLY B 2
REMARK 465 ILE B 3
REMARK 465 PHE B 4
REMARK 465 ALA B 5
REMARK 465 HIS B 6
REMARK 465 THR B 7
REMARK 465 TYR B 8
REMARK 465 TYR B 9
REMARK 465 TRP B 10
REMARK 465 SER B 142
REMARK 465 TYR B 143
REMARK 465 LEU B 144
REMARK 465 ALA B 145
REMARK 465 VAL B 146
REMARK 465 LYS B 147
REMARK 465 PRO B 148
REMARK 465 LEU B 149
REMARK 465 SER B 150
REMARK 465 TRP B 151
REMARK 465 PHE B 152
REMARK 465 SER B 153
REMARK 465 ASP B 154
REMARK 465 SER B 155
REMARK 465 ILE B 156
REMARK 465 ARG B 157
REMARK 465 GLU B 158
REMARK 465 MET B 159
REMARK 465 TYR B 242
REMARK 465 GLN B 243
REMARK 465 ASN B 244
REMARK 465 ASP B 245
REMARK 465 THR B 246
REMARK 465 GLU B 247
REMARK 465 GLU B 248
REMARK 465 VAL B 249
REMARK 465 LYS B 250
REMARK 465 ILE B 251
REMARK 465 SER B 252
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY B 34 C - N - CA ANGL. DEV. = -15.1 DEGREES
REMARK 500 LEU B 71 CB - CG - CD2 ANGL. DEV. = -11.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 74 -126.19 51.56
REMARK 500 LYS A 81 163.20 177.94
REMARK 500 SER A 108 -136.08 56.12
REMARK 500 LEU A 219 78.52 -116.86
REMARK 500 TYR B 25 -136.69 58.26
REMARK 500 GLU B 29 55.37 -97.61
REMARK 500 ALA B 73 89.65 61.07
REMARK 500 PHE B 74 -68.67 -163.36
REMARK 500 SER B 108 -136.84 54.64
REMARK 500 PHE B 120 -50.15 -130.81
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 ALA B 73 PHE B 74 -133.78
REMARK 500 PHE B 74 ASP B 75 137.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7X2P A 1 252 UNP Q5ZWH7 Q5ZWH7_LEGPH 18 269
DBREF 7X2P B 1 252 UNP Q5ZWH7 Q5ZWH7_LEGPH 18 269
SEQADV 7X2P ALA A 192 UNP Q5ZWH7 VAL 209 CONFLICT
SEQADV 7X2P ALA B 192 UNP Q5ZWH7 VAL 209 CONFLICT
SEQRES 1 A 252 THR GLY ILE PHE ALA HIS THR TYR TYR TRP LEU THR SER
SEQRES 2 A 252 PRO ALA GLY ASP GLN SER TYR GLN ASN PRO ASN TYR LYS
SEQRES 3 A 252 ASN GLU GLU ASP ASN ASN THR GLY THR ALA ILE TYR PHE
SEQRES 4 A 252 ILE HIS GLY THR ALA ASP GLN PRO ALA ALA PHE LYS ARG
SEQRES 5 A 252 VAL ALA GLU ARG LEU ILE ASP THR GLY LEU PRO ASP GLU
SEQRES 6 A 252 ILE CYS SER LEU ASN LEU LEU ALA PHE ASP GLN ARG TYR
SEQRES 7 A 252 GLN GLY LYS SER ILE LYS PHE PHE ALA GLU GLN LEU LYS
SEQRES 8 A 252 ASN LYS ILE LYS VAL ASN GLN HIS GLN ARG VAL ILE LEU
SEQRES 9 A 252 MET ALA HIS SER ARG GLY GLY LEU VAL ALA SER TYR PHE
SEQRES 10 A 252 ALA GLU PHE LEU ALA LYS GLU ALA SER ILE ASP VAL PRO
SEQRES 11 A 252 LEU VAL ILE THR MET GLY THR PRO PHE ASN GLY SER TYR
SEQRES 12 A 252 LEU ALA VAL LYS PRO LEU SER TRP PHE SER ASP SER ILE
SEQRES 13 A 252 ARG GLU MET GLU ILE ASN SER GLU PHE LEU ALA GLN LEU
SEQRES 14 A 252 LYS GLN GLU ILE VAL GLU HIS SER VAL SER ALA TYR HIS
SEQRES 15 A 252 PHE PHE ILE ALA LYS GLU ASP ALA ILE ALA PRO GLY GLU
SEQRES 16 A 252 SER GLY TYR ILE LYS ASP TYR VAL ASP LYS TYR PRO GLU
SEQRES 17 A 252 SER LEU HIS ILE LEU ASP ARG HIS GLY HIS LEU SER ILE
SEQRES 18 A 252 MET SER SER HIS ARG LEU VAL SER HIS ILE SER SER LEU
SEQRES 19 A 252 LEU HIS ASP TYR ILE ASP ASP TYR GLN ASN ASP THR GLU
SEQRES 20 A 252 GLU VAL LYS ILE SER
SEQRES 1 B 252 THR GLY ILE PHE ALA HIS THR TYR TYR TRP LEU THR SER
SEQRES 2 B 252 PRO ALA GLY ASP GLN SER TYR GLN ASN PRO ASN TYR LYS
SEQRES 3 B 252 ASN GLU GLU ASP ASN ASN THR GLY THR ALA ILE TYR PHE
SEQRES 4 B 252 ILE HIS GLY THR ALA ASP GLN PRO ALA ALA PHE LYS ARG
SEQRES 5 B 252 VAL ALA GLU ARG LEU ILE ASP THR GLY LEU PRO ASP GLU
SEQRES 6 B 252 ILE CYS SER LEU ASN LEU LEU ALA PHE ASP GLN ARG TYR
SEQRES 7 B 252 GLN GLY LYS SER ILE LYS PHE PHE ALA GLU GLN LEU LYS
SEQRES 8 B 252 ASN LYS ILE LYS VAL ASN GLN HIS GLN ARG VAL ILE LEU
SEQRES 9 B 252 MET ALA HIS SER ARG GLY GLY LEU VAL ALA SER TYR PHE
SEQRES 10 B 252 ALA GLU PHE LEU ALA LYS GLU ALA SER ILE ASP VAL PRO
SEQRES 11 B 252 LEU VAL ILE THR MET GLY THR PRO PHE ASN GLY SER TYR
SEQRES 12 B 252 LEU ALA VAL LYS PRO LEU SER TRP PHE SER ASP SER ILE
SEQRES 13 B 252 ARG GLU MET GLU ILE ASN SER GLU PHE LEU ALA GLN LEU
SEQRES 14 B 252 LYS GLN GLU ILE VAL GLU HIS SER VAL SER ALA TYR HIS
SEQRES 15 B 252 PHE PHE ILE ALA LYS GLU ASP ALA ILE ALA PRO GLY GLU
SEQRES 16 B 252 SER GLY TYR ILE LYS ASP TYR VAL ASP LYS TYR PRO GLU
SEQRES 17 B 252 SER LEU HIS ILE LEU ASP ARG HIS GLY HIS LEU SER ILE
SEQRES 18 B 252 MET SER SER HIS ARG LEU VAL SER HIS ILE SER SER LEU
SEQRES 19 B 252 LEU HIS ASP TYR ILE ASP ASP TYR GLN ASN ASP THR GLU
SEQRES 20 B 252 GLU VAL LYS ILE SER
HELIX 1 AA1 GLN A 46 GLY A 61 1 16
HELIX 2 AA2 SER A 82 ASN A 97 1 16
HELIX 3 AA3 ARG A 109 PHE A 120 1 12
HELIX 4 AA4 PHE A 120 ALA A 125 1 6
HELIX 5 AA5 ASN A 162 GLU A 175 1 14
HELIX 6 AA6 LYS A 187 ALA A 192 1 6
HELIX 7 AA7 ILE A 199 TYR A 206 1 8
HELIX 8 AA8 SER A 224 ASP A 241 1 18
HELIX 9 AA9 GLN B 46 GLY B 61 1 16
HELIX 10 AB1 SER B 82 ASN B 97 1 16
HELIX 11 AB2 SER B 108 PHE B 120 1 13
HELIX 12 AB3 PHE B 120 SER B 126 1 7
HELIX 13 AB4 ASN B 162 GLU B 175 1 14
HELIX 14 AB5 LYS B 187 ALA B 192 1 6
HELIX 15 AB6 ILE B 199 TYR B 206 1 8
HELIX 16 AB7 SER B 220 SER B 223 5 4
HELIX 17 AB8 SER B 224 ASP B 241 1 18
SHEET 1 AA1 8 LEU A 11 THR A 12 0
SHEET 2 AA1 8 GLN A 18 GLN A 21 -1 O SER A 19 N LEU A 11
SHEET 3 AA1 8 ILE A 66 LEU A 72 -1 O LEU A 71 N GLN A 18
SHEET 4 AA1 8 THR A 35 ILE A 40 1 N THR A 35 O CYS A 67
SHEET 5 AA1 8 ILE A 103 HIS A 107 1 O ILE A 103 N TYR A 38
SHEET 6 AA1 8 LEU A 131 MET A 135 1 O ILE A 133 N ALA A 106
SHEET 7 AA1 8 ALA A 180 ALA A 186 1 O PHE A 184 N THR A 134
SHEET 8 AA1 8 LEU A 210 LEU A 213 1 O HIS A 211 N PHE A 183
SHEET 1 AA2 7 SER B 19 GLN B 21 0
SHEET 2 AA2 7 ILE B 66 ASN B 70 -1 O LEU B 69 N TYR B 20
SHEET 3 AA2 7 THR B 35 ILE B 40 1 N ILE B 37 O ASN B 70
SHEET 4 AA2 7 ILE B 103 HIS B 107 1 O MET B 105 N TYR B 38
SHEET 5 AA2 7 LEU B 131 MET B 135 1 O ILE B 133 N ALA B 106
SHEET 6 AA2 7 ALA B 180 ALA B 186 1 O PHE B 184 N THR B 134
SHEET 7 AA2 7 LEU B 210 LEU B 213 1 O HIS B 211 N PHE B 183
CISPEP 1 ASP A 75 GLN A 76 0 -3.64
CISPEP 2 HIS A 218 LEU A 219 0 4.83
CISPEP 3 ASP B 75 GLN B 76 0 -11.31
CISPEP 4 HIS B 218 LEU B 219 0 -0.87
CRYST1 37.377 54.247 128.209 90.00 93.61 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 0.026754 0.000000 0.001688 0.00000
SCALE2 0.000000 0.018434 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007815 0.00000
MTRIX1 1 -0.999375 -0.034847 0.005979 19.66522 1
MTRIX2 1 -0.033257 0.869104 -0.493510 17.35099 1
MTRIX3 1 0.012002 -0.493400 -0.869720 65.11766 1
TER 1718 ASP A 241
TER 3410 ASP B 241
MASTER 355 0 0 17 15 0 0 9 3408 2 0 40
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