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HEADER HYDROLASE 08-JAN-25 9LF7
TITLE A PAE-HYDROLYSE POC14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POC14_A;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERYTHROBACTER CRYPTUS DSM 12079;
SOURCE 3 ORGANISM_TAXID: 1122970;
SOURCE 4 STRAIN: DSM 12079;
SOURCE 5 GENE: POC14;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTERASE, PAE-HYDROLYZING, HYDROLYSIS, ALPHA/BEITA HYDROLYSE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.RONG,Y.H.WU
REVDAT 1 19-FEB-25 9LF7 0
JRNL AUTH Z.RONG,L.G.HONG,Y.Y.HUO,D.Q.ZHENG,X.W.XU,J.X.LI,Y.H.WU
JRNL TITL STRUCTURE OF A PAE-HYDROLYZING EATERSE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 80299
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 1.8640 - 1.8000 0.98 0 0 0.1641 0.2141
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.60
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 4784
REMARK 3 ANGLE : 0.941 6528
REMARK 3 CHIRALITY : 0.054 751
REMARK 3 PLANARITY : 0.015 860
REMARK 3 DIHEDRAL : 19.321 2914
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 9LF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 10-JAN-25.
REMARK 100 THE DEPOSITION ID IS D_1300055445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 193.15
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NFPSS
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97891
REMARK 200 MONOCHROMATOR : NULL
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 : 80299
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.9000
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.01000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM, 2% V/V
REMARK 280 POLYETHYLENE GLYCOL 400, 2.0 M AMMONIUM SULFATE, PH 7.5,
REMARK 280 EVAPORATION, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 34.32850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.79600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.80150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.79600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.32850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.80150
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL
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 MET A 1
REMARK 465 ARG A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 PRO A 7
REMARK 465 ALA A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 TYR A 11
REMARK 465 ARG A 12
REMARK 465 SER A 13
REMARK 465 ALA A 14
REMARK 465 LYS A 15
REMARK 465 ASP A 16
REMARK 465 THR A 17
REMARK 465 GLY A 18
REMARK 465 GLU A 19
REMARK 465 SER A 20
REMARK 465 MET A 21
REMARK 465 THR A 22
REMARK 465 ASP A 23
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LEU B 3
REMARK 465 ALA B 4
REMARK 465 LYS B 5
REMARK 465 LEU B 6
REMARK 465 PRO B 7
REMARK 465 ALA B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 TYR B 11
REMARK 465 ARG B 12
REMARK 465 SER B 13
REMARK 465 ALA B 14
REMARK 465 LYS B 15
REMARK 465 ASP B 16
REMARK 465 THR B 17
REMARK 465 GLY B 18
REMARK 465 GLU B 19
REMARK 465 SER B 20
REMARK 465 MET B 21
REMARK 465 THR B 22
REMARK 465 ASP B 23
REMARK 465 ALA B 99
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 OG SER B 183 N4 MES B 401 1.31
REMARK 500 OG SER B 183 C3 MES B 401 2.11
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 ARG A 98 81.26 -154.05
REMARK 500 ASP A 117 -162.10 -166.03
REMARK 500 SER A 183 -117.75 67.44
REMARK 500 PHE A 212 63.03 24.57
REMARK 500 LEU A 232 -63.60 77.86
REMARK 500 ASP B 117 -160.83 -167.82
REMARK 500 PHE B 149 134.13 -38.68
REMARK 500 SER B 183 -119.15 64.39
REMARK 500 PHE B 212 62.32 25.35
REMARK 500 LEU B 232 -69.86 75.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 301 0.13 SIDE CHAIN
REMARK 500 ARG A 311 0.26 SIDE CHAIN
REMARK 500 ARG B 311 0.26 SIDE CHAIN
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 A 936 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 937 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 938 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 939 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 940 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A 941 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 942 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH B 934 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 935 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 936 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B 937 DISTANCE = 6.89 ANGSTROMS
DBREF 9LF7 A 1 336 PDB 9LF7 9LF7 1 336
DBREF 9LF7 B 1 336 PDB 9LF7 9LF7 1 336
SEQRES 1 A 336 MET ARG LEU ALA LYS LEU PRO ALA LEU ALA TYR ARG SER
SEQRES 2 A 336 ALA LYS ASP THR GLY GLU SER MET THR ASP THR PRO TYR
SEQRES 3 A 336 ILE ARG PRO ASP MET LYS ALA PHE LEU GLU MET MET ALA
SEQRES 4 A 336 GLN VAL ASN GLY PRO LYS LEU SER GLU MET SER LEU ASP
SEQRES 5 A 336 GLU ALA ARG ALA SER TYR LEU ALA MET HIS ASN LEU ALA
SEQRES 6 A 336 ASP ARG PRO ALA ARG ALA LEU PRO VAL ILE ARG ASP LEU
SEQRES 7 A 336 SER CYS PRO GLY PRO LYS GLY GLU ILE ALA LEU ARG LEU
SEQRES 8 A 336 TYR ASP PRO ARG GLU SER ARG ALA GLY PRO THR PRO VAL
SEQRES 9 A 336 ILE THR PHE PHE HIS GLY GLY GLY PHE VAL ILE GLY ASP
SEQRES 10 A 336 LEU ASP THR HIS HIS ALA LEU CYS THR GLU ILE ALA ALA
SEQRES 11 A 336 LEU MET ASP LEU PRO LEU VAL ALA VAL HIS TYR ALA ARG
SEQRES 12 A 336 ALA PRO GLU ALA PRO PHE PRO ALA ALA ILE LEU ASP CYS
SEQRES 13 A 336 GLU ALA ALA THR ARG TRP ILE ALA SER SER PRO ALA GLU
SEQRES 14 A 336 LEU GLY LEU THR ALA SER GLY ILE ILE THR ILE GLY ASP
SEQRES 15 A 336 SER ALA GLY GLY ASN ALA THR VAL VAL VAL GLY GLN LEU
SEQRES 16 A 336 LEU ALA ALA SER PRO ALA ALA VAL PRO VAL VAL LEU GLN
SEQRES 17 A 336 VAL PRO ILE PHE PRO LEU VAL ALA ASP ALA VAL SER SER
SEQRES 18 A 336 GLU SER MET ALA ALA PHE SER GLU GLY TYR LEU LEU THR
SEQRES 19 A 336 ALA GLU THR MET ALA PHE PHE ASP ALA ALA TYR GLY ALA
SEQRES 20 A 336 ASP ARG SER ASP PRO ARG GLY PHE PRO ILE LEU GLY ARG
SEQRES 21 A 336 HIS ASP ASN ALA PRO PRO THR ILE VAL VAL THR ALA SER
SEQRES 22 A 336 LEU ASP PRO ILE ARG ASP SER GLY ARG ALA TYR ALA LYS
SEQRES 23 A 336 ALA LEU ILE ASP ALA GLY ARG ASP CYS VAL PHE LEU GLU
SEQRES 24 A 336 MET ARG GLY VAL THR HIS SER PHE THR ASN LEU ARG GLN
SEQRES 25 A 336 MET VAL PRO SER THR GLN ALA ASP LEU GLU ARG VAL ILE
SEQRES 26 A 336 ALA ALA MET GLN PHE MET LEU ALA ASN PRO ALA
SEQRES 1 B 336 MET ARG LEU ALA LYS LEU PRO ALA LEU ALA TYR ARG SER
SEQRES 2 B 336 ALA LYS ASP THR GLY GLU SER MET THR ASP THR PRO TYR
SEQRES 3 B 336 ILE ARG PRO ASP MET LYS ALA PHE LEU GLU MET MET ALA
SEQRES 4 B 336 GLN VAL ASN GLY PRO LYS LEU SER GLU MET SER LEU ASP
SEQRES 5 B 336 GLU ALA ARG ALA SER TYR LEU ALA MET HIS ASN LEU ALA
SEQRES 6 B 336 ASP ARG PRO ALA ARG ALA LEU PRO VAL ILE ARG ASP LEU
SEQRES 7 B 336 SER CYS PRO GLY PRO LYS GLY GLU ILE ALA LEU ARG LEU
SEQRES 8 B 336 TYR ASP PRO ARG GLU SER ARG ALA GLY PRO THR PRO VAL
SEQRES 9 B 336 ILE THR PHE PHE HIS GLY GLY GLY PHE VAL ILE GLY ASP
SEQRES 10 B 336 LEU ASP THR HIS HIS ALA LEU CYS THR GLU ILE ALA ALA
SEQRES 11 B 336 LEU MET ASP LEU PRO LEU VAL ALA VAL HIS TYR ALA ARG
SEQRES 12 B 336 ALA PRO GLU ALA PRO PHE PRO ALA ALA ILE LEU ASP CYS
SEQRES 13 B 336 GLU ALA ALA THR ARG TRP ILE ALA SER SER PRO ALA GLU
SEQRES 14 B 336 LEU GLY LEU THR ALA SER GLY ILE ILE THR ILE GLY ASP
SEQRES 15 B 336 SER ALA GLY GLY ASN ALA THR VAL VAL VAL GLY GLN LEU
SEQRES 16 B 336 LEU ALA ALA SER PRO ALA ALA VAL PRO VAL VAL LEU GLN
SEQRES 17 B 336 VAL PRO ILE PHE PRO LEU VAL ALA ASP ALA VAL SER SER
SEQRES 18 B 336 GLU SER MET ALA ALA PHE SER GLU GLY TYR LEU LEU THR
SEQRES 19 B 336 ALA GLU THR MET ALA PHE PHE ASP ALA ALA TYR GLY ALA
SEQRES 20 B 336 ASP ARG SER ASP PRO ARG GLY PHE PRO ILE LEU GLY ARG
SEQRES 21 B 336 HIS ASP ASN ALA PRO PRO THR ILE VAL VAL THR ALA SER
SEQRES 22 B 336 LEU ASP PRO ILE ARG ASP SER GLY ARG ALA TYR ALA LYS
SEQRES 23 B 336 ALA LEU ILE ASP ALA GLY ARG ASP CYS VAL PHE LEU GLU
SEQRES 24 B 336 MET ARG GLY VAL THR HIS SER PHE THR ASN LEU ARG GLN
SEQRES 25 B 336 MET VAL PRO SER THR GLN ALA ASP LEU GLU ARG VAL ILE
SEQRES 26 B 336 ALA ALA MET GLN PHE MET LEU ALA ASN PRO ALA
HET MES A 401 12
HET MES B 401 12
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 MES 2(C6 H13 N O4 S)
FORMUL 5 HOH *879(H2 O)
HELIX 1 AA1 ARG A 28 ASN A 42 1 15
HELIX 2 AA2 LYS A 45 MET A 49 5 5
HELIX 3 AA3 SER A 50 ASP A 66 1 17
HELIX 4 AA4 HIS A 121 ASP A 133 1 13
HELIX 5 AA5 PRO A 150 SER A 165 1 16
HELIX 6 AA6 SER A 183 SER A 199 1 17
HELIX 7 AA7 SER A 221 SER A 228 1 8
HELIX 8 AA8 THR A 234 GLY A 246 1 13
HELIX 9 AA9 PHE A 255 GLY A 259 5 5
HELIX 10 AB1 ILE A 277 ALA A 291 1 15
HELIX 11 AB2 SER A 306 LEU A 310 5 5
HELIX 12 AB3 PRO A 315 ASN A 334 1 20
HELIX 13 AB4 ARG B 28 VAL B 41 1 14
HELIX 14 AB5 LYS B 45 MET B 49 5 5
HELIX 15 AB6 SER B 50 ASP B 66 1 17
HELIX 16 AB7 HIS B 121 ASP B 133 1 13
HELIX 17 AB8 PRO B 150 SER B 165 1 16
HELIX 18 AB9 SER B 183 SER B 199 1 17
HELIX 19 AC1 SER B 221 SER B 228 1 8
HELIX 20 AC2 THR B 234 GLY B 246 1 13
HELIX 21 AC3 PHE B 255 GLY B 259 5 5
HELIX 22 AC4 ILE B 277 ALA B 291 1 15
HELIX 23 AC5 SER B 306 LEU B 310 5 5
HELIX 24 AC6 PRO B 315 ASN B 334 1 20
SHEET 1 AA1 6 VAL A 74 GLY A 82 0
SHEET 2 AA1 6 GLY A 85 ASP A 93 -1 O LEU A 89 N LEU A 78
SHEET 3 AA1 6 LEU A 136 HIS A 140 -1 O LEU A 136 N TYR A 92
SHEET 4 AA1 6 PRO A 101 PHE A 108 1 N ILE A 105 O VAL A 137
SHEET 5 AA1 6 THR A 173 ASP A 182 1 O ILE A 178 N THR A 106
SHEET 6 AA1 6 VAL A 205 ILE A 211 1 O ILE A 211 N GLY A 181
SHEET 1 AA2 4 THR A 267 ALA A 272 0
SHEET 2 AA2 4 CYS A 295 MET A 300 1 O MET A 300 N THR A 271
SHEET 3 AA2 4 CYS B 295 MET B 300 -1 O CYS B 295 N PHE A 297
SHEET 4 AA2 4 THR B 267 ALA B 272 1 N THR B 271 O MET B 300
SHEET 1 AA3 6 VAL B 74 GLY B 82 0
SHEET 2 AA3 6 GLY B 85 ASP B 93 -1 O LEU B 89 N LEU B 78
SHEET 3 AA3 6 LEU B 136 HIS B 140 -1 O LEU B 136 N TYR B 92
SHEET 4 AA3 6 PRO B 101 PHE B 108 1 N ILE B 105 O VAL B 137
SHEET 5 AA3 6 THR B 173 ASP B 182 1 O ILE B 178 N THR B 106
SHEET 6 AA3 6 VAL B 205 ILE B 211 1 O ILE B 211 N GLY B 181
CISPEP 1 ALA A 144 PRO A 145 0 -1.09
CISPEP 2 PHE A 149 PRO A 150 0 4.59
CISPEP 3 ALA B 144 PRO B 145 0 2.03
CISPEP 4 PHE B 149 PRO B 150 0 1.82
CRYST1 68.657 89.603 139.592 90.00 90.00 90.00 P 21 21 21 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 0.014565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007164 0.00000
TER 2330 ALA A 336
TER 4655 ALA B 336
MASTER 326 0 2 24 16 0 0 6 5556 2 24 52
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