| content |
HEADER HYDROLASE 18-DEC-23 8XHO
TITLE DEEP SEA BACTERIAL PET PLASTIC HYDROLASE MTCUT WITH MUTATION S178C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PET PLASTIC HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MARINACTINOSPORA THERMOTOLERANS DSM 45154;
SOURCE 3 ORGANISM_TAXID: 1122192;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YANG
REVDAT 1 03-APR-24 8XHO 0
JRNL AUTH J.YANG
JRNL TITL DEEP SEA BACTERIAL PET PLASTIC HYDROLASE MTCUT WITH MUTATION
JRNL TITL 2 S178C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 16751
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1863
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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) : 0.231
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.24000
REMARK 3 B22 (A**2) : 2.28000
REMARK 3 B33 (A**2) : -1.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 8XHO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1300043315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-22
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R 200K-A
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 19.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4000
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) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.5; 40% V/V PEG 500 MME;
REMARK 280 20 % W/V PEG 20000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 44.07400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.78000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.07400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.78000
REMARK 290 SMTRY3 4 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 TOTAL BURIED SURFACE AREA: 80 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 TOTAL BURIED SURFACE AREA: 160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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 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 532 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 582 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 LEU A 312
REMARK 465 GLU A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 LEU B 312
REMARK 465 GLU B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
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 B 544 O HOH B 571 1.84
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 OG SER B 255 OG SER B 255 2565 1.88
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 THR A 111 -3.02 74.07
REMARK 500 CYS A 178 -125.67 60.66
REMARK 500 THR A 201 56.65 34.44
REMARK 500 ALA A 227 70.74 -115.18
REMARK 500 HIS A 232 -82.22 -123.35
REMARK 500 THR B 111 -3.00 74.98
REMARK 500 CYS B 178 -125.96 61.28
REMARK 500 THR B 201 56.98 33.69
REMARK 500 ALA B 227 70.11 -113.13
REMARK 500 HIS B 232 -81.12 -123.28
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 146 0.10 SIDE CHAIN
REMARK 500 ARG A 230 0.08 SIDE CHAIN
REMARK 500 ARG B 146 0.09 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 606 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH A 607 DISTANCE = 7.67 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 245 OE1
REMARK 620 2 GLU A 245 OE2 45.7
REMARK 620 3 SER A 306 O 67.1 111.7
REMARK 620 4 PRO A 308 O 87.2 87.0 77.6
REMARK 620 5 HOH A 574 O 114.6 69.0 163.2 85.7
REMARK 620 6 HOH A 596 O 71.3 73.0 99.6 157.3 96.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 72 OD1
REMARK 620 2 THR B 73 O 96.7
REMARK 620 3 HOH B 511 O 86.1 150.1
REMARK 620 4 HOH B 585 O 112.1 78.6 72.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 245 OE1
REMARK 620 2 GLU B 245 OE2 45.9
REMARK 620 3 SER B 306 O 66.4 110.0
REMARK 620 4 PRO B 308 O 83.4 82.6 73.0
REMARK 620 5 HOH B 609 O 79.2 83.1 102.6 162.3
REMARK 620 N 1 2 3 4
DBREF 8XHO A 50 319 PDB 8XHO 8XHO 50 319
DBREF 8XHO B 50 319 PDB 8XHO 8XHO 50 319
SEQRES 1 A 270 SER ASN PRO TYR GLU ARG GLY PRO ALA PRO THR GLU SER
SEQRES 2 A 270 SER VAL THR ALA VAL ARG GLY TYR PHE ASP THR ASP THR
SEQRES 3 A 270 ASP THR VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY
SEQRES 4 A 270 THR ILE TYR TYR PRO THR ASP THR SER GLU GLY THR PHE
SEQRES 5 A 270 GLY GLY VAL VAL ILE ALA PRO GLY TYR THR ALA SER GLN
SEQRES 6 A 270 SER SER MET ALA TRP MET GLY HIS ARG ILE ALA SER GLN
SEQRES 7 A 270 GLY PHE VAL VAL PHE THR ILE ASP THR ILE THR ARG TYR
SEQRES 8 A 270 ASP GLN PRO ASP SER ARG GLY ARG GLN ILE GLU ALA ALA
SEQRES 9 A 270 LEU ASP TYR LEU VAL GLU ASP SER ASP VAL ALA ASP ARG
SEQRES 10 A 270 VAL ASP GLY ASN ARG LEU ALA VAL MET GLY HIS CYS MET
SEQRES 11 A 270 GLY GLY GLY GLY THR LEU ALA ALA ALA GLU ASN ARG PRO
SEQRES 12 A 270 GLU LEU ARG ALA ALA ILE PRO LEU THR PRO TRP HIS LEU
SEQRES 13 A 270 GLN LYS ASN TRP SER ASP VAL GLU VAL PRO THR MET ILE
SEQRES 14 A 270 ILE GLY ALA GLU ASN ASP THR VAL ALA SER VAL ARG THR
SEQRES 15 A 270 HIS SER ILE PRO PHE TYR GLU SER LEU ASP GLU ASP LEU
SEQRES 16 A 270 GLU ARG ALA TYR LEU GLU LEU ASP GLY ALA SER HIS PHE
SEQRES 17 A 270 ALA PRO ASN ILE SER ASN THR VAL ILE ALA LYS TYR SER
SEQRES 18 A 270 ILE SER TRP LEU LYS ARG PHE VAL ASP GLU ASP GLU ARG
SEQRES 19 A 270 TYR GLU GLN PHE LEU CYS PRO PRO PRO ASP THR GLY LEU
SEQRES 20 A 270 PHE SER ASP PHE SER ASP TYR ARG ASP SER CYS PRO HIS
SEQRES 21 A 270 THR THR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 SER ASN PRO TYR GLU ARG GLY PRO ALA PRO THR GLU SER
SEQRES 2 B 270 SER VAL THR ALA VAL ARG GLY TYR PHE ASP THR ASP THR
SEQRES 3 B 270 ASP THR VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY
SEQRES 4 B 270 THR ILE TYR TYR PRO THR ASP THR SER GLU GLY THR PHE
SEQRES 5 B 270 GLY GLY VAL VAL ILE ALA PRO GLY TYR THR ALA SER GLN
SEQRES 6 B 270 SER SER MET ALA TRP MET GLY HIS ARG ILE ALA SER GLN
SEQRES 7 B 270 GLY PHE VAL VAL PHE THR ILE ASP THR ILE THR ARG TYR
SEQRES 8 B 270 ASP GLN PRO ASP SER ARG GLY ARG GLN ILE GLU ALA ALA
SEQRES 9 B 270 LEU ASP TYR LEU VAL GLU ASP SER ASP VAL ALA ASP ARG
SEQRES 10 B 270 VAL ASP GLY ASN ARG LEU ALA VAL MET GLY HIS CYS MET
SEQRES 11 B 270 GLY GLY GLY GLY THR LEU ALA ALA ALA GLU ASN ARG PRO
SEQRES 12 B 270 GLU LEU ARG ALA ALA ILE PRO LEU THR PRO TRP HIS LEU
SEQRES 13 B 270 GLN LYS ASN TRP SER ASP VAL GLU VAL PRO THR MET ILE
SEQRES 14 B 270 ILE GLY ALA GLU ASN ASP THR VAL ALA SER VAL ARG THR
SEQRES 15 B 270 HIS SER ILE PRO PHE TYR GLU SER LEU ASP GLU ASP LEU
SEQRES 16 B 270 GLU ARG ALA TYR LEU GLU LEU ASP GLY ALA SER HIS PHE
SEQRES 17 B 270 ALA PRO ASN ILE SER ASN THR VAL ILE ALA LYS TYR SER
SEQRES 18 B 270 ILE SER TRP LEU LYS ARG PHE VAL ASP GLU ASP GLU ARG
SEQRES 19 B 270 TYR GLU GLN PHE LEU CYS PRO PRO PRO ASP THR GLY LEU
SEQRES 20 B 270 PHE SER ASP PHE SER ASP TYR ARG ASP SER CYS PRO HIS
SEQRES 21 B 270 THR THR LEU GLU HIS HIS HIS HIS HIS HIS
HET CA A 401 1
HET CA B 401 1
HET CA B 402 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 3(CA 2+)
FORMUL 6 HOH *225(H2 O)
HELIX 1 AA1 THR A 60 THR A 65 1 6
HELIX 2 AA2 SER A 113 ALA A 118 5 6
HELIX 3 AA3 TRP A 119 SER A 126 1 8
HELIX 4 AA4 GLN A 142 ASP A 160 1 19
HELIX 5 AA5 VAL A 163 ASP A 165 5 3
HELIX 6 AA6 CYS A 178 ARG A 191 1 14
HELIX 7 AA7 HIS A 232 LEU A 240 1 9
HELIX 8 AA8 PHE A 257 ILE A 261 5 5
HELIX 9 AA9 ASN A 263 ASP A 279 1 17
HELIX 10 AB1 ASP A 281 LEU A 288 5 8
HELIX 11 AB2 THR B 60 THR B 65 1 6
HELIX 12 AB3 SER B 113 MET B 117 5 5
HELIX 13 AB4 ALA B 118 SER B 126 1 9
HELIX 14 AB5 GLN B 142 ASP B 160 1 19
HELIX 15 AB6 VAL B 163 ASP B 165 5 3
HELIX 16 AB7 CYS B 178 ARG B 191 1 14
HELIX 17 AB8 HIS B 232 LEU B 240 1 9
HELIX 18 AB9 PHE B 257 ILE B 261 5 5
HELIX 19 AC1 ASN B 263 ASP B 279 1 17
HELIX 20 AC2 ASP B 281 LEU B 288 5 8
SHEET 1 AA1 6 THR A 73 VAL A 78 0
SHEET 2 AA1 6 GLY A 88 PRO A 93 -1 O GLY A 88 N VAL A 78
SHEET 3 AA1 6 VAL A 130 ILE A 134 -1 O VAL A 131 N TYR A 91
SHEET 4 AA1 6 PHE A 101 ALA A 107 1 N VAL A 104 O PHE A 132
SHEET 5 AA1 6 VAL A 167 HIS A 177 1 O MET A 175 N VAL A 105
SHEET 6 AA1 6 ALA A 196 LEU A 200 1 O LEU A 200 N GLY A 176
SHEET 1 AA2 3 THR A 216 ALA A 221 0
SHEET 2 AA2 3 ARG A 246 LEU A 251 1 O LEU A 249 N ILE A 218
SHEET 3 AA2 3 PHE A 300 ARG A 304 -1 O SER A 301 N GLU A 250
SHEET 1 AA3 6 THR B 73 VAL B 78 0
SHEET 2 AA3 6 GLY B 88 PRO B 93 -1 O GLY B 88 N VAL B 78
SHEET 3 AA3 6 VAL B 130 ILE B 134 -1 O VAL B 131 N TYR B 91
SHEET 4 AA3 6 PHE B 101 ALA B 107 1 N VAL B 104 O PHE B 132
SHEET 5 AA3 6 VAL B 167 HIS B 177 1 O MET B 175 N VAL B 105
SHEET 6 AA3 6 ALA B 196 LEU B 200 1 O LEU B 200 N GLY B 176
SHEET 1 AA4 3 THR B 216 ALA B 221 0
SHEET 2 AA4 3 ARG B 246 LEU B 251 1 O LEU B 249 N ILE B 218
SHEET 3 AA4 3 PHE B 300 ARG B 304 -1 O SER B 301 N GLU B 250
SSBOND 1 CYS A 289 CYS A 307 1555 1555 2.36
SSBOND 2 CYS B 289 CYS B 307 1555 1555 2.34
LINK OE1 GLU A 245 CA CA A 401 1555 1555 2.94
LINK OE2 GLU A 245 CA CA A 401 1555 1555 2.67
LINK O SER A 306 CA CA A 401 1555 1555 2.38
LINK O PRO A 308 CA CA A 401 1555 1555 2.22
LINK CA CA A 401 O HOH A 574 1555 1555 2.41
LINK CA CA A 401 O HOH A 596 1555 1555 2.78
LINK OD1 ASP B 72 CA CA B 401 1555 1555 2.45
LINK O THR B 73 CA CA B 401 1555 1555 2.40
LINK OE1 GLU B 245 CA CA B 402 1555 1555 2.92
LINK OE2 GLU B 245 CA CA B 402 1555 1555 2.71
LINK O SER B 306 CA CA B 402 1555 1555 2.45
LINK O PRO B 308 CA CA B 402 1555 1555 2.42
LINK CA CA B 401 O HOH B 511 1555 4555 2.27
LINK CA CA B 401 O HOH B 585 1555 1555 2.10
LINK CA CA B 402 O HOH B 609 1555 1555 2.37
CISPEP 1 CYS A 289 PRO A 290 0 1.47
CISPEP 2 CYS A 307 PRO A 308 0 -7.51
CISPEP 3 CYS B 289 PRO B 290 0 -4.50
CISPEP 4 CYS B 307 PRO B 308 0 -6.59
CRYST1 88.148 85.560 69.520 90.00 90.00 90.00 P 21 21 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 0.011345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011688 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014384 0.00000
TER 2023 THR A 311
TER 4046 THR B 311
MASTER 359 0 3 20 18 0 0 6 4272 2 23 42
END |