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HEADER HYDROLASE 07-JUN-13 4L3W
TITLE CRYSTAL STRUCTURE OF LIPASE FROM RHIZOPUS MICROSPORUS VAR. CHINENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 94-389;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOPUS MICROSPORUS VAR. CHINENSIS;
SOURCE 3 ORGANISM_COMMON: BREAD MOLD;
SOURCE 4 ORGANISM_TAXID: 4843;
SOURCE 5 STRAIN: CCTCC M201021;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9K
KEYWDS ESTERASES FAMILY 3, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHANG,X.W.YU,Y.XU,C.H.HUANG,R.T.GUO
REVDAT 1 10-DEC-14 4L3W 0
JRNL AUTH M.ZHANG,X.W.YU,Y.XU,C.H.HUANG,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE OF LIPASE FROM RHIZOPUS MICROSPORUS VAR.
JRNL TITL 2 CHINENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 27593
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1346
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 116
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2062
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 61
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.67700
REMARK 3 B22 (A**2) : -11.67700
REMARK 3 B33 (A**2) : 23.35400
REMARK 3 B12 (A**2) : -5.44500
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.187 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.733 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.177 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.992 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 54.27
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PEG2.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4L3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB080148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : 30238
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.7000
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 : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.300
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 (%): 63.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS PH 8.0, 150MM NACL, 0.25M
REMARK 280 (NH4)2SO4, 25% PEG 4000 , VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.71700
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.43400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 67.43400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.71700
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 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 ASP A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 VAL A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 7
REMARK 465 MET A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 ASP A 11
REMARK 465 LEU A 12
REMARK 465 PRO A 13
REMARK 465 GLU A 14
REMARK 465 ASN A 15
REMARK 465 PRO A 16
REMARK 465 PRO A 17
REMARK 465 PRO A 18
REMARK 465 ILE A 19
REMARK 465 PRO A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 ALA A 25
REMARK 465 PRO A 26
REMARK 465 SER A 27
REMARK 465 SER A 28
REMARK 465 ASP A 29
REMARK 465 SER A 30
REMARK 465 GLY A 31
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE A 252 C ILE A 252 O -0.163
REMARK 500 LYS A 253 C LYS A 253 O -0.224
REMARK 500 GLU A 254 CD GLU A 254 OE1 -0.159
REMARK 500 GLU A 254 CD GLU A 254 OE2 -0.173
REMARK 500 ASP A 255 CA ASP A 255 CB -0.133
REMARK 500 ASP A 255 CG ASP A 255 OD2 -0.164
REMARK 500 ASP A 255 C ASP A 255 O -0.145
REMARK 500 ALA A 257 C ALA A 257 O -0.148
REMARK 500 ASP A 258 CG ASP A 258 OD1 -0.180
REMARK 500 ASP A 258 CG ASP A 258 OD2 -0.168
REMARK 500 ASP A 258 C ASP A 258 O -0.169
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 256 C - N - CD ANGL. DEV. = 17.3 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 TRP A 65 75.81 -114.40
REMARK 500 ASP A 66 19.25 -143.18
REMARK 500 SER A 172 -138.03 52.49
REMARK 500 LYS A 229 -110.27 39.40
REMARK 500 PRO A 234 0.86 -68.00
REMARK 500 CYS A 271 -132.34 -100.80
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 494 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH A 531 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 557 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH A 563 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 567 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A 582 DISTANCE = 8.31 ANGSTROMS
REMARK 525 HOH A 584 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A 585 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 587 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH A 601 DISTANCE = 7.80 ANGSTROMS
REMARK 525 HOH A 602 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 608 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH A 609 DISTANCE = 8.44 ANGSTROMS
REMARK 525 HOH A 612 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH A 613 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH A 614 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A 626 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH A 627 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH A 628 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH A 631 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A 635 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH A 637 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH A 638 DISTANCE = 10.04 ANGSTROMS
REMARK 525 HOH A 643 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH A 656 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH A 657 DISTANCE = 8.58 ANGSTROMS
REMARK 525 HOH A 666 DISTANCE = 9.93 ANGSTROMS
REMARK 525 HOH A 671 DISTANCE = 8.53 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 9.02 ANGSTROMS
REMARK 525 HOH A 676 DISTANCE = 8.34 ANGSTROMS
REMARK 525 HOH A 679 DISTANCE = 6.98 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 319
DBREF 4L3W A 1 296 UNP A3FM73 A3FM73_RHICH 94 389
SEQRES 1 A 296 ASP THR GLU THR VAL GLY GLY MET THR LEU ASP LEU PRO
SEQRES 2 A 296 GLU ASN PRO PRO PRO ILE PRO ALA THR SER THR ALA PRO
SEQRES 3 A 296 SER SER ASP SER GLY GLU VAL VAL THR ALA THR ALA ALA
SEQRES 4 A 296 GLN ILE LYS GLU LEU THR ASN TYR ALA GLY VAL ALA ALA
SEQRES 5 A 296 THR ALA TYR CYS ARG SER VAL VAL PRO GLY THR LYS TRP
SEQRES 6 A 296 ASP CYS LYS GLN CYS LEU LYS TYR VAL PRO ASP GLY LYS
SEQRES 7 A 296 LEU ILE LYS THR PHE THR SER LEU LEU THR ASP THR ASN
SEQRES 8 A 296 GLY PHE ILE LEU ARG SER ASP ALA GLN LYS THR ILE TYR
SEQRES 9 A 296 VAL THR PHE ARG GLY THR ASN SER PHE ARG SER ALA ILE
SEQRES 10 A 296 THR ASP MET VAL PHE THR PHE THR ASP TYR SER PRO VAL
SEQRES 11 A 296 LYS GLY ALA LYS VAL HIS ALA GLY PHE LEU SER SER TYR
SEQRES 12 A 296 ASN GLN VAL VAL LYS ASP TYR PHE PRO VAL VAL GLN ASP
SEQRES 13 A 296 GLN LEU THR ALA TYR PRO ASP TYR LYS VAL ILE VAL THR
SEQRES 14 A 296 GLY HIS SER LEU GLY GLY ALA GLN ALA LEU LEU ALA GLY
SEQRES 15 A 296 MET ASP LEU TYR GLN ARG GLU LYS ARG LEU SER PRO LYS
SEQRES 16 A 296 ASN LEU SER ILE TYR THR VAL GLY CYS PRO ARG VAL GLY
SEQRES 17 A 296 ASN ASN ALA PHE ALA TYR TYR VAL ASP SER THR GLY ILE
SEQRES 18 A 296 PRO PHE HIS ARG THR VAL HIS LYS ARG ASP ILE VAL PRO
SEQRES 19 A 296 HIS VAL PRO PRO GLN ALA PHE GLY TYR LEU HIS PRO GLY
SEQRES 20 A 296 VAL GLU SER TRP ILE LYS GLU ASP PRO ALA ASP VAL GLN
SEQRES 21 A 296 ILE CYS THR SER ASN ILE GLU THR LYS GLN CYS SER ASN
SEQRES 22 A 296 SER ILE VAL PRO PHE THR SER ILE ALA ASP HIS LEU THR
SEQRES 23 A 296 TYR PHE GLY ILE ASN GLU GLY SER CYS LEU
HET EDO A 301 3
HET EDO A 302 3
HET EDO A 303 3
HET EDO A 304 3
HET EDO A 305 3
HET EDO A 306 3
HET EDO A 307 3
HET EDO A 308 3
HET EDO A 309 3
HET EDO A 310 3
HET EDO A 311 3
HET EDO A 312 3
HET EDO A 313 3
HET EDO A 314 3
HET EDO A 315 3
HET EDO A 316 3
HET EDO A 317 3
HET SO4 A 318 5
HET SO4 A 319 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 17(C2 H6 O2)
FORMUL 19 SO4 2(O4 S 2-)
FORMUL 21 HOH *323(H2 O)
HELIX 1 1 THR A 37 THR A 53 1 17
HELIX 2 2 ALA A 54 CYS A 56 5 3
HELIX 3 3 CYS A 67 VAL A 74 1 8
HELIX 4 4 LEU A 86 ASP A 89 5 4
HELIX 5 5 SER A 112 ASP A 119 1 8
HELIX 6 6 ALA A 137 TYR A 161 1 25
HELIX 7 7 SER A 172 GLU A 189 1 18
HELIX 8 8 ASN A 209 GLY A 220 1 12
HELIX 9 9 ILE A 232 VAL A 236 5 5
HELIX 10 10 PRO A 238 GLY A 242 5 5
HELIX 11 11 CYS A 271 VAL A 276 5 6
HELIX 12 12 ILE A 281 HIS A 284 5 4
SHEET 1 A 9 VAL A 33 THR A 35 0
SHEET 2 A 9 ASP A 258 CYS A 262 -1 O ILE A 261 N VAL A 34
SHEET 3 A 9 VAL A 248 GLU A 254 -1 N TRP A 251 O GLN A 260
SHEET 4 A 9 PHE A 223 HIS A 228 1 N ARG A 225 O VAL A 248
SHEET 5 A 9 LEU A 197 VAL A 202 1 N ILE A 199 O HIS A 224
SHEET 6 A 9 LYS A 165 HIS A 171 1 N VAL A 168 O TYR A 200
SHEET 7 A 9 THR A 102 ARG A 108 1 N VAL A 105 O ILE A 167
SHEET 8 A 9 THR A 90 SER A 97 -1 N LEU A 95 O TYR A 104
SHEET 9 A 9 LYS A 78 SER A 85 -1 N SER A 85 O THR A 90
SHEET 1 B 2 PHE A 124 ASP A 126 0
SHEET 2 B 2 LYS A 134 HIS A 136 -1 O VAL A 135 N THR A 125
SHEET 1 C 2 THR A 286 TYR A 287 0
SHEET 2 C 2 ILE A 290 ASN A 291 -1 O ILE A 290 N TYR A 287
SSBOND 1 CYS A 56 CYS A 295 1555 1555 2.04
SSBOND 2 CYS A 67 CYS A 70 1555 1555 2.04
SSBOND 3 CYS A 262 CYS A 271 1555 1555 2.02
LINK C2 EDO A 301 O1 EDO A 302 1555 1555 1.51
LINK C2 EDO A 302 O1 EDO A 303 1555 1555 1.52
LINK C2 EDO A 303 O1 EDO A 304 1555 1555 1.52
LINK C2 EDO A 304 O1 EDO A 305 1555 1555 1.51
LINK C2 EDO A 305 O1 EDO A 306 1555 1555 1.52
LINK C2 EDO A 306 O1 EDO A 307 1555 1555 1.52
LINK C2 EDO A 307 O1 EDO A 308 1555 1555 1.52
LINK C2 EDO A 308 O1 EDO A 309 1555 1555 1.52
LINK C2 EDO A 309 O1 EDO A 310 1555 1555 1.54
LINK C2 EDO A 310 O1 EDO A 311 1555 1555 1.56
LINK C2 EDO A 311 O1 EDO A 312 1555 1555 1.52
LINK C2 EDO A 312 O1 EDO A 313 1555 1555 1.50
LINK C2 EDO A 313 O1 EDO A 314 1555 1555 1.51
LINK C2 EDO A 314 O1 EDO A 315 1555 1555 1.50
LINK C2 EDO A 315 O1 EDO A 316 1555 1555 1.53
LINK C2 EDO A 316 O1 EDO A 317 1555 1555 1.54
CISPEP 1 VAL A 60 PRO A 61 0 0.64
CISPEP 2 VAL A 236 PRO A 237 0 -0.62
CISPEP 3 ASP A 255 PRO A 256 0 1.97
CISPEP 4 VAL A 276 PRO A 277 0 0.13
SITE 1 AC1 2 EDO A 302 HOH A 701
SITE 1 AC2 5 ASP A 156 LYS A 253 EDO A 301 EDO A 303
SITE 2 AC2 5 HOH A 574
SITE 1 AC3 3 ASP A 156 EDO A 302 EDO A 304
SITE 1 AC4 3 EDO A 303 EDO A 305 HOH A 499
SITE 1 AC5 5 ARG A 230 EDO A 304 EDO A 306 HOH A 421
SITE 2 AC5 5 HOH A 499
SITE 1 AC6 4 EDO A 305 EDO A 307 HOH A 421 HOH A 498
SITE 1 AC7 3 EDO A 306 EDO A 308 HOH A 411
SITE 1 AC8 3 EDO A 307 EDO A 309 HOH A 411
SITE 1 AC9 3 EDO A 308 EDO A 310 HOH A 503
SITE 1 BC1 4 EDO A 309 EDO A 311 HOH A 503 HOH A 515
SITE 1 BC2 3 EDO A 310 EDO A 312 HOH A 449
SITE 1 BC3 4 THR A 279 EDO A 311 EDO A 313 HOH A 458
SITE 1 BC4 5 PRO A 277 THR A 279 EDO A 312 EDO A 314
SITE 2 BC4 5 HOH A 458
SITE 1 BC5 3 EDO A 313 EDO A 315 HOH A 470
SITE 1 BC6 3 EDO A 314 EDO A 316 HOH A 430
SITE 1 BC7 4 EDO A 315 EDO A 317 HOH A 430 HOH A 504
SITE 1 BC8 2 EDO A 316 HOH A 580
SITE 1 BC9 3 GLN A 40 GLU A 43 HIS A 224
SITE 1 CC1 7 HIS A 228 LYS A 229 ASP A 255 THR A 286
SITE 2 CC1 7 PHE A 288 GLY A 289 HOH A 704
CRYST1 86.225 86.225 101.151 90.00 90.00 120.00 P 31 2 1 6
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 0.011598 0.006696 0.000000 0.00000
SCALE2 0.000000 0.013392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009886 0.00000
TER 2063 LEU A 296
MASTER 456 0 19 12 13 0 23 6 2446 1 67 23
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