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HEADER HYDROLASE 28-OCT-20 7AT0
TITLE STRUCTURE OF THE HORMONE-SENSITIVE LIPASE LIKE ESTD11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTD11;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22
KEYWDS ESTERASE HORMONE-SENSITIVE LIPASE METAGENOME LIBRARY CRYSTAL
KEYWDS 2 STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MIGUEL-RUANO,I.RIVERA,J.A.HERMOSO
REVDAT 1 03-MAR-21 7AT0 0
JRNL AUTH V.MIGUEL-RUANO,I.RIVERA,J.RAJKOVIC,K.KNAPIK,A.TORRADO,
JRNL AUTH 2 J.M.OTERO,E.BENEVENTI,M.BECERRA,M.SANCHEZ-COSTA,A.HIDALGO,
JRNL AUTH 3 J.BERENGUER,M.I.GONZALEZ-SISO,J.CRUCES,M.L.RUA,J.A.HERMOSO
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 THERMOPHILIC ESTERASE ESTD11 PROVIDE CATALYTIC INSIGHTS FOR
JRNL TITL 3 THE HSL FAMILY
JRNL REF COMPUT STRUCT BIOTECHNOL J 2021
JRNL REFN ESSN 2001-0370
JRNL DOI 10.1016/J.CSBJ.2021.01.047
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 165932
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.124
REMARK 3 R VALUE (WORKING SET) : 0.123
REMARK 3 FREE R VALUE : 0.150
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8727
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12147
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 636
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4486
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 591
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.33000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.033
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.024
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.978
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5133 ; 0.012 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): 4892 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7061 ; 1.581 ; 1.890
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11311 ; 1.264 ; 2.931
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 696 ; 5.548 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;31.599 ;22.701
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 838 ;12.432 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;21.050 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 798 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6017 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1052 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2646 ; 1.591 ; 1.335
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2647 ; 1.603 ; 1.337
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3388 ; 1.990 ; 2.012
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3389 ; 2.000 ; 2.013
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2487 ; 2.905 ; 1.704
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2476 ; 2.794 ; 1.690
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3674 ; 3.364 ; 2.422
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5988 ; 3.700 ;18.285
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5828 ; 3.332 ;17.513
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 10025 ; 2.541 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.30
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7AT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292112029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 174770
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.40
REMARK 200 R MERGE FOR SHELL (I) : 0.99400
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: 4XVC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3,2M SODIUM FORMATE + 0,1M CITRATE PH
REMARK 280 5., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 23.94150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.49450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.08400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.49450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.94150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.08400
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 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 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 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 GLN B 296
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 A 734 O HOH A 832 1.87
REMARK 500 O HOH B 1189 O HOH B 1250 1.91
REMARK 500 O GLY B 161 O HOH B 1001 1.92
REMARK 500 O HOH B 1003 O HOH B 1191 1.94
REMARK 500 O HOH B 1258 O HOH B 1289 2.05
REMARK 500 O HOH B 1244 O HOH B 1282 2.08
REMARK 500 O HOH A 697 O HOH B 1006 2.12
REMARK 500 O ALA B 189 O HOH B 1002 2.12
REMARK 500 O HOH A 611 O HOH A 830 2.14
REMARK 500 O HOH B 1202 O HOH B 1260 2.17
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 O HOH A 809 O HOH B 1270 4555 1.17
REMARK 500 O HOH B 1142 O HOH B 1211 3555 1.83
REMARK 500 N ALA B 189 O HOH B 1211 3555 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 158 CZ ARG A 158 NH2 0.091
REMARK 500 GLN A 296 C GLN A 296 OXT 0.161
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 ARG A 158 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 158 NE - CZ - NH2 ANGL. DEV. = -3.4 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 SER A 144 -124.14 62.95
REMARK 500 ALA A 237 54.41 -95.77
REMARK 500 ASP A 265 -2.14 71.95
REMARK 500 ASP A 265 -2.14 72.56
REMARK 500 SER B 144 -123.45 61.75
REMARK 500 VAL B 190 -52.17 -124.69
REMARK 500 ASP B 191 111.34 -31.02
REMARK 500 ALA B 237 54.47 -98.53
REMARK 500 ASP B 265 -1.05 72.75
REMARK 500 ASP B 265 -1.05 70.34
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 901 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 902 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH B1288 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B1289 DISTANCE = 6.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 904
DBREF 7AT0 A 2 296 PDB 7AT0 7AT0 2 296
DBREF 7AT0 B 2 296 PDB 7AT0 7AT0 2 296
SEQRES 1 A 295 ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU ARG
SEQRES 2 A 295 SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN MET
SEQRES 3 A 295 ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO LEU
SEQRES 4 A 295 PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY GLY
SEQRES 5 A 295 VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP PRO
SEQRES 6 A 295 ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR VAL
SEQRES 7 A 295 ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN ARG
SEQRES 8 A 295 ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE ASP
SEQRES 9 A 295 TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA VAL
SEQRES 10 A 295 GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU THR
SEQRES 11 A 295 GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP SER
SEQRES 12 A 295 ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA LEU
SEQRES 13 A 295 ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL CYS
SEQRES 14 A 295 LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU SER
SEQRES 15 A 295 MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN ARG
SEQRES 16 A 295 GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA GLY
SEQRES 17 A 295 GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR ALA
SEQRES 18 A 295 ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL GLY
SEQRES 19 A 295 THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU ALA
SEQRES 20 A 295 GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU GLU
SEQRES 21 A 295 PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE ALA
SEQRES 22 A 295 ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG ILE
SEQRES 23 A 295 GLY GLU PHE LEU ARG GLN HIS TRP GLN
SEQRES 1 B 295 ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU ARG
SEQRES 2 B 295 SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN MET
SEQRES 3 B 295 ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO LEU
SEQRES 4 B 295 PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY GLY
SEQRES 5 B 295 VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP PRO
SEQRES 6 B 295 ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR VAL
SEQRES 7 B 295 ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN ARG
SEQRES 8 B 295 ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE ASP
SEQRES 9 B 295 TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA VAL
SEQRES 10 B 295 GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU THR
SEQRES 11 B 295 GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP SER
SEQRES 12 B 295 ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA LEU
SEQRES 13 B 295 ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL CYS
SEQRES 14 B 295 LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU SER
SEQRES 15 B 295 MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN ARG
SEQRES 16 B 295 GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA GLY
SEQRES 17 B 295 GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR ALA
SEQRES 18 B 295 ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL GLY
SEQRES 19 B 295 THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU ALA
SEQRES 20 B 295 GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU GLU
SEQRES 21 B 295 PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE ALA
SEQRES 22 B 295 ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG ILE
SEQRES 23 B 295 GLY GLU PHE LEU ARG GLN HIS TRP GLN
HET FMT A 501 3
HET FMT A 502 3
HET FMT A 503 3
HET IPH A 504 7
HET FMT A 505 3
HET FMT A 506 3
HET FMT B 901 3
HET FMT B 902 3
HET FMT B 903 3
HET FMT B 904 3
HETNAM FMT FORMIC ACID
HETNAM IPH PHENOL
FORMUL 3 FMT 9(C H2 O2)
FORMUL 6 IPH C6 H6 O
FORMUL 13 HOH *591(H2 O)
HELIX 1 AA1 GLU A 4 ARG A 17 1 14
HELIX 2 AA2 PRO A 18 GLU A 21 5 4
HELIX 3 AA3 THR A 23 GLN A 36 1 14
HELIX 4 AA4 SER A 82 ARG A 98 1 17
HELIX 5 AA5 PRO A 115 THR A 131 1 17
HELIX 6 AA6 ASP A 134 LYS A 136 5 3
HELIX 7 AA7 SER A 144 ALA A 160 1 17
HELIX 8 AA8 GLY A 181 LYS A 187 1 7
HELIX 9 AA9 GLN A 195 ALA A 208 1 14
HELIX 10 AB1 ALA A 218 ALA A 222 5 5
HELIX 11 AB2 LEU A 240 ALA A 254 1 15
HELIX 12 AB3 VAL A 269 ALA A 274 5 6
HELIX 13 AB4 LEU A 277 GLN A 296 1 20
HELIX 14 AB5 SER B 3 ARG B 17 1 15
HELIX 15 AB6 PRO B 18 GLU B 21 5 4
HELIX 16 AB7 THR B 23 GLN B 36 1 14
HELIX 17 AB8 SER B 82 ARG B 98 1 17
HELIX 18 AB9 PRO B 115 THR B 131 1 17
HELIX 19 AC1 ASP B 134 LYS B 136 5 3
HELIX 20 AC2 SER B 144 ALA B 160 1 17
HELIX 21 AC3 GLU B 182 LYS B 187 1 6
HELIX 22 AC4 GLN B 195 ALA B 208 1 14
HELIX 23 AC5 ALA B 218 ALA B 222 5 5
HELIX 24 AC6 LEU B 240 ALA B 254 1 15
HELIX 25 AC7 VAL B 269 ALA B 274 5 6
HELIX 26 AC8 LEU B 277 TRP B 295 1 19
SHEET 1 AA1 8 GLU A 45 ASP A 50 0
SHEET 2 AA1 8 PRO A 55 ARG A 60 -1 O TRP A 58 N THR A 47
SHEET 3 AA1 8 CYS A 99 ILE A 104 -1 O LEU A 103 N ALA A 57
SHEET 4 AA1 8 ASP A 65 LEU A 73 1 N VAL A 70 O LEU A 102
SHEET 5 AA1 8 MET A 138 ASP A 143 1 O ALA A 141 N LEU A 73
SHEET 6 AA1 8 ALA A 167 LEU A 171 1 O LEU A 171 N GLY A 142
SHEET 7 AA1 8 LEU A 230 GLY A 235 1 O LEU A 231 N CYS A 170
SHEET 8 AA1 8 VAL A 258 TRP A 263 1 O GLU A 261 N ILE A 232
SHEET 1 AA2 8 GLU B 45 ALA B 51 0
SHEET 2 AA2 8 VAL B 54 ARG B 60 -1 O ARG B 60 N GLU B 45
SHEET 3 AA2 8 CYS B 99 ILE B 104 -1 O LEU B 103 N ALA B 57
SHEET 4 AA2 8 ASP B 65 LEU B 73 1 N VAL B 70 O LEU B 102
SHEET 5 AA2 8 MET B 138 ASP B 143 1 O ALA B 141 N LEU B 73
SHEET 6 AA2 8 ALA B 167 LEU B 171 1 O LEU B 171 N GLY B 142
SHEET 7 AA2 8 LEU B 230 GLY B 235 1 O LEU B 231 N CYS B 170
SHEET 8 AA2 8 VAL B 258 TRP B 263 1 O GLU B 261 N ILE B 232
CISPEP 1 ALA A 109 PRO A 110 0 -1.16
CISPEP 2 HIS A 114 PRO A 115 0 9.73
CISPEP 3 ALA B 109 PRO B 110 0 1.55
CISPEP 4 HIS B 114 PRO B 115 0 8.70
SITE 1 AC1 9 PRO A 22 THR A 23 VAL A 24 ARG A 201
SITE 2 AC1 9 MET A 205 HOH A 650 VAL B 258 THR B 259
SITE 3 AC1 9 HOH B1156
SITE 1 AC2 4 THR A 48 HOH A 658 HOH A 682 HOH B1282
SITE 1 AC3 3 PRO A 41 ARG A 92 HOH A 685
SITE 1 AC4 4 ASN A 11 ARG A 14 SER A 15 ASP B 223
SITE 1 AC5 4 TRP A 58 ARG A 60 ARG A 100 HOH A 618
SITE 1 AC6 3 GLY A 52 ARG A 123 TRP A 127
SITE 1 AC7 4 ARG B 126 GLU B 130 HOH B1084 HOH B1135
SITE 1 AC8 4 SER B 3 ALA B 208 GLY B 209 PRO B 278
SITE 1 AC9 1 GLN B 16
SITE 1 AD1 5 SER B 82 ILE B 83 ARG B 84 ASP B 105
SITE 2 AD1 5 HOH B1021
CRYST1 47.883 80.168 144.989 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 0.020884 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006897 0.00000
TER 2415 GLN A 296
TER 4966 TRP B 295
MASTER 415 0 10 26 16 0 13 6 5111 2 34 46
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