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HEADER HYDROLASE 19-OCT-20 7APP
TITLE STRUCTURE OF LIPASE TL FROM CAPILLARY GROWN CRYSTAL IN THE PRESENCE OF
TITLE 2 AGAROSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_COMMON: HUMICOLA LANUGINOSA;
SOURCE 4 ORGANISM_TAXID: 5541;
SOURCE 5 GENE: LIP;
SOURCE 6 EXPRESSION_SYSTEM: ASPERGILLUS SP.;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 5065
KEYWDS LIPASE, REINFORCED CROSSLINKED LIPASE CRYSTALS, CLECS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.GAVIRA,S.MARTINEZ-RODRIGUEZ,R.FERNANDE-PENAS,C.VERDUGO-ESCAMILLA
REVDAT 1 03-MAR-21 7APP 0
JRNL AUTH R.FERNANDEZ-PENAS,C.VERDUGO-ESCAMILLA,S.MARTINEZ-RODRIGUEZ,
JRNL AUTH 2 J.A.GAVIRA
JRNL TITL PRODUCTION OF CROSS-LINKED LIPASE CRYSTALS AT A PREPARATIVE
JRNL TITL 2 SCALE
JRNL REF CRYST.GROWTH DES. 2021
JRNL REFN ESSN 1528-7505
JRNL DOI 10.1021/ACS.CGD.0C01608
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 89507
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) : 0.128
REMARK 3 R VALUE (WORKING SET) : 0.127
REMARK 3 FREE R VALUE : 0.154
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4792
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6589
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.1500
REMARK 3 BIN FREE R VALUE SET COUNT : 360
REMARK 3 BIN FREE R VALUE : 0.1930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.14000
REMARK 3 B22 (A**2) : 8.14000
REMARK 3 B33 (A**2) : -16.28000
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): 0.013
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.014
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.954
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4869 ; 0.017 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4261 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6675 ; 2.072 ; 1.652
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9916 ; 1.574 ; 1.592
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 7.240 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 282 ;32.176 ;21.844
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 740 ;15.021 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;15.763 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 627 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5919 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1141 ; 0.003 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.571
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -K, -H, -L
REMARK 3 TWIN FRACTION : 0.429
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7APP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292111875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94343
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 68.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 18.40
REMARK 200 R MERGE (I) : 0.15300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 16.40
REMARK 200 R MERGE FOR SHELL (I) : 0.85900
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: MOLREP
REMARK 200 STARTING MODEL: 6HW1
REMARK 200
REMARK 200 REMARK: HEXAGONAL BIPYRAMID
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5.0 M NAFORMATE, 0.1 M TRIS HCL,
REMARK 280 AGAROSE 0.2% (W/V), PH 7.0, COUNTER-DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 26.64733
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 53.29467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.97100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 66.61833
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 13.32367
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 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 OD1 ASN A 11 O HOH A 401 1.89
REMARK 500 O HOH B 408 O HOH B 556 1.97
REMARK 500 OD1 ASN A 11 O HOH A 402 2.01
REMARK 500 O HOH B 492 O HOH B 609 2.02
REMARK 500 OG SER A 85 O HOH A 403 2.04
REMARK 500 O HOH A 450 O HOH A 601 2.09
REMARK 500 O6 NAG B 301 O HOH B 401 2.10
REMARK 500 N GLU B 1 O HOH B 402 2.11
REMARK 500 OD1 ASN A 11 O HOH A 402 2.13
REMARK 500 O HOH A 501 O HOH A 549 2.13
REMARK 500 ND2 ASN A 11 O HOH A 404 2.13
REMARK 500 O HOH A 494 O HOH B 605 2.15
REMARK 500 O GLU A 56 O HOH A 405 2.17
REMARK 500 O HOH A 401 O HOH A 402 2.19
REMARK 500 ND2 ASN A 33 O5 NAG A 301 2.19
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 608 O HOH B 630 1554 2.15
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 195 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 232 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 232 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PHE B 142 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH1 ANGL. DEV. = -3.7 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 ASN A 26 103.38 -51.12
REMARK 500 ASP A 27 52.03 21.41
REMARK 500 CYS A 41 57.72 -143.80
REMARK 500 SER A 146 -128.22 65.96
REMARK 500 THR A 199 -120.48 37.59
REMARK 500 THR A 199 -121.59 37.59
REMARK 500 LYS B 24 89.93 -63.82
REMARK 500 ASN B 25 24.98 -155.09
REMARK 500 ASN B 25 27.81 -158.69
REMARK 500 ASP B 27 31.19 -145.35
REMARK 500 SER B 146 -135.30 69.60
REMARK 500 THR B 199 -114.59 38.99
REMARK 500 THR B 199 -117.81 38.99
REMARK 500 PHE B 262 -0.03 62.41
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 GLY A 245 GLY A 246 144.11
REMARK 500 GLY B 245 GLY B 246 148.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CYS B 36 -11.45
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 45 O
REMARK 620 2 ALA A 47 O 82.7
REMARK 620 3 HOH A 407 O 85.3 96.5
REMARK 620 4 HOH A 518 O 100.0 91.4 171.1
REMARK 620 5 HOH A 599 O 171.8 93.7 87.8 87.5
REMARK 620 6 HOH A 604 O 91.0 166.3 95.1 77.7 94.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 45 O
REMARK 620 2 ALA B 47 O 80.7
REMARK 620 3 HOH B 430 O 86.1 98.3
REMARK 620 4 HOH B 551 O 98.9 90.4 170.6
REMARK 620 5 HOH B 570 O 176.0 96.3 91.7 83.8
REMARK 620 6 HOH B 592 O 87.7 161.9 94.7 77.7 95.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 188 O
REMARK 620 2 GLY B 191 O 91.8
REMARK 620 3 HOH B 535 O 100.1 72.0
REMARK 620 4 HOH B 544 O 91.6 97.7 164.5
REMARK 620 5 HOH B 564 O 168.6 89.6 91.2 76.9
REMARK 620 6 HOH B 602 O 84.7 171.3 100.8 90.3 95.3
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7APN RELATED DB: PDB
REMARK 900 SAME PROTEIN AND SPACE GROUP BUT DIFFERENT PRECIPITANT.
DBREF 7APP A 1 269 UNP O59952 LIP_THELA 23 291
DBREF 7APP B 1 269 UNP O59952 LIP_THELA 23 291
SEQRES 1 A 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 A 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 A 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 A 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 A 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 A 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 A 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 A 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 A 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 A 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 A 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 A 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 A 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 A 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 A 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 A 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 A 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 A 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 A 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 A 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 A 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 B 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 B 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 B 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 B 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 B 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 B 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 B 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 B 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 B 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 B 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 B 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 B 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 B 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 B 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 B 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 B 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 B 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 B 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 B 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 B 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 B 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
HET NAG A 301 14
HET NA A 302 1
HET FMT A 303 3
HET FMT A 304 3
HET FMT A 305 3
HET FMT A 306 3
HET FMT A 307 3
HET FMT A 308 3
HET FMT A 309 3
HET FMT A 310 3
HET FMT A 311 3
HET NAG B 301 14
HET NA B 302 1
HET NA B 303 1
HET FMT B 304 3
HET FMT B 305 3
HET FMT B 306 3
HET FMT B 307 3
HET FMT B 308 3
HET FMT B 309 3
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NA SODIUM ION
HETNAM FMT FORMIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 NA 3(NA 1+)
FORMUL 5 FMT 15(C H2 O2)
FORMUL 23 HOH *480(H2 O)
HELIX 1 AA1 SER A 3 GLY A 23 1 21
HELIX 2 AA2 CYS A 41 ALA A 47 1 7
HELIX 3 AA3 SER A 85 LEU A 93 1 9
HELIX 4 AA4 ASP A 111 HIS A 135 1 25
HELIX 5 AA5 SER A 146 ARG A 160 1 15
HELIX 6 AA6 ASN A 178 GLN A 188 1 11
HELIX 7 AA7 ILE A 202 LEU A 206 5 5
HELIX 8 AA8 PRO A 208 GLY A 212 5 5
HELIX 9 AA9 THR A 231 ASN A 233 5 3
HELIX 10 AB1 ILE A 255 TRP A 260 5 6
HELIX 11 AB2 SER B 3 GLY B 23 1 21
HELIX 12 AB3 CYS B 41 ALA B 47 1 7
HELIX 13 AB4 SER B 85 ASN B 92 1 8
HELIX 14 AB5 ASP B 111 HIS B 135 1 25
HELIX 15 AB6 SER B 146 ARG B 160 1 15
HELIX 16 AB7 ASN B 178 GLN B 188 1 11
HELIX 17 AB8 ILE B 202 LEU B 206 5 5
HELIX 18 AB9 PRO B 208 GLY B 212 5 5
HELIX 19 AC1 THR B 231 ASN B 233 5 3
HELIX 20 AC2 ILE B 255 TRP B 260 5 6
SHEET 1 AA1 8 ALA A 49 SER A 58 0
SHEET 2 AA1 8 VAL A 63 ASP A 70 -1 O LEU A 67 N LEU A 52
SHEET 3 AA1 8 LEU A 75 PHE A 80 -1 O SER A 79 N PHE A 66
SHEET 4 AA1 8 ARG A 139 HIS A 145 1 O ARG A 139 N ILE A 76
SHEET 5 AA1 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA1 8 LEU A 193 HIS A 198 1 O TYR A 194 N VAL A 168
SHEET 7 AA1 8 GLU A 219 ILE A 222 1 O TYR A 220 N ARG A 195
SHEET 8 AA1 8 ILE A 235 ILE A 238 -1 O VAL A 236 N TRP A 221
SHEET 1 AA2 2 LEU A 97 GLU A 99 0
SHEET 2 AA2 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SHEET 1 AA3 8 ALA B 49 SER B 58 0
SHEET 2 AA3 8 VAL B 63 ASP B 70 -1 O LEU B 67 N TYR B 53
SHEET 3 AA3 8 LEU B 75 PHE B 80 -1 O SER B 79 N PHE B 66
SHEET 4 AA3 8 ARG B 139 HIS B 145 1 O ARG B 139 N ILE B 76
SHEET 5 AA3 8 ILE B 166 TYR B 171 1 O ASP B 167 N PHE B 142
SHEET 6 AA3 8 LEU B 193 HIS B 198 1 O TYR B 194 N VAL B 168
SHEET 7 AA3 8 GLU B 219 ILE B 222 1 O TYR B 220 N ARG B 195
SHEET 8 AA3 8 ILE B 235 ILE B 238 -1 O VAL B 236 N TRP B 221
SHEET 1 AA4 2 LEU B 97 GLU B 99 0
SHEET 2 AA4 2 ARG B 108 HIS B 110 -1 O GLY B 109 N LYS B 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.08
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.11
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 268 1555 1555 2.06
SSBOND 5 CYS B 36 CYS B 41 1555 1555 2.11
SSBOND 6 CYS B 104 CYS B 107 1555 1555 2.14
LINK ND2 ASN A 33 C1 NAG A 301 1555 1555 1.40
LINK ND2 ASN B 33 C1 NAG B 301 1555 1555 1.43
LINK O GLU A 45 NA NA A 302 1555 1555 2.44
LINK O ALA A 47 NA NA A 302 1555 1555 2.38
LINK NA NA A 302 O HOH A 407 1555 1555 2.60
LINK NA NA A 302 O HOH A 518 1555 1555 2.35
LINK NA NA A 302 O HOH A 599 1555 1555 2.39
LINK NA NA A 302 O HOH A 604 1555 1555 2.55
LINK O GLU B 45 NA NA B 302 1555 1555 2.27
LINK O ALA B 47 NA NA B 302 1555 1555 2.42
LINK O GLN B 188 NA NA B 303 1555 1555 2.46
LINK O GLY B 191 NA NA B 303 1555 1555 2.51
LINK NA NA B 302 O HOH B 430 1555 1555 2.34
LINK NA NA B 302 O HOH B 551 1555 1555 2.28
LINK NA NA B 302 O HOH B 570 1555 1555 2.36
LINK NA NA B 302 O HOH B 592 1555 1555 2.55
LINK NA NA B 303 O HOH B 535 1555 1555 2.76
LINK NA NA B 303 O HOH B 544 1555 1555 2.56
LINK NA NA B 303 O HOH B 564 1555 1555 2.23
LINK NA NA B 303 O HOH B 602 1555 1555 2.52
CISPEP 1 LEU A 206 PRO A 207 0 -19.74
CISPEP 2 SER A 217 PRO A 218 0 0.08
CISPEP 3 LEU B 206 PRO B 207 0 -24.05
CISPEP 4 SER B 217 PRO B 218 0 -3.27
CRYST1 137.851 137.851 79.942 90.00 90.00 120.00 P 61 12
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 0.007254 0.004188 0.000000 0.00000
SCALE2 0.000000 0.008376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012509 0.00000
TER 2354 LEU A 269
TER 4654 LEU B 269
MASTER 420 0 20 20 20 0 0 6 4698 2 112 42
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