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HEADER HYDROLASE 16-AUG-10 3OG9
TITLE STRUCTURE OF YAHD WITH MALIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN YAHD A COPPER INDUCIBLE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS SUBSP. LACTIS;
SOURCE 3 ORGANISM_COMMON: STREPTOCOCCUS LACTIS;
SOURCE 4 ORGANISM_TAXID: 272623;
SOURCE 5 STRAIN: IL1403;
SOURCE 6 GENE: YAHD, LL0076, L795, L79507;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, COPPER HOMEOSTASIS, MALIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MARTINEZ FONT,S.MANCINI,E.TAUBERGER,S.MONIOT
REVDAT 1 15-DEC-10 3OG9 0
JRNL AUTH J.MARTINEZ,S.MANCINI,E.TAUBERGER,C.WEISE,W.SAENGER,M.SOLIOZ
JRNL TITL REGULATION AND STRUCTURE OF YAHD, A COPPER INDUCIBLE
JRNL TITL 2 ALPHA/BETA HYDROLASE OF LACTOCOCCUS LACTIS IL1403
JRNL REF FEMS MICROBIOL.LETT. 2010
JRNL REFN ISSN 0378-1097
JRNL PMID 21059179
JRNL DOI 10.1111/J.1574-6968.2010.02144.X
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0040
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 33213
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1749
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) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2410
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3275
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 487
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.20000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.68000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.158
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3480 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4721 ; 1.458 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 441 ; 7.321 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 170 ;37.733 ;25.647
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 625 ;13.362 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ; 7.940 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 519 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2672 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1628 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2400 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 441 ; 0.171 ; 0.200
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): 61 ; 0.178 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 62 ; 0.242 ; 0.200
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): 2208 ; 1.043 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3440 ; 1.538 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1436 ; 2.513 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1281 ; 3.841 ; 4.500
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 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
REMARK 4
REMARK 4 3OG9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB061077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-09
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 : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34965
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 0.1590
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.900
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: PDB CODE 2HLI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 37.5% PEG 3350, 150MM DL-MALIC ACID PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING 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 20.32000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.53500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.32000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.53500
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 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 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 ALA A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 ALA B -2
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET B 1 CG SD CE
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 158 CB CG SD CE
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 486 O HOH A 487 2.00
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 B 403 O HOH B 488 1655 1.62
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 LEU A 186 CA - CB - CG ANGL. DEV. = -14.5 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 39 -8.87 81.74
REMARK 500 THR A 67 -94.10 -97.28
REMARK 500 SER A 107 -119.86 55.11
REMARK 500 SER B 39 -1.84 73.65
REMARK 500 ASN B 50 44.87 -146.34
REMARK 500 THR B 67 -87.36 -99.14
REMARK 500 SER B 107 -123.96 54.69
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 ARG A 61 GLY A 62 -99.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 61 24.1 L L OUTSIDE RANGE
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 383 DISTANCE = 5.34 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT B 500
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT THE UNP ENTRY Q9CJC1 SHOULD HAVE RESIDUES
REMARK 999 191T AND 199K
DBREF 3OG9 A 1 206 UNP Q9CJC1 Q9CJC1_LACLA 1 206
DBREF 3OG9 B 1 206 UNP Q9CJC1 Q9CJC1_LACLA 1 206
SEQADV 3OG9 ALA A -2 UNP Q9CJC1 EXPRESSION TAG
SEQADV 3OG9 GLY A -1 UNP Q9CJC1 EXPRESSION TAG
SEQADV 3OG9 HIS A 0 UNP Q9CJC1 EXPRESSION TAG
SEQADV 3OG9 THR A 191 UNP Q9CJC1 MET 191 SEE REMARK 999
SEQADV 3OG9 LYS A 199 UNP Q9CJC1 ASN 199 SEE REMARK 999
SEQADV 3OG9 ALA B -2 UNP Q9CJC1 EXPRESSION TAG
SEQADV 3OG9 GLY B -1 UNP Q9CJC1 EXPRESSION TAG
SEQADV 3OG9 HIS B 0 UNP Q9CJC1 EXPRESSION TAG
SEQADV 3OG9 THR B 191 UNP Q9CJC1 MET 191 SEE REMARK 999
SEQADV 3OG9 LYS B 199 UNP Q9CJC1 ASN 199 SEE REMARK 999
SEQRES 1 A 209 ALA GLY HIS MET THR ASP TYR VAL PHE LYS ALA GLY ARG
SEQRES 2 A 209 LYS ASP LEU ALA PRO LEU LEU LEU LEU HIS SER THR GLY
SEQRES 3 A 209 GLY ASP GLU HIS GLN LEU VAL GLU ILE ALA GLU MET ILE
SEQRES 4 A 209 ALA PRO SER HIS PRO ILE LEU SER ILE ARG GLY ARG ILE
SEQRES 5 A 209 ASN GLU GLN GLY VAL ASN ARG TYR PHE LYS LEU ARG GLY
SEQRES 6 A 209 LEU GLY GLY PHE THR LYS GLU ASN PHE ASP LEU GLU SER
SEQRES 7 A 209 LEU ASP GLU GLU THR ASP TRP LEU THR ASP GLU VAL SER
SEQRES 8 A 209 LEU LEU ALA GLU LYS HIS ASP LEU ASP VAL HIS LYS MET
SEQRES 9 A 209 ILE ALA ILE GLY TYR SER ASN GLY ALA ASN VAL ALA LEU
SEQRES 10 A 209 ASN MET PHE LEU ARG GLY LYS ILE ASN PHE ASP LYS ILE
SEQRES 11 A 209 ILE ALA PHE HIS GLY MET GLN LEU GLU ASP PHE GLU GLN
SEQRES 12 A 209 THR VAL GLN LEU ASP ASP LYS HIS VAL PHE LEU SER TYR
SEQRES 13 A 209 ALA PRO ASN ASP MET ILE VAL PRO GLN LYS ASN PHE GLY
SEQRES 14 A 209 ASP LEU LYS GLY ASP LEU GLU ASP SER GLY CYS GLN LEU
SEQRES 15 A 209 GLU ILE TYR GLU SER SER LEU GLY HIS GLN LEU THR GLN
SEQRES 16 A 209 GLU GLU VAL LEU ALA ALA LYS LYS TRP LEU THR GLU THR
SEQRES 17 A 209 LYS
SEQRES 1 B 209 ALA GLY HIS MET THR ASP TYR VAL PHE LYS ALA GLY ARG
SEQRES 2 B 209 LYS ASP LEU ALA PRO LEU LEU LEU LEU HIS SER THR GLY
SEQRES 3 B 209 GLY ASP GLU HIS GLN LEU VAL GLU ILE ALA GLU MET ILE
SEQRES 4 B 209 ALA PRO SER HIS PRO ILE LEU SER ILE ARG GLY ARG ILE
SEQRES 5 B 209 ASN GLU GLN GLY VAL ASN ARG TYR PHE LYS LEU ARG GLY
SEQRES 6 B 209 LEU GLY GLY PHE THR LYS GLU ASN PHE ASP LEU GLU SER
SEQRES 7 B 209 LEU ASP GLU GLU THR ASP TRP LEU THR ASP GLU VAL SER
SEQRES 8 B 209 LEU LEU ALA GLU LYS HIS ASP LEU ASP VAL HIS LYS MET
SEQRES 9 B 209 ILE ALA ILE GLY TYR SER ASN GLY ALA ASN VAL ALA LEU
SEQRES 10 B 209 ASN MET PHE LEU ARG GLY LYS ILE ASN PHE ASP LYS ILE
SEQRES 11 B 209 ILE ALA PHE HIS GLY MET GLN LEU GLU ASP PHE GLU GLN
SEQRES 12 B 209 THR VAL GLN LEU ASP ASP LYS HIS VAL PHE LEU SER TYR
SEQRES 13 B 209 ALA PRO ASN ASP MET ILE VAL PRO GLN LYS ASN PHE GLY
SEQRES 14 B 209 ASP LEU LYS GLY ASP LEU GLU ASP SER GLY CYS GLN LEU
SEQRES 15 B 209 GLU ILE TYR GLU SER SER LEU GLY HIS GLN LEU THR GLN
SEQRES 16 B 209 GLU GLU VAL LEU ALA ALA LYS LYS TRP LEU THR GLU THR
SEQRES 17 B 209 LYS
HET MLT A 500 9
HET MLT B 500 9
HETNAM MLT MALATE ION
FORMUL 3 MLT 2(C4 H5 O5 1-)
FORMUL 5 HOH *487(H2 O)
HELIX 1 1 LEU A 29 ALA A 37 1 9
HELIX 2 2 ASN A 50 VAL A 54 5 5
HELIX 3 3 THR A 67 PHE A 71 5 5
HELIX 4 4 ASP A 72 ASP A 95 1 24
HELIX 5 5 ASP A 97 LYS A 100 5 4
HELIX 6 6 SER A 107 ARG A 119 1 13
HELIX 7 7 PRO A 161 SER A 175 1 15
HELIX 8 8 THR A 191 LYS A 206 1 16
HELIX 9 9 LEU B 29 ALA B 37 1 9
HELIX 10 10 ASN B 50 VAL B 54 5 5
HELIX 11 11 THR B 67 PHE B 71 5 5
HELIX 12 12 ASP B 72 HIS B 94 1 23
HELIX 13 13 ASP B 97 LYS B 100 5 4
HELIX 14 14 SER B 107 ARG B 119 1 13
HELIX 15 15 PRO B 161 SER B 175 1 15
HELIX 16 16 THR B 191 THR B 205 1 15
SHEET 1 A 7 TYR A 4 LYS A 7 0
SHEET 2 A 7 ILE A 42 ILE A 45 -1 O SER A 44 N VAL A 5
SHEET 3 A 7 LEU A 16 LEU A 19 1 N LEU A 16 O LEU A 43
SHEET 4 A 7 ILE A 102 TYR A 106 1 O ILE A 104 N LEU A 17
SHEET 5 A 7 LYS A 126 PHE A 130 1 O ILE A 128 N ALA A 103
SHEET 6 A 7 HIS A 148 TYR A 153 1 O PHE A 150 N ALA A 129
SHEET 7 A 7 GLN A 178 GLU A 183 1 O TYR A 182 N LEU A 151
SHEET 1 B 7 TYR B 4 LYS B 7 0
SHEET 2 B 7 ILE B 42 ILE B 45 -1 O ILE B 42 N LYS B 7
SHEET 3 B 7 LEU B 16 LEU B 19 1 N LEU B 18 O LEU B 43
SHEET 4 B 7 ILE B 102 TYR B 106 1 O ILE B 104 N LEU B 17
SHEET 5 B 7 LYS B 126 PHE B 130 1 O ILE B 128 N ALA B 103
SHEET 6 B 7 HIS B 148 TYR B 153 1 O PHE B 150 N ALA B 129
SHEET 7 B 7 GLN B 178 GLU B 183 1 O TYR B 182 N LEU B 151
SITE 1 AC1 9 THR A 22 ARG A 56 PHE A 71 SER A 107
SITE 2 AC1 9 ASN A 108 ASN A 111 HIS A 188 HOH A 319
SITE 3 AC1 9 HOH A 348
SITE 1 AC2 9 THR B 22 ARG B 56 PHE B 71 SER B 107
SITE 2 AC2 9 ASN B 108 ASN B 111 HIS B 188 HOH B 358
SITE 3 AC2 9 HOH B 396
CRYST1 40.640 79.070 130.030 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 0.024606 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007691 0.00000
TER 1716 LYS A 206
TER 3392 LYS B 206
MASTER 395 0 2 16 14 0 6 6 3780 2 18 34
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