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HEADER HYDROLASE 20-NOV-18 6I8F
TITLE STRUCTURE OF ESTER-HYDROLASE EH1AB1 FROM THE METAGENOME OF LAKE ARREO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EH1AB1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-46 EK/LIC
KEYWDS ESTER HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 27-NOV-19 6I8F 0
JRNL AUTH I.CEA-RAMA,J.SANZ-APARICIO
JRNL TITL STRUCTURE OF SERINE ESTER HYDROLASE EH1AB1 FROM THE
JRNL TITL 2 METAGENOME OF LAKE ARREO
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 38599
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2081
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) : 2.11
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2847
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4770
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 342
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.80000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : -0.40000
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): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.157
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.046
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5008 ; 0.007 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 4408 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6766 ; 1.192 ; 1.685
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10318 ; 0.904 ; 1.681
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 628 ; 7.065 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 272 ;28.428 ;20.515
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 718 ;12.902 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;19.501 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 638 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5710 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 938 ; 0.001 ; 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): 2518 ; 1.893 ; 2.833
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2517 ; 1.893 ; 2.833
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3144 ; 3.208 ; 4.244
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3145 ; 3.208 ; 4.244
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2490 ; 2.251 ; 3.171
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2485 ; 2.251 ; 3.174
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3613 ; 3.609 ; 4.604
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5677 ; 7.169 ;35.773
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5678 ; 7.169 ;35.782
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 18 4
REMARK 3 1 B 1 B 18 4
REMARK 3 2 A 34 A 202 4
REMARK 3 2 B 34 B 202 4
REMARK 3 3 A 219 A 315 4
REMARK 3 3 B 219 B 315 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4060 ; 0.43 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4060 ; 3.68 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6I8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.966000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.11.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40731
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 43.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.02
REMARK 200 STARTING MODEL: 5JD4
REMARK 200
REMARK 200 REMARK: THIN BARS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45 % PEG P400, 0.1 M BIS-TRIS PH 6.5,
REMARK 280 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 41.11300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.08300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.02250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.08300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.11300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.02250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
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 O HOH B 647 O HOH B 653 1.91
REMARK 500 O HOH B 618 O HOH B 636 1.94
REMARK 500 O HOH A 501 O HOH A 647 2.03
REMARK 500 O HOH A 633 O HOH A 639 2.07
REMARK 500 O HOH B 660 O HOH B 668 2.07
REMARK 500 O HOH A 572 O HOH A 642 2.09
REMARK 500 NH2 ARG B 71 O ALA B 77 2.11
REMARK 500 O HOH A 611 O HOH A 661 2.12
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 CG2 VAL B 31 O ARG B 175 4445 2.02
REMARK 500 O HOH A 503 O HOH B 625 3454 2.16
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 HIS A 214 CB - CA - C ANGL. DEV. = 12.5 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 161 -123.20 59.07
REMARK 500 TYR A 189 63.96 28.12
REMARK 500 PHE A 209 103.58 -56.37
REMARK 500 LEU A 210 56.24 36.64
REMARK 500 LYS A 212 -80.67 55.81
REMARK 500 ALA A 213 33.82 -88.57
REMARK 500 TYR A 255 69.83 -103.79
REMARK 500 LEU A 291 47.30 -91.84
REMARK 500 THR B 17 71.78 69.46
REMARK 500 ASP B 25 52.44 -162.08
REMARK 500 PRO B 28 66.52 -67.81
REMARK 500 ALA B 30 -115.23 57.35
REMARK 500 SER B 161 -122.19 55.32
REMARK 500 TYR B 189 64.06 29.58
REMARK 500 SER B 198 171.29 -59.29
REMARK 500 PHE B 204 40.02 -108.07
REMARK 500 PHE B 209 -58.79 67.42
REMARK 500 TYR B 255 76.71 -114.12
REMARK 500 LEU B 291 47.69 -92.62
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 HIS A 214 MET A 215 149.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 18 0.15 SIDE CHAIN
REMARK 500 ARG A 69 0.09 SIDE CHAIN
REMARK 500 ARG A 111 0.10 SIDE CHAIN
REMARK 500 ARG A 201 0.08 SIDE CHAIN
REMARK 500 ARG B 18 0.13 SIDE CHAIN
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 MG A 412 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 644 O
REMARK 620 2 HOH A 657 O 92.3
REMARK 620 3 HOH A 515 O 94.6 89.7
REMARK 620 4 HOH A 528 O 175.1 89.3 90.1
REMARK 620 5 HOH A 532 O 88.3 178.8 91.2 90.0
REMARK 620 6 HOH A 541 O 89.3 88.9 175.9 86.0 90.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 410 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 524 O
REMARK 620 2 HOH B 519 O 91.2
REMARK 620 3 HOH B 534 O 86.0 90.4
REMARK 620 4 HOH B 561 O 88.3 177.4 92.0
REMARK 620 5 HOH B 645 O 174.8 91.7 89.7 89.0
REMARK 620 6 HOH B 662 O 93.4 86.4 176.8 91.1 91.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 410
DBREF 6I8F A 1 315 PDB 6I8F 6I8F 1 315
DBREF 6I8F B 1 315 PDB 6I8F 6I8F 1 315
SEQRES 1 A 315 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 A 315 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 A 315 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 A 315 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 A 315 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 A 315 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 A 315 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 A 315 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 A 315 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 A 315 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 A 315 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 A 315 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 A 315 VAL GLY GLY ASP SER ALA GLY GLY ALA MET ALA ALA VAL
SEQRES 14 A 315 VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY PRO
SEQRES 15 A 315 ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER SER
SEQRES 16 A 315 ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY TYR
SEQRES 17 A 315 PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU ALA
SEQRES 18 A 315 TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG LEU
SEQRES 19 A 315 SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO PRO
SEQRES 20 A 315 ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG ASP
SEQRES 21 A 315 GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA GLY
SEQRES 22 A 315 ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE HIS
SEQRES 23 A 315 GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY LEU
SEQRES 24 A 315 LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA HIS
SEQRES 25 A 315 PHE GLY THR
SEQRES 1 B 315 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 B 315 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 B 315 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 B 315 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 B 315 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 B 315 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 B 315 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 B 315 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 B 315 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 B 315 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 B 315 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 B 315 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 B 315 VAL GLY GLY ASP SER ALA GLY GLY ALA MET ALA ALA VAL
SEQRES 14 B 315 VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY PRO
SEQRES 15 B 315 ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER SER
SEQRES 16 B 315 ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY TYR
SEQRES 17 B 315 PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU ALA
SEQRES 18 B 315 TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG LEU
SEQRES 19 B 315 SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO PRO
SEQRES 20 B 315 ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG ASP
SEQRES 21 B 315 GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA GLY
SEQRES 22 B 315 ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE HIS
SEQRES 23 B 315 GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY LEU
SEQRES 24 B 315 LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA HIS
SEQRES 25 B 315 PHE GLY THR
HET PEG A 401 7
HET PEG A 402 7
HET PEG A 403 7
HET PEG A 404 7
HET PEG A 405 7
HET GOL A 406 6
HET GOL A 407 6
HET GOL A 408 6
HET GOL A 409 6
HET GOL A 410 6
HET GOL A 411 6
HET MG A 412 1
HET PEG B 401 7
HET PEG B 402 7
HET PEG B 403 7
HET PEG B 404 7
HET PEG B 405 7
HET GOL B 406 6
HET GOL B 407 6
HET GOL B 408 6
HET GOL B 409 6
HET MG B 410 1
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 PEG 10(C4 H10 O3)
FORMUL 8 GOL 10(C3 H8 O3)
FORMUL 14 MG 2(MG 2+)
FORMUL 25 HOH *342(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 19 1 17
HELIX 2 AA2 GLY A 23 LEU A 27 5 5
HELIX 3 AA3 PRO A 28 ASP A 42 1 15
HELIX 4 AA4 ILE A 96 THR A 98 5 3
HELIX 5 AA5 HIS A 99 ARG A 111 1 13
HELIX 6 AA6 PRO A 128 ASN A 144 1 17
HELIX 7 AA7 ALA A 145 PHE A 148 5 4
HELIX 8 AA8 SER A 161 ALA A 177 1 17
HELIX 9 AA9 SER A 198 GLU A 206 1 9
HELIX 10 AB1 MET A 215 VAL A 223 1 9
HELIX 11 AB2 SER A 235 ALA A 239 5 5
HELIX 12 AB3 LEU A 258 ALA A 272 1 15
HELIX 13 AB4 LEU A 295 GLY A 314 1 20
HELIX 14 AB5 LEU B 3 ALA B 16 1 14
HELIX 15 AB6 ALA B 30 GLU B 44 1 15
HELIX 16 AB7 ILE B 96 THR B 98 5 3
HELIX 17 AB8 HIS B 99 ARG B 111 1 13
HELIX 18 AB9 PRO B 128 ASN B 144 1 17
HELIX 19 AC1 ALA B 145 PHE B 148 5 4
HELIX 20 AC2 SER B 161 GLY B 178 1 18
HELIX 21 AC3 SER B 198 PHE B 204 1 7
HELIX 22 AC4 SER B 211 VAL B 223 1 13
HELIX 23 AC5 SER B 235 ALA B 239 5 5
HELIX 24 AC6 LEU B 258 ALA B 272 1 15
HELIX 25 AC7 LEU B 295 GLY B 314 1 20
SHEET 1 AA116 GLU A 52 ALA A 59 0
SHEET 2 AA116 GLU A 64 ARG A 71 -1 O ARG A 69 N ALA A 54
SHEET 3 AA116 GLN A 113 ASP A 118 -1 O VAL A 114 N TYR A 70
SHEET 4 AA116 LEU A 80 TYR A 86 1 N LEU A 83 O ILE A 115
SHEET 5 AA116 ALA A 150 ASP A 160 1 O ALA A 156 N THR A 82
SHEET 6 AA116 PHE A 184 ILE A 188 1 O MET A 186 N VAL A 157
SHEET 7 AA116 ALA A 248 TYR A 255 1 O PHE A 249 N LEU A 187
SHEET 8 AA116 THR A 276 ILE A 285 1 O THR A 277 N VAL A 250
SHEET 9 AA116 THR B 276 ILE B 285 -1 O TYR B 278 N TYR A 278
SHEET 10 AA116 ALA B 248 TYR B 255 1 N VAL B 250 O THR B 277
SHEET 11 AA116 PHE B 184 ILE B 188 1 N LEU B 187 O PHE B 249
SHEET 12 AA116 ALA B 150 ASP B 160 1 N VAL B 157 O MET B 186
SHEET 13 AA116 LEU B 80 TYR B 86 1 N THR B 82 O ALA B 156
SHEET 14 AA116 GLN B 113 ASP B 118 1 O ILE B 115 N LEU B 83
SHEET 15 AA116 GLU B 64 ARG B 71 -1 N TYR B 70 O VAL B 114
SHEET 16 AA116 GLU B 52 ALA B 59 -1 N PHE B 58 O ILE B 65
LINK MG MG A 412 O HOH A 644 1555 1555 2.15
LINK MG MG A 412 O HOH A 657 1555 1555 2.17
LINK MG MG A 412 O HOH A 515 1555 1555 2.16
LINK MG MG A 412 O HOH A 528 1555 1555 2.15
LINK MG MG A 412 O HOH A 532 1555 1555 2.17
LINK MG MG A 412 O HOH A 541 1555 1555 2.18
LINK MG MG B 410 O HOH B 524 1555 1555 2.13
LINK MG MG B 410 O HOH B 519 1555 1555 2.16
LINK MG MG B 410 O HOH B 534 1555 1555 2.19
LINK MG MG B 410 O HOH B 561 1555 1555 2.18
LINK MG MG B 410 O HOH B 645 1555 1555 2.15
LINK MG MG B 410 O HOH B 662 1555 1555 2.17
CISPEP 1 ALA A 122 PRO A 123 0 8.06
CISPEP 2 PHE A 127 PRO A 128 0 11.67
CISPEP 3 ALA B 122 PRO B 123 0 4.77
CISPEP 4 PHE B 127 PRO B 128 0 5.95
SITE 1 AC1 5 ARG A 259 ASP A 260 ARG A 263 HOH A 612
SITE 2 AC1 5 ILE B 270
SITE 1 AC2 2 MET A 13 GOL A 411
SITE 1 AC3 5 THR A 292 ARG A 293 PHE A 294 SER A 296
SITE 2 AC3 5 LEU A 299
SITE 1 AC4 5 GLU A 64 ARG A 66 ASP A 118 TYR A 119
SITE 2 AC4 5 HOH A 571
SITE 1 AC5 5 ASN A 55 GOL A 406 HOH A 503 VAL B 53
SITE 2 AC5 5 ASN B 55
SITE 1 AC6 6 GLU A 49 VAL A 50 ARG A 104 PEG A 405
SITE 2 AC6 6 ASN B 55 GLY B 56
SITE 1 AC7 9 GLU A 52 ARG A 69 ARG A 71 GLY A 78
SITE 2 AC7 9 GLY A 149 HOH A 505 ARG B 69 GLU B 146
SITE 3 AC7 9 SER B 147
SITE 1 AC8 3 ARG A 120 ASP A 132 ASP B 11
SITE 1 AC9 5 ALA A 77 LEU A 79 PRO A 81 ARG A 154
SITE 2 AC9 5 HOH A 513
SITE 1 AD1 3 GLY A 89 ASP A 160 HOH A 537
SITE 1 AD2 4 MET A 39 ASP A 42 PEG A 402 VAL B 202
SITE 1 AD3 6 HOH A 515 HOH A 528 HOH A 532 HOH A 541
SITE 2 AD3 6 HOH A 644 HOH A 657
SITE 1 AD4 4 MET B 13 TYR B 208 HIS B 286 HOH B 556
SITE 1 AD5 4 ILE A 270 ARG B 259 ASP B 260 ARG B 263
SITE 1 AD6 3 ARG B 105 LYS B 109 LYS B 300
SITE 1 AD7 4 ASP B 118 TYR B 119 LEU B 121 GLU B 124
SITE 1 AD8 3 THR B 227 ARG B 233 HOH B 591
SITE 1 AD9 9 ARG A 263 ASP A 267 ILE A 270 TYR A 278
SITE 2 AD9 9 ARG B 263 ALA B 266 ASP B 267 ILE B 270
SITE 3 AD9 9 TYR B 278
SITE 1 AE1 4 GLU B 49 VAL B 50 VAL B 53 ARG B 104
SITE 1 AE2 4 PRO B 81 ARG B 154 GLY B 314 HOH B 508
SITE 1 AE3 5 GLN B 172 ALA B 173 ASP B 176 ARG B 233
SITE 2 AE3 5 HOH B 518
SITE 1 AE4 6 HOH B 519 HOH B 524 HOH B 534 HOH B 561
SITE 2 AE4 6 HOH B 645 HOH B 662
CRYST1 82.226 86.045 98.166 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 0.012162 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011622 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010187 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.487908 -0.023057 0.872591 -39.46196 1
MTRIX2 2 -0.041977 -0.997875 -0.049839 1.93466 1
MTRIX3 2 0.871885 -0.060946 0.485903 23.48877 1
TER 2386 THR A 315
TER 4772 THR B 315
MASTER 487 0 22 25 16 0 35 12 5244 2 146 50
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