HEADER TRANSFERASE 10-APR-13 4K3L
TITLE E. COLI SLIDING CLAMP IN COMPLEX WITH ACLF DIPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE III SUBUNIT BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.7.7;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: DNAN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: AN1459;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PND261
KEYWDS E. COLI SLIDING CLAMP, DNAN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.YIN,A.J.OAKLEY
REVDAT 3 08-NOV-23 4K3L 1 REMARK LINK
REVDAT 2 15-JAN-14 4K3L 1 JRNL
REVDAT 1 01-MAY-13 4K3L 0
JRNL AUTH Z.YIN,M.J.KELSO,J.L.BECK,A.J.OAKLEY
JRNL TITL STRUCTURAL AND THERMODYNAMIC DISSECTION OF LINEAR MOTIF
JRNL TITL 2 RECOGNITION BY THE E. COLI SLIDING CLAMP
JRNL REF J.MED.CHEM. V. 56 8665 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 24090409
JRNL DOI 10.1021/JM401118F
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 3 NUMBER OF REFLECTIONS : 109336
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5422
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2724
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 30.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 808
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5902 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5768 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8030 ; 1.120 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13282 ; 0.680 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 781 ; 5.609 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 268 ;36.062 ;23.918
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1044 ;12.551 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;12.044 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 927 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6713 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1316 ; 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): 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 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 4K3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-12
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 125264
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.91900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 1MMI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 100-150MM CACL2, 25
REMARK 280 -30%(V/V) PEG400, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.73200
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 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 GLY A 19
REMARK 465 PRO A 20
REMARK 465 LEU A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 ARG A 24
REMARK 465 PRO A 25
REMARK 465 THR A 26
REMARK 465 LEU A 27
REMARK 465 GLY A 209
REMARK 465 GLY A 210
REMARK 465 ASP A 211
REMARK 465 LEU A 366
REMARK 465 PRO B 20
REMARK 465 LEU B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 ARG B 24
REMARK 465 PRO B 25
REMARK 465 THR B 26
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 LYS A 12 CG CD CE NZ
REMARK 470 GLN A 15 CD OE1 NE2
REMARK 470 GLU A 93 CG CD OE1 OE2
REMARK 470 ARG A 100 NE CZ NH1 NH2
REMARK 470 LYS A 198 CD CE NZ
REMARK 470 ASP A 261 CG OD1 OD2
REMARK 470 GLU A 298 CD OE1 OE2
REMARK 470 LYS A 332 CG CD CE NZ
REMARK 470 ARG A 365 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 12 CE NZ
REMARK 470 GLU B 84 CG CD OE1 OE2
REMARK 470 GLU B 93 CG CD OE1 OE2
REMARK 470 ARG B 105 CZ NH1 NH2
REMARK 470 LYS B 235 CE NZ
REMARK 470 ARG B 240 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 250 CD CE NZ
REMARK 470 HIS B 255 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 277 CG CD CE NZ
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 N LEU B 401 O ACE B 400 2.10
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 CYS A 333 CA - CB - SG ANGL. DEV. = 10.1 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 ASP A 39 -129.14 48.41
REMARK 500 LEU A 49 -20.87 78.22
REMARK 500 ASN A 251 72.24 -158.93
REMARK 500 ASP B 39 56.50 39.91
REMARK 500 LEU B 49 -24.23 80.09
REMARK 500 GLN B 149 49.44 -140.76
REMARK 500 ASN B 288 29.78 48.17
REMARK 500 THR B 341 -64.02 -125.91
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 CA A 408 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 618 O
REMARK 620 2 HOH A 859 O 106.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 163 OE1
REMARK 620 2 GLU B 166 OE1 86.4
REMARK 620 3 HOH B 588 O 84.2 90.2
REMARK 620 4 HOH B 617 O 83.7 169.7 86.2
REMARK 620 5 HOH B 792 O 163.2 107.6 86.4 81.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 339 O
REMARK 620 2 THR B 341 OG1 130.3
REMARK 620 3 SER B 346 O 105.5 115.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 412 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 616 O
REMARK 620 2 HOH B 790 O 121.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 417 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 685 O
REMARK 620 2 HOH B 691 O 78.0
REMARK 620 3 HOH B 767 O 136.4 90.4
REMARK 620 4 HOH B 899 O 74.7 106.3 68.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 400 to 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES B 400 to 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MMI RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE OF P21 SPACE GROUP
REMARK 900 RELATED ID: 4K3K RELATED DB: PDB
REMARK 900 RELATED ID: 4K3M RELATED DB: PDB
REMARK 900 RELATED ID: 4K3O RELATED DB: PDB
REMARK 900 RELATED ID: 4K3P RELATED DB: PDB
REMARK 900 RELATED ID: 4K3Q RELATED DB: PDB
REMARK 900 RELATED ID: 4K3R RELATED DB: PDB
REMARK 900 RELATED ID: 4K3S RELATED DB: PDB
DBREF 4K3L A 1 366 UNP P0A988 DPO3B_ECOLI 1 366
DBREF 4K3L B 1 366 UNP P0A988 DPO3B_ECOLI 1 366
SEQRES 1 A 366 MET LYS PHE THR VAL GLU ARG GLU HIS LEU LEU LYS PRO
SEQRES 2 A 366 LEU GLN GLN VAL SER GLY PRO LEU GLY GLY ARG PRO THR
SEQRES 3 A 366 LEU PRO ILE LEU GLY ASN LEU LEU LEU GLN VAL ALA ASP
SEQRES 4 A 366 GLY THR LEU SER LEU THR GLY THR ASP LEU GLU MET GLU
SEQRES 5 A 366 MET VAL ALA ARG VAL ALA LEU VAL GLN PRO HIS GLU PRO
SEQRES 6 A 366 GLY ALA THR THR VAL PRO ALA ARG LYS PHE PHE ASP ILE
SEQRES 7 A 366 CYS ARG GLY LEU PRO GLU GLY ALA GLU ILE ALA VAL GLN
SEQRES 8 A 366 LEU GLU GLY GLU ARG MET LEU VAL ARG SER GLY ARG SER
SEQRES 9 A 366 ARG PHE SER LEU SER THR LEU PRO ALA ALA ASP PHE PRO
SEQRES 10 A 366 ASN LEU ASP ASP TRP GLN SER GLU VAL GLU PHE THR LEU
SEQRES 11 A 366 PRO GLN ALA THR MET LYS ARG LEU ILE GLU ALA THR GLN
SEQRES 12 A 366 PHE SER MET ALA HIS GLN ASP VAL ARG TYR TYR LEU ASN
SEQRES 13 A 366 GLY MET LEU PHE GLU THR GLU GLY GLU GLU LEU ARG THR
SEQRES 14 A 366 VAL ALA THR ASP GLY HIS ARG LEU ALA VAL CYS SER MET
SEQRES 15 A 366 PRO ILE GLY GLN SER LEU PRO SER HIS SER VAL ILE VAL
SEQRES 16 A 366 PRO ARG LYS GLY VAL ILE GLU LEU MET ARG MET LEU ASP
SEQRES 17 A 366 GLY GLY ASP ASN PRO LEU ARG VAL GLN ILE GLY SER ASN
SEQRES 18 A 366 ASN ILE ARG ALA HIS VAL GLY ASP PHE ILE PHE THR SER
SEQRES 19 A 366 LYS LEU VAL ASP GLY ARG PHE PRO ASP TYR ARG ARG VAL
SEQRES 20 A 366 LEU PRO LYS ASN PRO ASP LYS HIS LEU GLU ALA GLY CYS
SEQRES 21 A 366 ASP LEU LEU LYS GLN ALA PHE ALA ARG ALA ALA ILE LEU
SEQRES 22 A 366 SER ASN GLU LYS PHE ARG GLY VAL ARG LEU TYR VAL SER
SEQRES 23 A 366 GLU ASN GLN LEU LYS ILE THR ALA ASN ASN PRO GLU GLN
SEQRES 24 A 366 GLU GLU ALA GLU GLU ILE LEU ASP VAL THR TYR SER GLY
SEQRES 25 A 366 ALA GLU MET GLU ILE GLY PHE ASN VAL SER TYR VAL LEU
SEQRES 26 A 366 ASP VAL LEU ASN ALA LEU LYS CYS GLU ASN VAL ARG MET
SEQRES 27 A 366 MET LEU THR ASP SER VAL SER SER VAL GLN ILE GLU ASP
SEQRES 28 A 366 ALA ALA SER GLN SER ALA ALA TYR VAL VAL MET PRO MET
SEQRES 29 A 366 ARG LEU
SEQRES 1 B 366 MET LYS PHE THR VAL GLU ARG GLU HIS LEU LEU LYS PRO
SEQRES 2 B 366 LEU GLN GLN VAL SER GLY PRO LEU GLY GLY ARG PRO THR
SEQRES 3 B 366 LEU PRO ILE LEU GLY ASN LEU LEU LEU GLN VAL ALA ASP
SEQRES 4 B 366 GLY THR LEU SER LEU THR GLY THR ASP LEU GLU MET GLU
SEQRES 5 B 366 MET VAL ALA ARG VAL ALA LEU VAL GLN PRO HIS GLU PRO
SEQRES 6 B 366 GLY ALA THR THR VAL PRO ALA ARG LYS PHE PHE ASP ILE
SEQRES 7 B 366 CYS ARG GLY LEU PRO GLU GLY ALA GLU ILE ALA VAL GLN
SEQRES 8 B 366 LEU GLU GLY GLU ARG MET LEU VAL ARG SER GLY ARG SER
SEQRES 9 B 366 ARG PHE SER LEU SER THR LEU PRO ALA ALA ASP PHE PRO
SEQRES 10 B 366 ASN LEU ASP ASP TRP GLN SER GLU VAL GLU PHE THR LEU
SEQRES 11 B 366 PRO GLN ALA THR MET LYS ARG LEU ILE GLU ALA THR GLN
SEQRES 12 B 366 PHE SER MET ALA HIS GLN ASP VAL ARG TYR TYR LEU ASN
SEQRES 13 B 366 GLY MET LEU PHE GLU THR GLU GLY GLU GLU LEU ARG THR
SEQRES 14 B 366 VAL ALA THR ASP GLY HIS ARG LEU ALA VAL CYS SER MET
SEQRES 15 B 366 PRO ILE GLY GLN SER LEU PRO SER HIS SER VAL ILE VAL
SEQRES 16 B 366 PRO ARG LYS GLY VAL ILE GLU LEU MET ARG MET LEU ASP
SEQRES 17 B 366 GLY GLY ASP ASN PRO LEU ARG VAL GLN ILE GLY SER ASN
SEQRES 18 B 366 ASN ILE ARG ALA HIS VAL GLY ASP PHE ILE PHE THR SER
SEQRES 19 B 366 LYS LEU VAL ASP GLY ARG PHE PRO ASP TYR ARG ARG VAL
SEQRES 20 B 366 LEU PRO LYS ASN PRO ASP LYS HIS LEU GLU ALA GLY CYS
SEQRES 21 B 366 ASP LEU LEU LYS GLN ALA PHE ALA ARG ALA ALA ILE LEU
SEQRES 22 B 366 SER ASN GLU LYS PHE ARG GLY VAL ARG LEU TYR VAL SER
SEQRES 23 B 366 GLU ASN GLN LEU LYS ILE THR ALA ASN ASN PRO GLU GLN
SEQRES 24 B 366 GLU GLU ALA GLU GLU ILE LEU ASP VAL THR TYR SER GLY
SEQRES 25 B 366 ALA GLU MET GLU ILE GLY PHE ASN VAL SER TYR VAL LEU
SEQRES 26 B 366 ASP VAL LEU ASN ALA LEU LYS CYS GLU ASN VAL ARG MET
SEQRES 27 B 366 MET LEU THR ASP SER VAL SER SER VAL GLN ILE GLU ASP
SEQRES 28 B 366 ALA ALA SER GLN SER ALA ALA TYR VAL VAL MET PRO MET
SEQRES 29 B 366 ARG LEU
HET LEU A 401 8
HET PHE A 402 12
HET CA A 403 1
HET CA A 404 1
HET PEG A 405 7
HET PEG A 406 7
HET CA A 407 1
HET CA A 408 1
HET ACE A 400 3
HET LEU B 401 8
HET PHE B 402 12
HET CA B 403 1
HET CA B 404 1
HET CA B 405 1
HET CA B 406 1
HET PEG B 407 7
HET PEG B 408 7
HET PGE B 409 10
HET PEG B 410 7
HET CA B 411 1
HET CA B 412 1
HET CA B 413 1
HET EDO B 414 4
HET ACE B 400 3
HET CL B 416 1
HET CA B 417 1
HETNAM LEU LEUCINE
HETNAM PHE PHENYLALANINE
HETNAM CA CALCIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ACE ACETYL GROUP
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 LEU 2(C6 H13 N O2)
FORMUL 4 PHE 2(C9 H11 N O2)
FORMUL 5 CA 12(CA 2+)
FORMUL 7 PEG 5(C4 H10 O3)
FORMUL 11 ACE 2(C2 H4 O)
FORMUL 20 PGE C6 H14 O4
FORMUL 25 EDO C2 H6 O2
FORMUL 27 CL CL 1-
FORMUL 29 HOH *808(H2 O)
HELIX 1 1 ARG A 7 SER A 18 1 12
HELIX 2 2 PRO A 28 LEU A 30 5 3
HELIX 3 3 ALA A 72 LEU A 82 1 11
HELIX 4 4 PRO A 112 PHE A 116 5 5
HELIX 5 5 GLN A 132 GLN A 143 1 12
HELIX 6 6 PHE A 144 MET A 146 5 3
HELIX 7 7 ARG A 152 GLY A 157 5 6
HELIX 8 8 PRO A 196 MET A 206 1 11
HELIX 9 9 ASP A 243 VAL A 247 5 5
HELIX 10 10 CYS A 260 ILE A 272 1 13
HELIX 11 11 VAL A 321 LYS A 332 1 12
HELIX 12 12 ARG B 7 SER B 18 1 12
HELIX 13 13 LEU B 27 LEU B 30 5 4
HELIX 14 14 ALA B 72 LEU B 82 1 11
HELIX 15 15 PRO B 112 PHE B 116 5 5
HELIX 16 16 PRO B 131 GLN B 143 1 13
HELIX 17 17 PHE B 144 MET B 146 5 3
HELIX 18 18 ARG B 152 LEU B 155 5 4
HELIX 19 19 ARG B 197 LEU B 207 1 11
HELIX 20 20 ASP B 243 LEU B 248 1 6
HELIX 21 21 CYS B 260 ILE B 272 1 13
HELIX 22 22 VAL B 321 LYS B 332 1 12
SHEET 1 A 8 LYS A 2 GLU A 6 0
SHEET 2 A 8 GLU A 87 GLU A 93 -1 O VAL A 90 N PHE A 3
SHEET 3 A 8 ARG A 96 SER A 101 -1 O ARG A 100 N ALA A 89
SHEET 4 A 8 SER A 104 SER A 109 -1 O LEU A 108 N MET A 97
SHEET 5 A 8 GLU B 301 ASP B 307 -1 O GLU B 303 N ARG A 105
SHEET 6 A 8 GLN B 289 ASN B 295 -1 N ILE B 292 O GLU B 304
SHEET 7 A 8 GLY B 280 SER B 286 -1 N ARG B 282 O THR B 293
SHEET 8 A 8 MET B 315 ASN B 320 -1 O ILE B 317 N LEU B 283
SHEET 1 B 8 GLY A 66 PRO A 71 0
SHEET 2 B 8 ASN A 32 ALA A 38 -1 N VAL A 37 O GLY A 66
SHEET 3 B 8 THR A 41 THR A 47 -1 O SER A 43 N GLN A 36
SHEET 4 B 8 MET A 51 ALA A 58 -1 O VAL A 57 N LEU A 42
SHEET 5 B 8 PHE A 230 LYS A 235 -1 O THR A 233 N GLU A 52
SHEET 6 B 8 ASN A 222 VAL A 227 -1 N ALA A 225 O PHE A 232
SHEET 7 B 8 PRO A 213 ILE A 218 -1 N GLN A 217 O ARG A 224
SHEET 8 B 8 VAL A 126 PRO A 131 -1 N PHE A 128 O VAL A 216
SHEET 1 C 8 HIS A 191 VAL A 195 0
SHEET 2 C 8 MET A 158 GLU A 163 -1 N THR A 162 O HIS A 191
SHEET 3 C 8 GLU A 166 THR A 172 -1 O ARG A 168 N GLU A 161
SHEET 4 C 8 ARG A 176 PRO A 183 -1 O MET A 182 N LEU A 167
SHEET 5 C 8 SER A 354 VAL A 361 -1 O ALA A 358 N VAL A 179
SHEET 6 C 8 VAL A 347 ASP A 351 -1 N ILE A 349 O TYR A 359
SHEET 7 C 8 ASN A 335 LEU A 340 -1 N MET A 339 O GLN A 348
SHEET 8 C 8 LYS A 254 GLY A 259 -1 N LEU A 256 O MET A 338
SHEET 1 D 8 MET A 315 ASN A 320 0
SHEET 2 D 8 GLY A 280 SER A 286 -1 N LEU A 283 O ILE A 317
SHEET 3 D 8 GLN A 289 ASN A 295 -1 O LYS A 291 N TYR A 284
SHEET 4 D 8 GLU A 301 ASP A 307 -1 O GLU A 304 N ILE A 292
SHEET 5 D 8 SER B 104 SER B 109 -1 O ARG B 105 N GLU A 303
SHEET 6 D 8 ARG B 96 SER B 101 -1 N MET B 97 O LEU B 108
SHEET 7 D 8 GLU B 87 GLU B 93 -1 N GLN B 91 O LEU B 98
SHEET 8 D 8 LYS B 2 GLU B 6 -1 N PHE B 3 O VAL B 90
SHEET 1 E 8 GLY B 66 PRO B 71 0
SHEET 2 E 8 ASN B 32 ALA B 38 -1 N LEU B 35 O THR B 68
SHEET 3 E 8 THR B 41 THR B 47 -1 O SER B 43 N GLN B 36
SHEET 4 E 8 MET B 51 ALA B 58 -1 O VAL B 57 N LEU B 42
SHEET 5 E 8 PHE B 230 LYS B 235 -1 O THR B 233 N GLU B 52
SHEET 6 E 8 ASN B 222 VAL B 227 -1 N ALA B 225 O PHE B 232
SHEET 7 E 8 LEU B 214 ILE B 218 -1 N GLN B 217 O ARG B 224
SHEET 8 E 8 VAL B 126 LEU B 130 -1 N VAL B 126 O ILE B 218
SHEET 1 F 8 HIS B 191 PRO B 196 0
SHEET 2 F 8 GLY B 157 GLU B 163 -1 N PHE B 160 O VAL B 193
SHEET 3 F 8 GLU B 166 THR B 172 -1 O ARG B 168 N GLU B 161
SHEET 4 F 8 ARG B 176 PRO B 183 -1 O ALA B 178 N ALA B 171
SHEET 5 F 8 SER B 354 VAL B 361 -1 O ALA B 358 N VAL B 179
SHEET 6 F 8 VAL B 347 ASP B 351 -1 N ILE B 349 O TYR B 359
SHEET 7 F 8 ASN B 335 LEU B 340 -1 N MET B 339 O GLN B 348
SHEET 8 F 8 LYS B 254 GLY B 259 -1 N ALA B 258 O VAL B 336
SSBOND 1 CYS A 260 CYS A 333 1555 1555 2.03
SSBOND 2 CYS B 260 CYS B 333 1555 1555 2.03
LINK C ACE A 400 N LEU A 401 1555 1555 1.36
LINK C LEU A 401 N PHE A 402 1555 1555 1.33
LINK C ACE B 400 N LEU B 401 1555 1555 1.25
LINK C LEU B 401 N PHE B 402 1555 1555 1.33
LINK CA CA A 403 O HOH A 560 1555 1555 2.93
LINK CA CA A 408 O HOH A 618 1555 1555 2.94
LINK CA CA A 408 O HOH A 859 1555 1555 2.63
LINK OE1 GLU B 163 CA CA B 403 1555 1555 2.30
LINK OE1 GLU B 166 CA CA B 403 1555 1555 2.31
LINK O MET B 339 CA CA B 404 1555 1555 2.90
LINK OG1 THR B 341 CA CA B 404 1555 1555 2.79
LINK O SER B 346 CA CA B 404 1555 1555 2.66
LINK CA CA B 403 O HOH B 588 1555 1555 2.35
LINK CA CA B 403 O HOH B 617 1555 1555 2.32
LINK CA CA B 403 O HOH B 792 1555 1555 2.45
LINK CA CA B 412 O HOH B 616 1555 1555 2.91
LINK CA CA B 412 O HOH B 790 1555 1555 2.70
LINK CA CA B 413 O HOH B 656 1555 1555 2.98
LINK CA CA B 417 O HOH B 685 1555 1555 2.54
LINK CA CA B 417 O HOH B 691 1555 1555 2.42
LINK CA CA B 417 O HOH B 767 1555 1555 2.42
LINK CA CA B 417 O HOH B 899 1555 1555 2.58
SITE 1 AC1 4 GLU A 6 HIS A 9 GLN A 61 HOH A 560
SITE 1 AC2 3 SER A 181 GLN A 355 SER A 356
SITE 1 AC3 6 ASN A 275 ARG A 282 ASN A 295 ASN A 296
SITE 2 AC3 6 PRO A 297 HOH A 535
SITE 1 AC4 4 ASP A 121 TRP A 122 ARG A 224 HOH A 828
SITE 1 AC5 5 HOH A 618 HOH A 859 MET B 1 LYS B 2
SITE 2 AC5 5 GLU B 64
SITE 1 AC6 6 HOH A 534 GLU B 163 GLU B 166 HOH B 588
SITE 2 AC6 6 HOH B 617 HOH B 792
SITE 1 AC7 6 PRO B 249 PRO B 252 MET B 339 LEU B 340
SITE 2 AC7 6 THR B 341 SER B 346
SITE 1 AC8 2 GLY B 46 GLU B 202
SITE 1 AC9 5 ASP B 121 TRP B 122 ARG B 224 HOH B 651
SITE 2 AC9 5 HOH B 836
SITE 1 BC1 2 ALA B 133 HOH B 868
SITE 1 BC2 11 GLN B 132 MET B 206 ASP B 208 GLY B 210
SITE 2 BC2 11 ASP B 211 ASN B 212 VAL B 227 PHE B 230
SITE 3 BC2 11 HOH B 615 HOH B 805 HOH B 806
SITE 1 BC3 5 SER B 187 LEU B 188 PRO B 189 HOH B 786
SITE 2 BC3 5 HOH B 818
SITE 1 BC4 5 PRO A 65 VAL B 126 GLU B 127 HOH B 616
SITE 2 BC4 5 HOH B 790
SITE 1 BC5 2 PRO B 83 HOH B 656
SITE 1 BC6 7 GLU B 161 GLU B 163 ARG B 168 ASP B 243
SITE 2 BC6 7 TYR B 244 ARG B 245 HOH B 648
SITE 1 BC7 5 GLU B 95 THR B 110 HOH B 688 HOH B 817
SITE 2 BC7 5 HOH B 822
SITE 1 BC8 6 HOH A 724 HOH A 758 HOH B 685 HOH B 691
SITE 2 BC8 6 HOH B 767 HOH B 899
SITE 1 BC9 10 ARG A 152 THR A 172 GLY A 174 ARG A 176
SITE 2 BC9 10 PRO A 242 MET A 362 HOH A 563 HOH A 611
SITE 3 BC9 10 HOH A 652 ASN B 251
SITE 1 CC1 8 THR B 172 GLY B 174 HIS B 175 ARG B 176
SITE 2 CC1 8 PRO B 242 MET B 362 HOH B 599 HOH B 759
CRYST1 79.845 67.464 81.369 90.00 113.73 90.00 P 1 21 1 4
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 0.012524 0.000000 0.005506 0.00000
SCALE2 0.000000 0.014823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013425 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
