HEADER ISOMERASE 10-APR-09 3H12
TITLE CRYSTAL STRUCTURE OF PUTATIVE MANDELATE RACEMASE FROM BORDETELLA
TITLE 2 BRONCHISEPTICA RB50
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANDELATE RACEMASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA BRONCHISEPTICA;
SOURCE 3 ORGANISM_COMMON: ALCALIGENES BRONCHISEPTICUS;
SOURCE 4 ORGANISM_TAXID: 518;
SOURCE 5 STRAIN: RB50;
SOURCE 6 GENE: BB4687;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK
KEYWDS 2 STRUCTURAL GENOMIX RESEARCH CONSORTIUM, NYSGXRC, ENOLASE, PSI-2, NEW
KEYWDS 3 YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,R.TORO,C.MORANO,J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW
AUTHOR 2 YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 8 21-FEB-24 3H12 1 REMARK
REVDAT 7 10-FEB-21 3H12 1 AUTHOR JRNL REMARK LINK
REVDAT 6 21-NOV-18 3H12 1 AUTHOR
REVDAT 5 01-NOV-17 3H12 1 REMARK
REVDAT 4 24-OCT-12 3H12 1 AUTHOR
REVDAT 3 13-JUL-11 3H12 1 VERSN
REVDAT 2 06-OCT-10 3H12 1 TITLE
REVDAT 1 21-APR-09 3H12 0
JRNL AUTH V.N.MALASHKEVICH,R.TORO,C.MORANO,J.M.SAUDER,S.K.BURLEY,
JRNL AUTH 2 S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE MANDELATE RACEMASE FROM
JRNL TITL 2 BORDETELLA BRONCHISEPTICA RB50
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 8.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 128899
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6483
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) : 8571
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 449
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6026
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 781
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
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): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.063
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.475
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6214 ; 0.032 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8449 ; 2.453 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 792 ; 6.593 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 291 ;36.383 ;23.436
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 997 ;13.655 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;16.844 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 921 ; 0.203 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4814 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3900 ; 1.572 ; 3.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6221 ; 3.971 ;50.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2314 ; 7.928 ;50.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2224 ; 2.987 ; 4.500
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 393
REMARK 3 RESIDUE RANGE : A 500 A 500
REMARK 3 RESIDUE RANGE : A 398 A 895
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8756 29.1660 27.7869
REMARK 3 T TENSOR
REMARK 3 T11: 0.0143 T22: 0.0032
REMARK 3 T33: 0.0157 T12: -0.0048
REMARK 3 T13: 0.0112 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2172 L22: 0.1641
REMARK 3 L33: 0.2776 L12: -0.0038
REMARK 3 L13: 0.0069 L23: 0.0337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.0122 S13: -0.0458
REMARK 3 S21: 0.0177 S22: -0.0055 S23: 0.0192
REMARK 3 S31: 0.0444 S32: -0.0234 S33: 0.0186
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 393
REMARK 3 RESIDUE RANGE : B 500 B 500
REMARK 3 RESIDUE RANGE : B 398 B 894
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6977 45.3485 1.9409
REMARK 3 T TENSOR
REMARK 3 T11: 0.0045 T22: 0.0193
REMARK 3 T33: 0.0121 T12: -0.0052
REMARK 3 T13: -0.0019 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.1637 L22: 0.2334
REMARK 3 L33: 0.2417 L12: 0.0001
REMARK 3 L13: -0.0412 L23: -0.0093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: 0.0275 S13: -0.0013
REMARK 3 S21: -0.0204 S22: -0.0077 S23: 0.0421
REMARK 3 S31: 0.0247 S32: -0.0489 S33: 0.0150
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 : RESIDUAL ONLY
REMARK 4
REMARK 4 3H12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 240271
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5740
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.78500
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: SAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8 M NA-ACETATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.07400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.07400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 64.06800
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.07400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.07400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.06800
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 58.07400
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 58.07400
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 64.06800
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 58.07400
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 58.07400
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 64.06800
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 40630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 116.14800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 116.14800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 116.14800
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 116.14800
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 861 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 865 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 HIS A 394
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 MET B 1
REMARK 465 HIS B 394
REMARK 465 HIS B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
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 NH2 ARG A 191 O HOH A 881 1.54
REMARK 500 O HOH B 830 O HOH B 851 1.62
REMARK 500 O HOH B 510 O HOH B 519 1.77
REMARK 500 NH2 ARG B 191 O HOH B 882 1.86
REMARK 500 O HOH B 581 O HOH B 851 1.88
REMARK 500 O HOH B 445 O HOH B 829 1.89
REMARK 500 O HOH B 829 O HOH B 872 1.91
REMARK 500 O HOH B 581 O HOH B 830 1.91
REMARK 500 O HOH B 475 O HOH B 852 1.96
REMARK 500 O HOH A 490 O HOH A 842 1.96
REMARK 500 O HOH B 763 O HOH B 888 1.98
REMARK 500 NE ARG B 191 O HOH B 882 1.99
REMARK 500 O HOH A 470 O HOH A 847 1.99
REMARK 500 NH2 ARG A 191 O HOH A 823 1.99
REMARK 500 O HOH B 427 O HOH B 888 2.00
REMARK 500 O HOH B 503 O HOH B 725 2.01
REMARK 500 O HOH B 513 O HOH B 867 2.02
REMARK 500 O HOH B 519 O HOH B 866 2.03
REMARK 500 O HOH A 442 O HOH A 671 2.03
REMARK 500 O HOH B 461 O HOH B 687 2.06
REMARK 500 OG SER A 343 O HOH A 698 2.07
REMARK 500 O HOH A 756 O HOH A 855 2.07
REMARK 500 CB GLU A 364 O HOH A 537 2.08
REMARK 500 O HOH B 657 O HOH B 747 2.10
REMARK 500 O HOH A 686 O HOH A 880 2.12
REMARK 500 O HOH A 608 O HOH A 835 2.12
REMARK 500 O ALA A 342 O HOH A 489 2.13
REMARK 500 O HOH B 558 O HOH B 592 2.15
REMARK 500 O HOH B 510 O HOH B 858 2.15
REMARK 500 CZ ARG B 191 O HOH B 882 2.17
REMARK 500 O HOH A 532 O HOH A 662 2.18
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 732 O HOH B 482 3655 2.04
REMARK 500 O HOH A 715 O HOH B 890 6555 2.09
REMARK 500 O HOH A 622 O HOH B 623 3655 2.12
REMARK 500 O HOH A 461 O HOH B 834 3655 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 21 CB MET A 21 CG 0.406
REMARK 500 MET A 21 CG MET A 21 SD 0.273
REMARK 500 ARG A 140 CZ ARG A 140 NH1 0.081
REMARK 500 GLU A 220 CG GLU A 220 CD 0.109
REMARK 500 SER A 293 CB SER A 293 OG 0.098
REMARK 500 GLU B 19 CB GLU B 19 CG -0.159
REMARK 500 GLU B 19 CG GLU B 19 CD -0.111
REMARK 500 TYR B 147 CZ TYR B 147 CE2 0.090
REMARK 500 GLU B 158 CD GLU B 158 OE1 0.076
REMARK 500 GLU B 220 CG GLU B 220 CD 0.133
REMARK 500 GLU B 254 CD GLU B 254 OE2 -0.082
REMARK 500 SER B 293 CB SER B 293 OG 0.084
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 13 CB - CG - CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 MET A 21 CB - CG - SD ANGL. DEV. = -30.9 DEGREES
REMARK 500 MET A 21 CG - SD - CE ANGL. DEV. = 11.7 DEGREES
REMARK 500 TYR A 127 CG - CD2 - CE2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 149 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 176 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 195 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 210 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 LEU A 218 CB - CG - CD2 ANGL. DEV. = 15.3 DEGREES
REMARK 500 ASP A 234 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 340 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 MET A 387 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 63 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 120 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET B 122 CG - SD - CE ANGL. DEV. = -12.3 DEGREES
REMARK 500 ARG B 137 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 140 NH1 - CZ - NH2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TYR B 147 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP B 149 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 176 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 186 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP B 201 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU B 218 CB - CG - CD1 ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASP B 233 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU B 318 CB - CG - CD1 ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP B 331 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP B 336 CB - CG - OD2 ANGL. DEV. = -5.5 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 53 -162.13 59.59
REMARK 500 GLU A 92 -51.37 -136.01
REMARK 500 ASP A 149 16.58 84.64
REMARK 500 THR A 258 161.87 65.66
REMARK 500 ASN A 307 -54.08 -167.19
REMARK 500 PRO A 323 57.10 -91.55
REMARK 500 MET A 327 77.52 -150.69
REMARK 500 ASN A 335 100.05 -160.84
REMARK 500 SER B 53 -160.13 64.84
REMARK 500 TYR B 56 -112.42 -123.23
REMARK 500 GLU B 92 -51.67 -136.00
REMARK 500 GLU B 228 57.66 37.96
REMARK 500 THR B 258 160.63 67.62
REMARK 500 ASN B 307 -55.00 -165.94
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 500 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 201 OD2
REMARK 620 2 GLU A 227 OE2 86.5
REMARK 620 3 GLU A 254 OE2 162.6 88.6
REMARK 620 4 HOH A 475 O 97.0 175.6 88.7
REMARK 620 5 HOH A 534 O 78.9 99.6 85.5 83.6
REMARK 620 6 HOH A 594 O 93.8 96.4 103.4 80.9 161.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 500 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 201 OD2
REMARK 620 2 GLU B 227 OE2 87.4
REMARK 620 3 GLU B 254 OE1 162.5 88.8
REMARK 620 4 HOH B 432 O 77.8 99.8 86.1
REMARK 620 5 HOH B 540 O 94.6 95.5 102.7 162.5
REMARK 620 6 HOH B 579 O 97.6 173.9 87.3 84.6 80.8
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 NA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-9280A RELATED DB: TARGETDB
DBREF 3H12 A 4 389 UNP Q7WEE8 Q7WEE8_BORBR 2 387
DBREF 3H12 B 4 389 UNP Q7WEE8 Q7WEE8_BORBR 2 387
SEQADV 3H12 MET A 1 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 SER A 2 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 LEU A 3 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 GLU A 390 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 GLY A 391 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS A 392 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS A 393 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS A 394 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS A 395 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS A 396 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS A 397 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 MET B 1 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 SER B 2 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 LEU B 3 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 GLU B 390 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 GLY B 391 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS B 392 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS B 393 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS B 394 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS B 395 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS B 396 UNP Q7WEE8 EXPRESSION TAG
SEQADV 3H12 HIS B 397 UNP Q7WEE8 EXPRESSION TAG
SEQRES 1 A 397 MET SER LEU LYS ILE THR GLU VAL LYS ALA HIS ALA LEU
SEQRES 2 A 397 SER THR PRO ILE PRO GLU ARG MET ARG VAL GLU SER GLY
SEQRES 3 A 397 ALA GLY LEU LYS LEU ASN ARG GLN MET ILE LEU VAL GLU
SEQRES 4 A 397 VAL ARG THR ASP GLU GLY VAL THR GLY VAL GLY SER PRO
SEQRES 5 A 397 SER GLY PRO TYR ASP LEU ALA VAL LEU LYS ARG ALA ILE
SEQRES 6 A 397 GLU ASP VAL ILE GLY PRO GLN LEU ILE GLY GLU ASP PRO
SEQRES 7 A 397 ALA ASN ILE ASN TYR LEU TRP HIS LYS VAL PHE HIS GLY
SEQRES 8 A 397 GLU VAL SER ARG ASN LEU GLY HIS ARG SER VAL GLY ILE
SEQRES 9 A 397 ALA ALA MET SER GLY VAL ASP ILE ALA LEU TRP ASP LEU
SEQRES 10 A 397 LYS GLY ARG ALA MET ASN GLN PRO ILE TYR GLN LEU LEU
SEQRES 11 A 397 GLY GLY LYS PHE HIS THR ARG GLY VAL ARG ALA TYR ALA
SEQRES 12 A 397 SER SER ILE TYR TRP ASP LEU THR PRO ASP GLN ALA ALA
SEQRES 13 A 397 ASP GLU LEU ALA GLY TRP VAL GLU GLN GLY PHE THR ALA
SEQRES 14 A 397 ALA LYS LEU LYS VAL GLY ARG ALA PRO ARG LYS ASP ALA
SEQRES 15 A 397 ALA ASN LEU ARG ALA MET ARG GLN ARG VAL GLY ALA ASP
SEQRES 16 A 397 VAL GLU ILE LEU VAL ASP ALA ASN GLN SER LEU GLY ARG
SEQRES 17 A 397 HIS ASP ALA LEU ALA MET LEU ARG ILE LEU ASP GLU ALA
SEQRES 18 A 397 GLY CYS TYR TRP PHE GLU GLU PRO LEU SER ILE ASP ASP
SEQRES 19 A 397 ILE GLU GLY HIS ARG ILE LEU ARG ALA GLN GLY THR PRO
SEQRES 20 A 397 VAL ARG ILE ALA THR GLY GLU ASN LEU TYR THR ARG ASN
SEQRES 21 A 397 ALA PHE ASN ASP TYR ILE ARG ASN ASP ALA ILE ASP VAL
SEQRES 22 A 397 LEU GLN ALA ASP ALA SER ARG ALA GLY GLY ILE THR GLU
SEQRES 23 A 397 ALA LEU ALA ILE SER ALA SER ALA ALA SER ALA HIS LEU
SEQRES 24 A 397 ALA TRP ASN PRO HIS THR PHE ASN ASP ILE ILE THR VAL
SEQRES 25 A 397 ALA ALA ASN LEU HIS LEU VAL ALA ALA SER PRO HIS PRO
SEQRES 26 A 397 ALA MET PHE GLU TRP ASP ILE THR HIS ASN ASP LEU MET
SEQRES 27 A 397 THR ARG LEU ALA SER TYR ASP LEU LYS LEU GLU ASN GLY
SEQRES 28 A 397 LEU VAL GLN PRO PRO GLN GLY PRO GLY LEU GLY PHE GLU
SEQRES 29 A 397 ILE ASP TRP ASP PHE VAL ALA ALA HIS ALA TRP LYS GLY
SEQRES 30 A 397 GLU PRO ALA ILE GLY ALA GLY HIS GLY MET LYS LYS GLU
SEQRES 31 A 397 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 397 MET SER LEU LYS ILE THR GLU VAL LYS ALA HIS ALA LEU
SEQRES 2 B 397 SER THR PRO ILE PRO GLU ARG MET ARG VAL GLU SER GLY
SEQRES 3 B 397 ALA GLY LEU LYS LEU ASN ARG GLN MET ILE LEU VAL GLU
SEQRES 4 B 397 VAL ARG THR ASP GLU GLY VAL THR GLY VAL GLY SER PRO
SEQRES 5 B 397 SER GLY PRO TYR ASP LEU ALA VAL LEU LYS ARG ALA ILE
SEQRES 6 B 397 GLU ASP VAL ILE GLY PRO GLN LEU ILE GLY GLU ASP PRO
SEQRES 7 B 397 ALA ASN ILE ASN TYR LEU TRP HIS LYS VAL PHE HIS GLY
SEQRES 8 B 397 GLU VAL SER ARG ASN LEU GLY HIS ARG SER VAL GLY ILE
SEQRES 9 B 397 ALA ALA MET SER GLY VAL ASP ILE ALA LEU TRP ASP LEU
SEQRES 10 B 397 LYS GLY ARG ALA MET ASN GLN PRO ILE TYR GLN LEU LEU
SEQRES 11 B 397 GLY GLY LYS PHE HIS THR ARG GLY VAL ARG ALA TYR ALA
SEQRES 12 B 397 SER SER ILE TYR TRP ASP LEU THR PRO ASP GLN ALA ALA
SEQRES 13 B 397 ASP GLU LEU ALA GLY TRP VAL GLU GLN GLY PHE THR ALA
SEQRES 14 B 397 ALA LYS LEU LYS VAL GLY ARG ALA PRO ARG LYS ASP ALA
SEQRES 15 B 397 ALA ASN LEU ARG ALA MET ARG GLN ARG VAL GLY ALA ASP
SEQRES 16 B 397 VAL GLU ILE LEU VAL ASP ALA ASN GLN SER LEU GLY ARG
SEQRES 17 B 397 HIS ASP ALA LEU ALA MET LEU ARG ILE LEU ASP GLU ALA
SEQRES 18 B 397 GLY CYS TYR TRP PHE GLU GLU PRO LEU SER ILE ASP ASP
SEQRES 19 B 397 ILE GLU GLY HIS ARG ILE LEU ARG ALA GLN GLY THR PRO
SEQRES 20 B 397 VAL ARG ILE ALA THR GLY GLU ASN LEU TYR THR ARG ASN
SEQRES 21 B 397 ALA PHE ASN ASP TYR ILE ARG ASN ASP ALA ILE ASP VAL
SEQRES 22 B 397 LEU GLN ALA ASP ALA SER ARG ALA GLY GLY ILE THR GLU
SEQRES 23 B 397 ALA LEU ALA ILE SER ALA SER ALA ALA SER ALA HIS LEU
SEQRES 24 B 397 ALA TRP ASN PRO HIS THR PHE ASN ASP ILE ILE THR VAL
SEQRES 25 B 397 ALA ALA ASN LEU HIS LEU VAL ALA ALA SER PRO HIS PRO
SEQRES 26 B 397 ALA MET PHE GLU TRP ASP ILE THR HIS ASN ASP LEU MET
SEQRES 27 B 397 THR ARG LEU ALA SER TYR ASP LEU LYS LEU GLU ASN GLY
SEQRES 28 B 397 LEU VAL GLN PRO PRO GLN GLY PRO GLY LEU GLY PHE GLU
SEQRES 29 B 397 ILE ASP TRP ASP PHE VAL ALA ALA HIS ALA TRP LYS GLY
SEQRES 30 B 397 GLU PRO ALA ILE GLY ALA GLY HIS GLY MET LYS LYS GLU
SEQRES 31 B 397 GLY HIS HIS HIS HIS HIS HIS
HET NA A 500 1
HET NA B 500 1
HETNAM NA SODIUM ION
FORMUL 3 NA 2(NA 1+)
FORMUL 5 HOH *781(H2 O)
HELIX 1 1 PRO A 18 ARG A 22 5 5
HELIX 2 2 ASP A 57 VAL A 68 1 12
HELIX 3 3 ILE A 69 LEU A 73 5 5
HELIX 4 4 ASN A 80 GLU A 92 1 13
HELIX 5 5 GLU A 92 GLY A 98 1 7
HELIX 6 6 SER A 101 ASN A 123 1 23
HELIX 7 7 PRO A 125 LEU A 130 1 6
HELIX 8 8 THR A 151 GLY A 166 1 16
HELIX 9 9 ALA A 177 GLY A 193 1 17
HELIX 10 10 GLY A 207 ALA A 221 1 15
HELIX 11 11 ASP A 234 ALA A 243 1 10
HELIX 12 12 TYR A 257 ASN A 268 1 12
HELIX 13 13 GLY A 283 ALA A 297 1 15
HELIX 14 14 ASP A 308 SER A 322 1 15
HELIX 15 15 ASN A 335 THR A 339 5 5
HELIX 16 16 ASP A 366 HIS A 373 1 8
HELIX 17 17 GLY A 386 GLY A 391 1 6
HELIX 18 18 PRO B 18 ARG B 22 5 5
HELIX 19 19 ASP B 57 VAL B 68 1 12
HELIX 20 20 ILE B 69 ILE B 74 1 6
HELIX 21 21 ASN B 80 GLU B 92 1 13
HELIX 22 22 GLU B 92 GLY B 98 1 7
HELIX 23 23 SER B 101 ASN B 123 1 23
HELIX 24 24 PRO B 125 LEU B 130 1 6
HELIX 25 25 THR B 151 GLY B 166 1 16
HELIX 26 26 ALA B 177 GLY B 193 1 17
HELIX 27 27 GLY B 207 ALA B 221 1 15
HELIX 28 28 ASP B 234 ALA B 243 1 10
HELIX 29 29 TYR B 257 ASN B 268 1 12
HELIX 30 30 GLY B 283 ALA B 297 1 15
HELIX 31 31 ASP B 308 SER B 322 1 15
HELIX 32 32 ASN B 335 THR B 339 5 5
HELIX 33 33 ASP B 366 HIS B 373 1 8
HELIX 34 34 GLY B 386 GLY B 391 1 6
SHEET 1 A 3 ILE A 5 PRO A 16 0
SHEET 2 A 3 ASN A 32 THR A 42 -1 O GLU A 39 N LYS A 9
SHEET 3 A 3 GLY A 48 GLY A 50 -1 O GLY A 50 N VAL A 38
SHEET 1 B 2 GLU A 24 SER A 25 0
SHEET 2 B 2 GLY A 28 LEU A 29 -1 O GLY A 28 N SER A 25
SHEET 1 C 8 ALA A 300 TRP A 301 0
SHEET 2 C 8 VAL A 273 LEU A 274 1 N LEU A 274 O ALA A 300
SHEET 3 C 8 ARG A 249 THR A 252 1 O ILE A 250 N VAL A 273
SHEET 4 C 8 TRP A 225 GLU A 227 1 N PHE A 226 O ARG A 249
SHEET 5 C 8 GLU A 197 ASP A 201 1 N VAL A 200 O GLU A 227
SHEET 6 C 8 ALA A 169 LYS A 173 1 N LEU A 172 O LEU A 199
SHEET 7 C 8 VAL A 139 ILE A 146 1 N ILE A 146 O LYS A 173
SHEET 8 C 8 PHE A 328 ASP A 331 1 O PHE A 328 N ARG A 140
SHEET 1 D 8 ALA A 300 TRP A 301 0
SHEET 2 D 8 VAL A 273 LEU A 274 1 N LEU A 274 O ALA A 300
SHEET 3 D 8 ARG A 249 THR A 252 1 O ILE A 250 N VAL A 273
SHEET 4 D 8 TRP A 225 GLU A 227 1 N PHE A 226 O ARG A 249
SHEET 5 D 8 GLU A 197 ASP A 201 1 N VAL A 200 O GLU A 227
SHEET 6 D 8 ALA A 169 LYS A 173 1 N LEU A 172 O LEU A 199
SHEET 7 D 8 VAL A 139 ILE A 146 1 N ILE A 146 O LYS A 173
SHEET 8 D 8 LEU A 352 VAL A 353 -1 O VAL A 353 N VAL A 139
SHEET 1 E 3 ILE B 5 PRO B 16 0
SHEET 2 E 3 ASN B 32 THR B 42 -1 O GLU B 39 N LYS B 9
SHEET 3 E 3 GLY B 48 GLY B 50 -1 O GLY B 50 N VAL B 38
SHEET 1 F 2 GLU B 24 SER B 25 0
SHEET 2 F 2 GLY B 28 LEU B 29 -1 O GLY B 28 N SER B 25
SHEET 1 G 8 ALA B 300 TRP B 301 0
SHEET 2 G 8 VAL B 273 LEU B 274 1 N LEU B 274 O ALA B 300
SHEET 3 G 8 ARG B 249 THR B 252 1 O ILE B 250 N VAL B 273
SHEET 4 G 8 TRP B 225 GLU B 227 1 N PHE B 226 O ARG B 249
SHEET 5 G 8 GLU B 197 ASP B 201 1 N VAL B 200 O GLU B 227
SHEET 6 G 8 ALA B 169 LYS B 173 1 N LEU B 172 O LEU B 199
SHEET 7 G 8 VAL B 139 ILE B 146 1 N ILE B 146 O LYS B 173
SHEET 8 G 8 PHE B 328 ASP B 331 1 O PHE B 328 N TYR B 142
SHEET 1 H 8 ALA B 300 TRP B 301 0
SHEET 2 H 8 VAL B 273 LEU B 274 1 N LEU B 274 O ALA B 300
SHEET 3 H 8 ARG B 249 THR B 252 1 O ILE B 250 N VAL B 273
SHEET 4 H 8 TRP B 225 GLU B 227 1 N PHE B 226 O ARG B 249
SHEET 5 H 8 GLU B 197 ASP B 201 1 N VAL B 200 O GLU B 227
SHEET 6 H 8 ALA B 169 LYS B 173 1 N LEU B 172 O LEU B 199
SHEET 7 H 8 VAL B 139 ILE B 146 1 N ILE B 146 O LYS B 173
SHEET 8 H 8 LEU B 352 VAL B 353 -1 O VAL B 353 N VAL B 139
LINK OD2 ASP A 201 NA NA A 500 1555 1555 2.46
LINK OE2 GLU A 227 NA NA A 500 1555 1555 2.36
LINK OE2 GLU A 254 NA NA A 500 1555 1555 2.21
LINK O HOH A 475 NA NA A 500 1555 1555 2.36
LINK NA NA A 500 O HOH A 534 1555 1555 2.32
LINK NA NA A 500 O HOH A 594 1555 1555 2.50
LINK OD2 ASP B 201 NA NA B 500 1555 1555 2.43
LINK OE2 GLU B 227 NA NA B 500 1555 1555 2.30
LINK OE1 GLU B 254 NA NA B 500 1555 1555 2.22
LINK O HOH B 432 NA NA B 500 1555 1555 2.33
LINK NA NA B 500 O HOH B 540 1555 1555 2.53
LINK NA NA B 500 O HOH B 579 1555 1555 2.40
CISPEP 1 GLY A 54 PRO A 55 0 2.76
CISPEP 2 SER A 144 SER A 145 0 0.33
CISPEP 3 GLY B 54 PRO B 55 0 6.95
CISPEP 4 SER B 144 SER B 145 0 -0.78
SITE 1 AC1 6 ASP A 201 GLU A 227 GLU A 254 HOH A 475
SITE 2 AC1 6 HOH A 534 HOH A 594
SITE 1 AC2 6 ASP B 201 GLU B 227 GLU B 254 HOH B 432
SITE 2 AC2 6 HOH B 540 HOH B 579
CRYST1 116.148 116.148 128.136 90.00 90.00 90.00 I 4 16
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 0.008610 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007804 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
