HEADER ISOMERASE 03-FEB-10 3LNT
TITLE CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
TITLE 2 PSEUDOMALLEI 1710B WITH BOUND MALONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;
COMPND 5 EC: 5.4.2.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;
SOURCE 3 ORGANISM_TAXID: 320372;
SOURCE 4 STRAIN: 1710B;
SOURCE 5 GENE: GPMA, BURPS1710B_0662;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MUTASE, PHOSPHOGLYCERYLMUTASE, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, SSGCID, GLYCOLYSIS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 05-OCT-11 3LNT 1 JRNL VERSN
REVDAT 1 09-FEB-10 3LNT 0
JRNL AUTH D.R.DAVIES,B.L.STAKER,J.A.ABENDROTH,T.E.EDWARDS,R.HARTLEY,
JRNL AUTH 2 J.LEONARD,H.KIM,A.L.RYCHEL,S.N.HEWITT,P.J.MYLER,L.J.STEWART
JRNL TITL AN ENSEMBLE OF STRUCTURES OF BURKHOLDERIA PSEUDOMALLEI
JRNL TITL 2 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 67 1044 2011
JRNL REFN ESSN 1744-3091
JRNL PMID 21904048
JRNL DOI 10.1107/S1744309111030405
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0104
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 49078
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) : 0.170
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2481
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3405
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 189
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3765
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
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): 0.134
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.918
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3928 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5355 ; 1.385 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 486 ; 6.179 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;35.936 ;23.476
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 644 ;13.217 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;19.039 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 585 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3038 ; 0.007 ; 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): 2387 ; 0.738 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3850 ; 1.324 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1541 ; 2.179 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1498 ; 3.483 ; 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 : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2611 -23.4626 -7.5301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0587 T22: 0.0786
REMARK 3 T33: 0.0773 T12: -0.0003
REMARK 3 T13: 0.0108 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.6547 L22: 0.4551
REMARK 3 L33: 0.6499 L12: 0.0487
REMARK 3 L13: 0.0958 L23: 0.2745
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: 0.0967 S13: -0.0241
REMARK 3 S21: -0.0094 S22: 0.0049 S23: -0.0242
REMARK 3 S31: -0.0322 S32: 0.0440 S33: -0.0170
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9641 -11.7181 9.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0770 T22: 0.1354
REMARK 3 T33: 0.0906 T12: -0.0380
REMARK 3 T13: -0.0399 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 3.8415 L22: 4.4591
REMARK 3 L33: 1.3977 L12: 2.2986
REMARK 3 L13: -0.9386 L23: -1.8127
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.0032 S13: -0.1879
REMARK 3 S21: 0.3719 S22: 0.0137 S23: -0.3278
REMARK 3 S31: -0.2079 S32: 0.2260 S33: 0.0234
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 109 A 187
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0607 -24.8346 8.7168
REMARK 3 T TENSOR
REMARK 3 T11: 0.0597 T22: 0.0482
REMARK 3 T33: 0.0746 T12: 0.0081
REMARK 3 T13: 0.0019 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.7635 L22: 1.2455
REMARK 3 L33: 1.1273 L12: 0.1334
REMARK 3 L13: 0.0783 L23: 0.8071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: -0.0577 S13: -0.0623
REMARK 3 S21: 0.0937 S22: 0.0245 S23: -0.0975
REMARK 3 S31: 0.0726 S32: 0.0459 S33: -0.0283
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 188 A 227
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2783 -36.1021 -1.9443
REMARK 3 T TENSOR
REMARK 3 T11: 0.0309 T22: 0.0593
REMARK 3 T33: 0.1296 T12: 0.0271
REMARK 3 T13: 0.0200 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.0219 L22: 0.6306
REMARK 3 L33: 0.7047 L12: -0.0146
REMARK 3 L13: -0.1117 L23: 0.0335
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: -0.0428 S13: -0.1914
REMARK 3 S21: -0.0073 S22: 0.0577 S23: -0.0144
REMARK 3 S31: -0.0130 S32: 0.1103 S33: -0.0460
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 228 A 244
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4439 -24.7451 -10.9749
REMARK 3 T TENSOR
REMARK 3 T11: 0.0491 T22: 0.0834
REMARK 3 T33: 0.0961 T12: 0.0261
REMARK 3 T13: 0.0287 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 5.0900 L22: 2.1907
REMARK 3 L33: 0.4123 L12: 0.6700
REMARK 3 L13: -0.0667 L23: 0.9213
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: 0.0820 S13: -0.0077
REMARK 3 S21: 0.1420 S22: 0.0275 S23: -0.0591
REMARK 3 S31: 0.0635 S32: 0.0096 S33: -0.0296
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 88
REMARK 3 ORIGIN FOR THE GROUP (A): -47.2729 -17.9332 -14.4280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0846 T22: 0.0681
REMARK 3 T33: 0.0507 T12: -0.0050
REMARK 3 T13: -0.0126 T23: 0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.7513 L22: 0.4469
REMARK 3 L33: 1.0518 L12: -0.1667
REMARK 3 L13: 0.5398 L23: 0.2309
REMARK 3 S TENSOR
REMARK 3 S11: -0.0682 S12: 0.0181 S13: 0.0529
REMARK 3 S21: -0.0569 S22: 0.0761 S23: -0.0079
REMARK 3 S31: -0.0871 S32: -0.0088 S33: -0.0078
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 89 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): -60.0363 -24.2640 -36.2654
REMARK 3 T TENSOR
REMARK 3 T11: 0.1598 T22: 0.0744
REMARK 3 T33: 0.0384 T12: -0.0117
REMARK 3 T13: -0.0553 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.5750 L22: 0.3206
REMARK 3 L33: 2.0071 L12: 0.6912
REMARK 3 L13: -0.2318 L23: 0.0806
REMARK 3 S TENSOR
REMARK 3 S11: -0.0612 S12: 0.1124 S13: 0.0661
REMARK 3 S21: -0.0430 S22: 0.0500 S23: 0.0338
REMARK 3 S31: -0.2809 S32: 0.2279 S33: 0.0112
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 115 B 161
REMARK 3 ORIGIN FOR THE GROUP (A): -56.1488 -34.3249 -23.2371
REMARK 3 T TENSOR
REMARK 3 T11: 0.0712 T22: 0.1014
REMARK 3 T33: 0.0688 T12: -0.0167
REMARK 3 T13: -0.0643 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 2.3403 L22: 0.9024
REMARK 3 L33: 1.8481 L12: 0.1821
REMARK 3 L13: 0.9401 L23: 1.2007
REMARK 3 S TENSOR
REMARK 3 S11: 0.2901 S12: 0.0473 S13: -0.3321
REMARK 3 S21: 0.0099 S22: -0.0734 S23: -0.0891
REMARK 3 S31: 0.1165 S32: -0.1483 S33: -0.2168
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 162 B 186
REMARK 3 ORIGIN FOR THE GROUP (A): -56.0395 -24.1784 -5.1987
REMARK 3 T TENSOR
REMARK 3 T11: 0.0275 T22: 0.1322
REMARK 3 T33: 0.0789 T12: 0.0255
REMARK 3 T13: -0.0152 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.0691 L22: 1.6525
REMARK 3 L33: 3.1836 L12: 0.2667
REMARK 3 L13: -0.2620 L23: 0.0577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: -0.0043 S13: 0.0303
REMARK 3 S21: 0.0077 S22: 0.0323 S23: 0.2171
REMARK 3 S31: -0.0951 S32: -0.1047 S33: -0.0413
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 187 B 229
REMARK 3 ORIGIN FOR THE GROUP (A): -63.4265 -15.8646 -10.7778
REMARK 3 T TENSOR
REMARK 3 T11: 0.0368 T22: 0.2196
REMARK 3 T33: 0.1265 T12: 0.0468
REMARK 3 T13: -0.0257 T23: 0.0947
REMARK 3 L TENSOR
REMARK 3 L11: 4.6627 L22: 0.4307
REMARK 3 L33: 1.5026 L12: 0.9925
REMARK 3 L13: 1.6834 L23: 0.7516
REMARK 3 S TENSOR
REMARK 3 S11: -0.2026 S12: 0.0004 S13: 0.2547
REMARK 3 S21: -0.0997 S22: 0.0036 S23: 0.1590
REMARK 3 S31: -0.2103 S32: -0.2323 S33: 0.1990
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 3LNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057507.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49080
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 46.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.72100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, PH 7.0. CRYSTAL
REMARK 280 TRANSFERRED TO 2.4 M MALONATE, PH 7.0 PLUS 25% (V/V) ETHYLENE
REMARK 280 GLYCOL FOR CRYOPROTECTION, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.11333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.55667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.83500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.27833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 86.39167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
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: 3
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 GLY A 245
REMARK 465 LYS A 246
REMARK 465 SER A 247
REMARK 465 ALA A 248
REMARK 465 ALA A 249
REMARK 465 SER B 0
REMARK 465 ASP B 230
REMARK 465 GLN B 231
REMARK 465 GLU B 232
REMARK 465 ALA B 233
REMARK 465 ILE B 234
REMARK 465 ALA B 235
REMARK 465 LYS B 236
REMARK 465 ALA B 237
REMARK 465 GLN B 238
REMARK 465 ALA B 239
REMARK 465 ALA B 240
REMARK 465 VAL B 241
REMARK 465 ALA B 242
REMARK 465 GLN B 243
REMARK 465 GLN B 244
REMARK 465 GLY B 245
REMARK 465 LYS B 246
REMARK 465 SER B 247
REMARK 465 ALA B 248
REMARK 465 ALA B 249
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 GLU A 108 CG CD OE1 OE2
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 GLU B 218 CG CD OE1 OE2
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 OE2 GLU B 165 O HOH B 363 2.15
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 375 O HOH A 387 5555 2.11
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 THR A 21 -60.40 -109.42
REMARK 500 GLU A 87 154.79 -47.91
REMARK 500 SER A 166 -54.60 -126.92
REMARK 500 ALA A 181 -137.79 -147.33
REMARK 500 GLU B 87 153.72 -49.90
REMARK 500 SER B 166 -53.09 -135.49
REMARK 500 ALA B 181 -140.93 -147.64
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 250 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 284 O
REMARK 620 2 HOH A 252 O 97.3
REMARK 620 3 HOH A 259 O 116.5 145.5
REMARK 620 4 HOH A 281 O 96.9 108.6 75.2
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 NA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 990
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI B 990
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 251
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GW8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
REMARK 900 PSEUDOMALLEI WITH VANADATE AND GLYCEROL
REMARK 900 RELATED ID: 3GP3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
REMARK 900 PSEUDOMALLEI WITH 2-PHOSPHOSERINE
REMARK 900 RELATED ID: 3GP5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
REMARK 900 PSEUDOMALLEI WITH 3-PHOSPHOGLYCERIC ACID AND VANADATE
REMARK 900 RELATED ID: 3FDZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
REMARK 900 PSEUDOMALLEI 1710B WITH BOUND 2,3-DIPHOSPHOGLYCERIC ACID
REMARK 900 AND 3-PHOSPHOGLYCERIC ACID
REMARK 900 RELATED ID: 3EZN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA
REMARK 900 PSEUDOMALLEI 1710B
REMARK 900 RELATED ID: BUPSA.00114.A RELATED DB: TARGETDB
DBREF 3LNT A 1 249 UNP Q3JWH7 GPMA_BURP1 1 249
DBREF 3LNT B 1 249 UNP Q3JWH7 GPMA_BURP1 1 249
SEQADV 3LNT SER A 0 UNP Q3JWH7 EXPRESSION TAG
SEQADV 3LNT SER B 0 UNP Q3JWH7 EXPRESSION TAG
SEQRES 1 A 250 SER MET TYR LYS LEU VAL LEU ILE ARG HIS GLY GLU SER
SEQRES 2 A 250 THR TRP ASN LYS GLU ASN ARG PHE THR GLY TRP VAL ASP
SEQRES 3 A 250 VAL ASP LEU THR GLU GLN GLY ASN ARG GLU ALA ARG GLN
SEQRES 4 A 250 ALA GLY GLN LEU LEU LYS GLU ALA GLY TYR THR PHE ASP
SEQRES 5 A 250 ILE ALA TYR THR SER VAL LEU LYS ARG ALA ILE ARG THR
SEQRES 6 A 250 LEU TRP HIS VAL GLN ASP GLN MET ASP LEU MET TYR VAL
SEQRES 7 A 250 PRO VAL VAL HIS SER TRP ARG LEU ASN GLU ARG HIS TYR
SEQRES 8 A 250 GLY ALA LEU SER GLY LEU ASN LYS ALA GLU THR ALA ALA
SEQRES 9 A 250 LYS TYR GLY ASP GLU GLN VAL LEU VAL TRP ARG ARG SER
SEQRES 10 A 250 TYR ASP THR PRO PRO PRO ALA LEU GLU PRO GLY ASP GLU
SEQRES 11 A 250 ARG ALA PRO TYR ALA ASP PRO ARG TYR ALA LYS VAL PRO
SEQRES 12 A 250 ARG GLU GLN LEU PRO LEU THR GLU CYS LEU LYS ASP THR
SEQRES 13 A 250 VAL ALA ARG VAL LEU PRO LEU TRP ASN GLU SER ILE ALA
SEQRES 14 A 250 PRO ALA VAL LYS ALA GLY LYS GLN VAL LEU ILE ALA ALA
SEQRES 15 A 250 HIS GLY ASN SER LEU ARG ALA LEU ILE LYS TYR LEU ASP
SEQRES 16 A 250 GLY ILE SER ASP ALA ASP ILE VAL GLY LEU ASN ILE PRO
SEQRES 17 A 250 ASN GLY VAL PRO LEU VAL TYR GLU LEU ASP GLU SER LEU
SEQRES 18 A 250 THR PRO ILE ARG HIS TYR TYR LEU GLY ASP GLN GLU ALA
SEQRES 19 A 250 ILE ALA LYS ALA GLN ALA ALA VAL ALA GLN GLN GLY LYS
SEQRES 20 A 250 SER ALA ALA
SEQRES 1 B 250 SER MET TYR LYS LEU VAL LEU ILE ARG HIS GLY GLU SER
SEQRES 2 B 250 THR TRP ASN LYS GLU ASN ARG PHE THR GLY TRP VAL ASP
SEQRES 3 B 250 VAL ASP LEU THR GLU GLN GLY ASN ARG GLU ALA ARG GLN
SEQRES 4 B 250 ALA GLY GLN LEU LEU LYS GLU ALA GLY TYR THR PHE ASP
SEQRES 5 B 250 ILE ALA TYR THR SER VAL LEU LYS ARG ALA ILE ARG THR
SEQRES 6 B 250 LEU TRP HIS VAL GLN ASP GLN MET ASP LEU MET TYR VAL
SEQRES 7 B 250 PRO VAL VAL HIS SER TRP ARG LEU ASN GLU ARG HIS TYR
SEQRES 8 B 250 GLY ALA LEU SER GLY LEU ASN LYS ALA GLU THR ALA ALA
SEQRES 9 B 250 LYS TYR GLY ASP GLU GLN VAL LEU VAL TRP ARG ARG SER
SEQRES 10 B 250 TYR ASP THR PRO PRO PRO ALA LEU GLU PRO GLY ASP GLU
SEQRES 11 B 250 ARG ALA PRO TYR ALA ASP PRO ARG TYR ALA LYS VAL PRO
SEQRES 12 B 250 ARG GLU GLN LEU PRO LEU THR GLU CYS LEU LYS ASP THR
SEQRES 13 B 250 VAL ALA ARG VAL LEU PRO LEU TRP ASN GLU SER ILE ALA
SEQRES 14 B 250 PRO ALA VAL LYS ALA GLY LYS GLN VAL LEU ILE ALA ALA
SEQRES 15 B 250 HIS GLY ASN SER LEU ARG ALA LEU ILE LYS TYR LEU ASP
SEQRES 16 B 250 GLY ILE SER ASP ALA ASP ILE VAL GLY LEU ASN ILE PRO
SEQRES 17 B 250 ASN GLY VAL PRO LEU VAL TYR GLU LEU ASP GLU SER LEU
SEQRES 18 B 250 THR PRO ILE ARG HIS TYR TYR LEU GLY ASP GLN GLU ALA
SEQRES 19 B 250 ILE ALA LYS ALA GLN ALA ALA VAL ALA GLN GLN GLY LYS
SEQRES 20 B 250 SER ALA ALA
HET NA A 250 1
HET MLI A 990 7
HET EDO A 251 4
HET MLI B 990 7
HET EDO B 250 4
HET EDO B 251 4
HETNAM NA SODIUM ION
HETNAM MLI MALONATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NA NA 1+
FORMUL 4 MLI 2(C3 H2 O4 2-)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 9 HOH *256(H2 O)
HELIX 1 1 SER A 12 GLU A 17 1 6
HELIX 2 2 THR A 29 ALA A 46 1 18
HELIX 3 3 LEU A 58 ASP A 73 1 16
HELIX 4 4 TRP A 83 ASN A 86 5 4
HELIX 5 5 TYR A 90 SER A 94 5 5
HELIX 6 6 ASN A 97 GLY A 106 1 10
HELIX 7 7 GLY A 106 SER A 116 1 11
HELIX 8 8 ASP A 135 ALA A 139 5 5
HELIX 9 9 PRO A 142 LEU A 146 5 5
HELIX 10 10 CYS A 151 SER A 166 1 16
HELIX 11 11 SER A 166 ALA A 173 1 8
HELIX 12 12 HIS A 182 ASP A 194 1 13
HELIX 13 13 ASP A 200 LEU A 204 5 5
HELIX 14 14 ASP A 230 GLN A 244 1 15
HELIX 15 15 SER B 12 GLU B 17 1 6
HELIX 16 16 THR B 29 ALA B 46 1 18
HELIX 17 17 LEU B 58 ASP B 73 1 16
HELIX 18 18 TRP B 83 ASN B 86 5 4
HELIX 19 19 TYR B 90 SER B 94 5 5
HELIX 20 20 ASN B 97 GLY B 106 1 10
HELIX 21 21 GLY B 106 SER B 116 1 11
HELIX 22 22 ASP B 135 ALA B 139 5 5
HELIX 23 23 PRO B 142 LEU B 146 5 5
HELIX 24 24 CYS B 151 LEU B 160 1 10
HELIX 25 25 LEU B 160 SER B 166 1 7
HELIX 26 26 SER B 166 ALA B 173 1 8
HELIX 27 27 HIS B 182 ASP B 194 1 13
HELIX 28 28 SER B 197 VAL B 202 1 6
SHEET 1 A 6 VAL A 79 HIS A 81 0
SHEET 2 A 6 ILE A 52 THR A 55 1 N THR A 55 O VAL A 80
SHEET 3 A 6 VAL A 177 ALA A 181 1 O LEU A 178 N TYR A 54
SHEET 4 A 6 TYR A 2 ARG A 8 1 N ILE A 7 O ALA A 181
SHEET 5 A 6 LEU A 212 LEU A 216 -1 O TYR A 214 N LEU A 4
SHEET 6 A 6 PRO A 222 TYR A 227 -1 O ILE A 223 N GLU A 215
SHEET 1 B 6 VAL B 79 HIS B 81 0
SHEET 2 B 6 ILE B 52 THR B 55 1 N THR B 55 O VAL B 80
SHEET 3 B 6 VAL B 177 ALA B 181 1 O LEU B 178 N TYR B 54
SHEET 4 B 6 TYR B 2 ARG B 8 1 N ILE B 7 O ALA B 181
SHEET 5 B 6 LEU B 212 LEU B 216 -1 O LEU B 212 N LEU B 6
SHEET 6 B 6 PRO B 222 TYR B 227 -1 O TYR B 226 N VAL B 213
LINK NA NA A 250 O HOH A 284 1555 1555 2.65
LINK NA NA A 250 O HOH A 252 1555 1555 2.68
LINK NA NA A 250 O HOH A 259 1555 1555 2.75
LINK NA NA A 250 O HOH A 281 1555 1555 3.11
SITE 1 AC1 4 TRP A 23 HOH A 252 HOH A 259 HOH A 284
SITE 1 AC2 13 ARG A 8 HIS A 9 ASN A 15 ARG A 19
SITE 2 AC2 13 THR A 21 GLY A 22 GLU A 87 TYR A 90
SITE 3 AC2 13 HOH A 255 HOH A 268 HOH A 300 HOH A 304
SITE 4 AC2 13 HOH A 360
SITE 1 AC3 12 ARG B 8 HIS B 9 ASN B 15 ARG B 19
SITE 2 AC3 12 THR B 21 GLY B 22 GLU B 87 TYR B 90
SITE 3 AC3 12 HOH B 273 HOH B 322 HOH B 327 HOH B 359
SITE 1 AC4 4 EDO A 251 ARG B 63 TRP B 66 HIS B 67
SITE 1 AC5 3 ARG A 63 HIS A 67 EDO B 250
SITE 1 AC6 6 VAL A 79 HOH A 260 PRO B 78 VAL B 79
SITE 2 AC6 6 ARG B 115 HOH B 289
CRYST1 119.620 119.620 103.670 90.00 90.00 120.00 P 65 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008360 0.004827 0.000000 0.00000
SCALE2 0.000000 0.009653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009646 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
