HEADER IMMUNE SYSTEM 11-OCT-10 2XTM
TITLE CRYSTAL STRUCTURE OF GDP-BOUND HUMAN GIMAP2, AMINO ACID RESIDUES
TITLE 2 1-234
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE IMAP FAMILY MEMBER 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-234;
COMPND 5 SYNONYM: GIMAP2, IMMUNITY-ASSOCIATED PROTEIN 2, HIMAP2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P1
KEYWDS IMMUNE SYSTEM, G PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.SCHWEFEL,C.FROEHLICH,O.DAUMKE
REVDAT 4 08-DEC-10 2XTM 1 JRNL
REVDAT 3 24-NOV-10 2XTM 1 JRNL
REVDAT 2 17-NOV-10 2XTM 1 JRNL
REVDAT 1 20-OCT-10 2XTM 0
JRNL AUTH D.SCHWEFEL,C.FROEHLICH,J.EICHHORST,B.WIESNER,J.BEHLKE,
JRNL AUTH 2 L.ARAVIND,O.DAUMKE
JRNL TITL STRUCTURAL BASIS OF OLIGOMERIZATION IN SEPTIN-LIKE GTPASE
JRNL TITL 2 OF IMMUNITY-ASSOCIATED PROTEIN 2 (GIMAP2)
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 20299 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 21059949
JRNL DOI 10.1073/PNAS.1010322107
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.SCHWEFEL,C.FROHLICH,O.DAUMKE
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X- RAY
REMARK 1 TITL 2 ANALYSIS OF HUMAN GIMAP2.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 66 725 2010
REMARK 1 REFN ISSN 1744-3091
REMARK 1 PMID 20516611
REMARK 1 DOI 10.1107/S174430911001537X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0070
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 52141
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 FREE R VALUE TEST SET COUNT : 2807
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3720
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3134
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 298
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.51000
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): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.598
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3270 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4442 ; 1.250 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 438 ; 5.262 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 134 ;36.448 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 580 ;13.158 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.552 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 505 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2403 ; 0.005 ; 0.020
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): 2052 ; 0.617 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3284 ; 1.166 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1218 ; 2.015 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1140 ; 3.252 ; 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 21 A 92
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7880 -3.3103 -36.3018
REMARK 3 T TENSOR
REMARK 3 T11: 0.0221 T22: 0.0117
REMARK 3 T33: 0.0524 T12: -0.0008
REMARK 3 T13: -0.0202 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.5937 L22: 1.0904
REMARK 3 L33: 1.0594 L12: 0.0457
REMARK 3 L13: -0.1142 L23: -0.1520
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: -0.0523 S13: 0.0404
REMARK 3 S21: 0.0121 S22: -0.0508 S23: -0.1036
REMARK 3 S31: -0.0186 S32: 0.0809 S33: 0.0338
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 93 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7760 -0.5122 -36.4610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.0079
REMARK 3 T33: 0.0409 T12: 0.0042
REMARK 3 T13: -0.0100 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.4518 L22: 0.7306
REMARK 3 L33: 1.1637 L12: 0.0020
REMARK 3 L13: 0.1368 L23: -0.1416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0413 S13: 0.0397
REMARK 3 S21: -0.0190 S22: 0.0089 S23: 0.0319
REMARK 3 S31: -0.0597 S32: -0.0570 S33: -0.0047
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 139 A 184
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3511 6.5082 -51.2746
REMARK 3 T TENSOR
REMARK 3 T11: 0.0603 T22: 0.0021
REMARK 3 T33: 0.0533 T12: -0.0029
REMARK 3 T13: -0.0137 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.8283 L22: 1.0876
REMARK 3 L33: 1.4245 L12: -0.3338
REMARK 3 L13: -0.0475 L23: -0.5940
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: 0.0151 S13: 0.0652
REMARK 3 S21: -0.1359 S22: -0.0066 S23: 0.0248
REMARK 3 S31: 0.0476 S32: -0.0381 S33: -0.0004
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 185 A 227
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2786 11.1415 -34.7223
REMARK 3 T TENSOR
REMARK 3 T11: 0.0438 T22: 0.0114
REMARK 3 T33: 0.0917 T12: -0.0036
REMARK 3 T13: -0.0166 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.9342 L22: 1.1084
REMARK 3 L33: 2.0776 L12: 0.4414
REMARK 3 L13: -0.4598 L23: -0.5484
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: -0.0854 S13: 0.1860
REMARK 3 S21: 0.0668 S22: -0.0749 S23: -0.0360
REMARK 3 S31: -0.2326 S32: 0.0376 S33: 0.0696
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 : B 21 B 31
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2038 -3.8344 -8.7011
REMARK 3 T TENSOR
REMARK 3 T11: 0.0758 T22: 0.1550
REMARK 3 T33: 0.0178 T12: -0.0225
REMARK 3 T13: -0.0165 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 2.4017 L22: 9.9327
REMARK 3 L33: 4.8078 L12: 0.7182
REMARK 3 L13: 0.1570 L23: 5.3426
REMARK 3 S TENSOR
REMARK 3 S11: 0.0921 S12: -0.5445 S13: -0.1335
REMARK 3 S21: 0.2740 S22: -0.1170 S23: -0.0340
REMARK 3 S31: 0.2085 S32: -0.0313 S33: 0.0249
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 32 B 68
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8812 -7.5015 -0.5675
REMARK 3 T TENSOR
REMARK 3 T11: 0.2733 T22: 0.4000
REMARK 3 T33: 0.0620 T12: -0.0438
REMARK 3 T13: -0.0705 T23: 0.1042
REMARK 3 L TENSOR
REMARK 3 L11: 4.7326 L22: 3.2260
REMARK 3 L33: 1.5920 L12: 1.5215
REMARK 3 L13: -0.7695 L23: 1.0706
REMARK 3 S TENSOR
REMARK 3 S11: 0.1787 S12: -1.0782 S13: -0.4110
REMARK 3 S21: 0.6840 S22: -0.1536 S23: -0.1641
REMARK 3 S31: 0.3072 S32: 0.1110 S33: -0.0251
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 69 B 96
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7991 -1.6986 -8.9004
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.1857
REMARK 3 T33: 0.0527 T12: 0.0237
REMARK 3 T13: -0.0382 T23: -0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 4.6701 L22: 1.9786
REMARK 3 L33: 3.0473 L12: 1.5851
REMARK 3 L13: -0.5972 L23: 0.2523
REMARK 3 S TENSOR
REMARK 3 S11: 0.1821 S12: -0.6402 S13: -0.1236
REMARK 3 S21: 0.0311 S22: -0.0167 S23: -0.2148
REMARK 3 S31: -0.0141 S32: 0.1250 S33: -0.1654
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 97 B 150
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6910 3.4391 -10.3830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0619 T22: 0.1356
REMARK 3 T33: 0.0298 T12: -0.0316
REMARK 3 T13: 0.0024 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 2.5805 L22: 1.7872
REMARK 3 L33: 1.4146 L12: -0.0911
REMARK 3 L13: -0.3588 L23: 1.0736
REMARK 3 S TENSOR
REMARK 3 S11: 0.1244 S12: -0.4471 S13: 0.1936
REMARK 3 S21: 0.1362 S22: -0.0610 S23: -0.0693
REMARK 3 S31: -0.0496 S32: 0.0429 S33: -0.0633
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 151 B 167
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1010 12.7438 -2.4481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1992 T22: 0.3782
REMARK 3 T33: 0.2230 T12: 0.0193
REMARK 3 T13: 0.0541 T23: -0.2450
REMARK 3 L TENSOR
REMARK 3 L11: 9.4094 L22: 7.9305
REMARK 3 L33: 5.2885 L12: -0.5887
REMARK 3 L13: -4.1355 L23: -3.8989
REMARK 3 S TENSOR
REMARK 3 S11: 0.2449 S12: -0.2802 S13: 0.2363
REMARK 3 S21: 0.4061 S22: -0.0780 S23: 0.4320
REMARK 3 S31: -0.3425 S32: -0.3214 S33: -0.1669
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 168 B 226
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1143 -3.6250 -13.2021
REMARK 3 T TENSOR
REMARK 3 T11: 0.0368 T22: 0.1041
REMARK 3 T33: 0.0102 T12: -0.0243
REMARK 3 T13: -0.0016 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 2.3230 L22: 1.1467
REMARK 3 L33: 0.9270 L12: 0.0454
REMARK 3 L13: -0.4381 L23: 0.4432
REMARK 3 S TENSOR
REMARK 3 S11: 0.1078 S12: -0.3648 S13: -0.0500
REMARK 3 S21: 0.0877 S22: -0.1042 S23: 0.0623
REMARK 3 S31: 0.0017 S32: -0.0508 S33: -0.0036
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2XTM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-OCT-10.
REMARK 100 THE PDBE ID CODE IS EBI-45739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54984
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% 2-PROPANOL, 30% GLYCEROL, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.44500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.90500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 92.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.44500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.90500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 ASN A 4
REMARK 465 GLU A 5
REMARK 465 HIS A 6
REMARK 465 SER A 7
REMARK 465 HIS A 8
REMARK 465 TRP A 9
REMARK 465 GLY A 10
REMARK 465 PRO A 11
REMARK 465 HIS A 12
REMARK 465 ALA A 13
REMARK 465 LYS A 14
REMARK 465 GLY A 15
REMARK 465 GLN A 16
REMARK 465 CYS A 17
REMARK 465 ALA A 18
REMARK 465 SER A 19
REMARK 465 ARG A 20
REMARK 465 GLY A 228
REMARK 465 PRO A 229
REMARK 465 VAL A 230
REMARK 465 GLY A 231
REMARK 465 SER A 232
REMARK 465 ASP A 233
REMARK 465 GLU A 234
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 ASN B 4
REMARK 465 GLU B 5
REMARK 465 HIS B 6
REMARK 465 SER B 7
REMARK 465 HIS B 8
REMARK 465 TRP B 9
REMARK 465 GLY B 10
REMARK 465 PRO B 11
REMARK 465 HIS B 12
REMARK 465 ALA B 13
REMARK 465 LYS B 14
REMARK 465 GLY B 15
REMARK 465 GLN B 16
REMARK 465 CYS B 17
REMARK 465 ALA B 18
REMARK 465 SER B 19
REMARK 465 ARG B 20
REMARK 465 LYS B 51
REMARK 465 LEU B 52
REMARK 465 GLY B 53
REMARK 465 SER B 54
REMARK 465 GLN B 55
REMARK 465 THR B 56
REMARK 465 LEU B 57
REMARK 465 CYS B 227
REMARK 465 GLY B 228
REMARK 465 PRO B 229
REMARK 465 VAL B 230
REMARK 465 GLY B 231
REMARK 465 SER B 232
REMARK 465 ASP B 233
REMARK 465 GLU B 234
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 ASN A 70 CG OD1 ND2
REMARK 470 ARG A 71 CZ NH1 NH2
REMARK 470 LYS A 93 CD CE NZ
REMARK 470 GLN A 124 OE1 NE2
REMARK 470 LYS A 166 CD CE NZ
REMARK 470 LYS A 170 CE NZ
REMARK 470 GLU A 197 CD OE1 OE2
REMARK 470 GLN A 223 OE1 NE2
REMARK 470 GLU B 49 CD OE1 OE2
REMARK 470 LYS B 59 CG CD CE NZ
REMARK 470 ASN B 70 CG OD1 ND2
REMARK 470 LYS B 85 CE NZ
REMARK 470 ASP B 86 CG OD1 OD2
REMARK 470 GLU B 89 OE1 OE2
REMARK 470 LYS B 93 CD CE NZ
REMARK 470 GLN B 114 CG CD OE1 NE2
REMARK 470 ARG B 117 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 121 CG CD OE1 NE2
REMARK 470 TYR B 159 CE1 CE2 CZ OH
REMARK 470 HIS B 161 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 164 CG OD1 OD2
REMARK 470 LYS B 166 CD CE NZ
REMARK 470 LYS B 170 CE NZ
REMARK 470 ASN B 183 CG OD1 ND2
REMARK 470 ARG B 185 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 187 CG CD OE1 OE2
REMARK 470 ASN B 190 CG OD1 ND2
REMARK 470 LYS B 196 CE NZ
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 86 -175.28 75.34
REMARK 500 ASN B 70 35.80 -94.77
REMARK 500 ARG B 117 55.37 -141.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1229 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2011 O
REMARK 620 2 HOH A2189 O 88.1
REMARK 620 3 HOH A2191 O 89.5 89.8
REMARK 620 4 SER A 36 OG 89.3 90.1 178.8
REMARK 620 5 GDP A1228 O3B 179.0 90.9 90.3 90.9
REMARK 620 6 HOH A2059 O 84.8 172.9 90.1 89.9 96.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1228 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 36 OG
REMARK 620 2 HOH B2015 O 89.9
REMARK 620 3 GDP B1227 O2B 93.3 102.4
REMARK 620 4 THR B 58 OG1 93.7 88.1 167.3
REMARK 620 5 HOH B2019 O 172.0 96.3 90.3 81.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A1228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B1227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1228
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XTN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GTP-BOUND HUMAN GIMAP2
REMARK 900 , AMINO ACID RESIDUES 1-234
REMARK 900 RELATED ID: 2XTO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GDP-BOUND HUMAN GIMAP2
REMARK 900 , AMINO ACID RESIDUES 21-260
REMARK 900 RELATED ID: 2XTP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NUCLEOTIDE-FREE HUMAN
REMARK 900 GIMAP2, AMINO ACID RESIDUES 1-260
DBREF 2XTM A 1 234 UNP Q9UG22 GIMA2_HUMAN 1 234
DBREF 2XTM B 1 234 UNP Q9UG22 GIMA2_HUMAN 1 234
SEQRES 1 A 234 MET ASP GLN ASN GLU HIS SER HIS TRP GLY PRO HIS ALA
SEQRES 2 A 234 LYS GLY GLN CYS ALA SER ARG SER GLU LEU ARG ILE ILE
SEQRES 3 A 234 LEU VAL GLY LYS THR GLY THR GLY LYS SER ALA ALA GLY
SEQRES 4 A 234 ASN SER ILE LEU ARG LYS GLN ALA PHE GLU SER LYS LEU
SEQRES 5 A 234 GLY SER GLN THR LEU THR LYS THR CYS SER LYS SER GLN
SEQRES 6 A 234 GLY SER TRP GLY ASN ARG GLU ILE VAL ILE ILE ASP THR
SEQRES 7 A 234 PRO ASP MET PHE SER TRP LYS ASP HIS CYS GLU ALA LEU
SEQRES 8 A 234 TYR LYS GLU VAL GLN ARG CYS TYR LEU LEU SER ALA PRO
SEQRES 9 A 234 GLY PRO HIS VAL LEU LEU LEU VAL THR GLN LEU GLY ARG
SEQRES 10 A 234 TYR THR SER GLN ASP GLN GLN ALA ALA GLN ARG VAL LYS
SEQRES 11 A 234 GLU ILE PHE GLY GLU ASP ALA MET GLY HIS THR ILE VAL
SEQRES 12 A 234 LEU PHE THR HIS LYS GLU ASP LEU ASN GLY GLY SER LEU
SEQRES 13 A 234 MET ASP TYR MET HIS ASP SER ASP ASN LYS ALA LEU SER
SEQRES 14 A 234 LYS LEU VAL ALA ALA CYS GLY GLY ARG ILE CYS ALA PHE
SEQRES 15 A 234 ASN ASN ARG ALA GLU GLY SER ASN GLN ASP ASP GLN VAL
SEQRES 16 A 234 LYS GLU LEU MET ASP CYS ILE GLU ASP LEU LEU MET GLU
SEQRES 17 A 234 LYS ASN GLY ASP HIS TYR THR ASN GLY LEU TYR SER LEU
SEQRES 18 A 234 ILE GLN ARG SER LYS CYS GLY PRO VAL GLY SER ASP GLU
SEQRES 1 B 234 MET ASP GLN ASN GLU HIS SER HIS TRP GLY PRO HIS ALA
SEQRES 2 B 234 LYS GLY GLN CYS ALA SER ARG SER GLU LEU ARG ILE ILE
SEQRES 3 B 234 LEU VAL GLY LYS THR GLY THR GLY LYS SER ALA ALA GLY
SEQRES 4 B 234 ASN SER ILE LEU ARG LYS GLN ALA PHE GLU SER LYS LEU
SEQRES 5 B 234 GLY SER GLN THR LEU THR LYS THR CYS SER LYS SER GLN
SEQRES 6 B 234 GLY SER TRP GLY ASN ARG GLU ILE VAL ILE ILE ASP THR
SEQRES 7 B 234 PRO ASP MET PHE SER TRP LYS ASP HIS CYS GLU ALA LEU
SEQRES 8 B 234 TYR LYS GLU VAL GLN ARG CYS TYR LEU LEU SER ALA PRO
SEQRES 9 B 234 GLY PRO HIS VAL LEU LEU LEU VAL THR GLN LEU GLY ARG
SEQRES 10 B 234 TYR THR SER GLN ASP GLN GLN ALA ALA GLN ARG VAL LYS
SEQRES 11 B 234 GLU ILE PHE GLY GLU ASP ALA MET GLY HIS THR ILE VAL
SEQRES 12 B 234 LEU PHE THR HIS LYS GLU ASP LEU ASN GLY GLY SER LEU
SEQRES 13 B 234 MET ASP TYR MET HIS ASP SER ASP ASN LYS ALA LEU SER
SEQRES 14 B 234 LYS LEU VAL ALA ALA CYS GLY GLY ARG ILE CYS ALA PHE
SEQRES 15 B 234 ASN ASN ARG ALA GLU GLY SER ASN GLN ASP ASP GLN VAL
SEQRES 16 B 234 LYS GLU LEU MET ASP CYS ILE GLU ASP LEU LEU MET GLU
SEQRES 17 B 234 LYS ASN GLY ASP HIS TYR THR ASN GLY LEU TYR SER LEU
SEQRES 18 B 234 ILE GLN ARG SER LYS CYS GLY PRO VAL GLY SER ASP GLU
HET GDP A1228 28
HET MG A1229 1
HET GOL A1230 6
HET GOL A1231 6
HET GOL A1232 6
HET GDP B1227 28
HET MG B1228 1
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 6 HOH *298(H2 O)
HELIX 1 1 GLY A 34 ARG A 44 1 11
HELIX 2 2 PRO A 79 TRP A 84 5 6
HELIX 3 3 ALA A 90 ALA A 103 1 14
HELIX 4 4 THR A 119 GLY A 134 1 16
HELIX 5 5 ASP A 136 GLY A 139 5 4
HELIX 6 6 HIS A 147 ASN A 152 5 6
HELIX 7 7 SER A 155 SER A 163 1 9
HELIX 8 8 ASN A 165 CYS A 175 1 11
HELIX 9 9 GLU A 187 LYS A 209 1 23
HELIX 10 10 ASN A 216 ARG A 224 1 9
HELIX 11 11 GLY B 34 ARG B 44 1 11
HELIX 12 12 PRO B 79 TRP B 84 5 6
HELIX 13 13 ALA B 90 ALA B 103 1 14
HELIX 14 14 THR B 119 GLY B 134 1 16
HELIX 15 15 ASP B 136 GLY B 139 5 4
HELIX 16 16 HIS B 147 ASN B 152 5 6
HELIX 17 17 SER B 155 SER B 163 1 9
HELIX 18 18 ASN B 165 CYS B 175 1 11
HELIX 19 19 GLU B 187 LYS B 209 1 23
HELIX 20 20 ASN B 216 SER B 225 1 10
SHEET 1 AA 6 SER A 62 TRP A 68 0
SHEET 2 AA 6 ARG A 71 ASP A 77 -1 O ARG A 71 N TRP A 68
SHEET 3 AA 6 GLU A 22 VAL A 28 1 O LEU A 23 N VAL A 74
SHEET 4 AA 6 VAL A 108 GLN A 114 1 O VAL A 108 N ILE A 26
SHEET 5 AA 6 THR A 141 THR A 146 1 O ILE A 142 N LEU A 111
SHEET 6 AA 6 ILE A 179 ALA A 181 1 O CYS A 180 N PHE A 145
SHEET 1 BA 6 SER B 62 TRP B 68 0
SHEET 2 BA 6 ARG B 71 ASP B 77 -1 O ARG B 71 N TRP B 68
SHEET 3 BA 6 GLU B 22 VAL B 28 1 O LEU B 23 N VAL B 74
SHEET 4 BA 6 VAL B 108 GLN B 114 1 O VAL B 108 N ILE B 26
SHEET 5 BA 6 THR B 141 THR B 146 1 O ILE B 142 N LEU B 111
SHEET 6 BA 6 ILE B 179 ALA B 181 1 O CYS B 180 N PHE B 145
LINK O3B GDP A1228 MG MG A1229 1555 1555 2.03
LINK MG MG A1229 O HOH A2011 1555 1555 2.13
LINK MG MG A1229 O HOH A2189 1555 1555 2.10
LINK MG MG A1229 O HOH A2191 1555 1555 2.10
LINK MG MG A1229 OG SER A 36 1555 1555 2.16
LINK MG MG A1229 O HOH A2059 1555 1555 2.17
LINK O2B GDP B1227 MG MG B1228 1555 1555 2.03
LINK MG MG B1228 O HOH B2015 1555 1555 1.98
LINK MG MG B1228 OG1 THR B 58 1555 1555 2.29
LINK MG MG B1228 O HOH B2019 1555 1555 2.18
LINK MG MG B1228 OG SER B 36 1555 1555 2.06
CISPEP 1 ALA A 103 PRO A 104 0 7.12
CISPEP 2 ALA B 103 PRO B 104 0 5.40
SITE 1 AC1 20 GLY A 32 THR A 33 GLY A 34 LYS A 35
SITE 2 AC1 20 SER A 36 ALA A 37 SER A 50 LYS A 51
SITE 3 AC1 20 LEU A 52 HIS A 147 GLU A 149 ASN A 184
SITE 4 AC1 20 ARG A 185 MG A1229 HOH A2114 HOH A2188
SITE 5 AC1 20 HOH A2189 HOH A2191 HOH A2193 HOH A2194
SITE 1 AC2 6 SER A 36 GDP A1228 HOH A2011 HOH A2059
SITE 2 AC2 6 HOH A2189 HOH A2191
SITE 1 AC3 9 GLU A 131 ILE A 132 GLY A 134 ASN A 216
SITE 2 AC3 9 GLY A 217 LEU A 218 GOL A1231 HOH A2195
SITE 3 AC3 9 HOH A2196
SITE 1 AC4 10 GLY A 217 GOL A1230 HOH A2197 HOH A2198
SITE 2 AC4 10 GLU B 131 ILE B 132 GLY B 134 ASN B 216
SITE 3 AC4 10 GLY B 217 LEU B 218
SITE 1 AC5 9 SER A 62 LYS A 63 ARG A 97 LEU A 101
SITE 2 AC5 9 HOH A2199 HOH A2200 GLU B 208 LYS B 209
SITE 3 AC5 9 HOH B2079
SITE 1 AC6 13 GLY B 32 THR B 33 GLY B 34 LYS B 35
SITE 2 AC6 13 SER B 36 ALA B 37 SER B 50 HIS B 147
SITE 3 AC6 13 GLU B 149 ASN B 183 ASN B 184 MG B1228
SITE 4 AC6 13 HOH B2019
SITE 1 AC7 5 SER B 36 THR B 58 GDP B1227 HOH B2015
SITE 2 AC7 5 HOH B2019
CRYST1 42.890 61.810 185.310 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023315 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016179 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005396 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
