HEADER HYDROLASE/HYDROLASE INHIBITOR 11-JUL-14 4QUO
TITLE CRYSTAL STRUCTURE OF AMINOPEPTIDASE N IN COMPLEX WITH THE PHOSPHINIC
TITLE 2 DIPEPTIDE ANALOGUE LL-(R,S)-HPHEP[CH2]PHE(3-CH2NH2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE N;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MEMBRANE ALANYL AMINOPEPTIDASE;
COMPND 5 EC: 3.4.11.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS MC58;
SOURCE 3 ORGANISM_TAXID: 122586;
SOURCE 4 GENE: PEPN, NMBH4476_0804, NMH_0477;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS M1 FAMILY AMINOPEPTIDASE, METALLOPROTEASE, APN, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NOCEK,R.MULLIGAN,A.JOACHIMIAK,S.VASSILIOU,L.BERLICKI,A.MUCHA
REVDAT 6 06-DEC-23 4QUO 1 REMARK
REVDAT 5 20-SEP-23 4QUO 1 REMARK LINK
REVDAT 4 13-MAY-20 4QUO 1 AUTHOR SEQADV LINK
REVDAT 3 22-OCT-14 4QUO 1 JRNL
REVDAT 2 17-SEP-14 4QUO 1 JRNL LINK
REVDAT 1 10-SEP-14 4QUO 0
JRNL AUTH S.VASSILIOU,E.WEGLARZ-TOMCZAK,L.BERLICKI,M.PAWECZAK,B.NOCEK,
JRNL AUTH 2 R.MULLIGAN,A.JOACHIMIAK,A.MUCHA
JRNL TITL STRUCTURE-GUIDED, SINGLE-POINT MODIFICATIONS IN THE
JRNL TITL 2 PHOSPHINIC DIPEPTIDE STRUCTURE YIELD HIGHLY POTENT AND
JRNL TITL 3 SELECTIVE INHIBITORS OF NEUTRAL AMINOPEPTIDASES.
JRNL REF J.MED.CHEM. V. 57 8140 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25192493
JRNL DOI 10.1021/JM501071F
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 111770
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5953
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3042
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 33.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6847
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 1041
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.52000
REMARK 3 B12 (A**2) : 0.16000
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): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.942
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7264 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6827 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9874 ; 2.035 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15691 ; 0.938 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 897 ; 6.003 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 355 ;35.639 ;24.141
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1142 ;13.145 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;18.178 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1084 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8250 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1724 ; 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 : 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 3 A 85
REMARK 3 ORIGIN FOR THE GROUP (A): -64.9289 0.7470 -24.2494
REMARK 3 T TENSOR
REMARK 3 T11: 0.0236 T22: 0.0674
REMARK 3 T33: 0.0551 T12: 0.0092
REMARK 3 T13: -0.0005 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.4082 L22: 0.4227
REMARK 3 L33: 0.5252 L12: -0.0511
REMARK 3 L13: -0.3387 L23: -0.1564
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.0130 S13: 0.0199
REMARK 3 S21: 0.0244 S22: 0.0005 S23: 0.0357
REMARK 3 S31: -0.0252 S32: -0.0891 S33: 0.0275
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 86 A 194
REMARK 3 ORIGIN FOR THE GROUP (A): -52.0082 -1.4353 -34.8512
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0422
REMARK 3 T33: 0.0497 T12: -0.0072
REMARK 3 T13: 0.0031 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.3663 L22: 0.3088
REMARK 3 L33: 0.4123 L12: -0.0699
REMARK 3 L13: -0.0257 L23: 0.1710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: 0.0207 S13: 0.0477
REMARK 3 S21: -0.0293 S22: 0.0052 S23: 0.0029
REMARK 3 S31: -0.0262 S32: -0.0254 S33: 0.0173
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 195 A 444
REMARK 3 ORIGIN FOR THE GROUP (A): -43.0889 -21.1329 -23.7448
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0313
REMARK 3 T33: 0.0386 T12: -0.0111
REMARK 3 T13: 0.0081 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.1064 L22: 0.1064
REMARK 3 L33: 0.3539 L12: -0.0098
REMARK 3 L13: 0.0204 L23: 0.0140
REMARK 3 S TENSOR
REMARK 3 S11: -0.0016 S12: -0.0025 S13: -0.0011
REMARK 3 S21: 0.0105 S22: -0.0102 S23: -0.0037
REMARK 3 S31: 0.0717 S32: -0.0074 S33: 0.0118
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 445 A 519
REMARK 3 ORIGIN FOR THE GROUP (A): -37.9128 -41.0859 -0.7795
REMARK 3 T TENSOR
REMARK 3 T11: 0.2028 T22: 0.0855
REMARK 3 T33: 0.0957 T12: -0.1010
REMARK 3 T13: 0.0323 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.3217 L22: 1.5449
REMARK 3 L33: 0.3546 L12: -0.8683
REMARK 3 L13: -0.2637 L23: 0.5423
REMARK 3 S TENSOR
REMARK 3 S11: 0.0911 S12: -0.1010 S13: -0.1590
REMARK 3 S21: 0.1656 S22: -0.1890 S23: 0.0047
REMARK 3 S31: 0.1964 S32: -0.1135 S33: 0.0979
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 520 A 560
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6577 -37.3057 -4.8331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1828 T22: 0.0674
REMARK 3 T33: 0.0756 T12: -0.0220
REMARK 3 T13: 0.0289 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.9242 L22: 0.2895
REMARK 3 L33: 0.3941 L12: 0.2121
REMARK 3 L13: 0.1756 L23: -0.2226
REMARK 3 S TENSOR
REMARK 3 S11: 0.0457 S12: -0.0456 S13: -0.1537
REMARK 3 S21: -0.0272 S22: -0.1162 S23: -0.1012
REMARK 3 S31: 0.1444 S32: 0.0679 S33: 0.0705
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 : A 561 A 611
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3109 -27.8368 -5.1552
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.0667
REMARK 3 T33: 0.0434 T12: 0.0256
REMARK 3 T13: 0.0098 T23: 0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 0.9596 L22: 0.6213
REMARK 3 L33: 1.3071 L12: 0.1148
REMARK 3 L13: 0.1945 L23: -0.0850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: -0.1150 S13: -0.1217
REMARK 3 S21: 0.0487 S22: -0.0614 S23: -0.0535
REMARK 3 S31: 0.2895 S32: 0.0495 S33: 0.0355
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 : A 612 A 639
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9582 -15.3640 -0.6599
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.0828
REMARK 3 T33: 0.0322 T12: -0.0121
REMARK 3 T13: 0.0177 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.5552 L22: 1.3247
REMARK 3 L33: 1.7688 L12: -1.1347
REMARK 3 L13: -1.5559 L23: 1.3333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: -0.0994 S13: -0.0377
REMARK 3 S21: 0.0627 S22: -0.0966 S23: 0.0490
REMARK 3 S31: 0.0766 S32: 0.0502 S33: 0.0792
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 : A 640 A 699
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0201 -21.7485 -21.8180
REMARK 3 T TENSOR
REMARK 3 T11: 0.0596 T22: 0.0659
REMARK 3 T33: 0.0562 T12: 0.0409
REMARK 3 T13: 0.0146 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.0742 L22: 0.0598
REMARK 3 L33: 0.6319 L12: -0.2488
REMARK 3 L13: 0.5593 L23: -0.1429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0263 S12: 0.0622 S13: -0.0980
REMARK 3 S21: -0.0106 S22: -0.0240 S23: 0.0159
REMARK 3 S31: 0.1548 S32: 0.1364 S33: -0.0024
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 : A 700 A 780
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7950 -3.4857 -22.4760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0064 T22: 0.0496
REMARK 3 T33: 0.0562 T12: -0.0138
REMARK 3 T13: 0.0030 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.4193 L22: 0.5006
REMARK 3 L33: 0.5734 L12: -0.0218
REMARK 3 L13: -0.0512 L23: 0.3701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: 0.0438 S13: 0.0262
REMARK 3 S21: 0.0022 S22: 0.0103 S23: -0.0740
REMARK 3 S31: 0.0003 S32: 0.0649 S33: -0.0136
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 : A 781 A 867
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6125 0.3512 -4.9772
REMARK 3 T TENSOR
REMARK 3 T11: 0.0260 T22: 0.0378
REMARK 3 T33: 0.0462 T12: -0.0154
REMARK 3 T13: -0.0019 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.5998 L22: 0.2706
REMARK 3 L33: 0.8300 L12: -0.0991
REMARK 3 L13: 0.0950 L23: -0.1703
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: -0.0321 S13: 0.0033
REMARK 3 S21: 0.0121 S22: -0.0106 S23: 0.0210
REMARK 3 S31: -0.0443 S32: 0.0199 S33: 0.0105
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 4QUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000086535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-13
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 : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129700
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP, CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 2GTQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 111.85350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 64.57865
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.25633
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 111.85350
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 64.57865
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.25633
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 111.85350
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 64.57865
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.25633
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 129.15730
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 38.51267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 129.15730
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 38.51267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 129.15730
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 38.51267
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: 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 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 SER A 868
REMARK 465 ASN A 869
REMARK 465 ALA A 870
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 3 CG CD CE NZ
REMARK 470 LYS A 451 CD CE NZ
REMARK 470 ARG A 486 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 586 CG CD CE NZ
REMARK 470 LYS A 596 CG CD CE NZ
REMARK 470 ARG A 728 CD NE CZ NH1 NH2
REMARK 470 LYS A 856 CD 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 ASN A 63 47.46 37.87
REMARK 500 GLU A 260 31.25 -84.83
REMARK 500 LEU A 264 71.70 -151.42
REMARK 500 ALA A 331 149.89 -170.31
REMARK 500 ASN A 452 -130.43 67.17
REMARK 500 CYS A 830 -60.62 -29.10
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 ZN A 907 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 293 NE2
REMARK 620 2 HIS A 297 NE2 98.6
REMARK 620 3 GLU A 316 OE1 100.3 97.7
REMARK 620 4 3DZ A 901 OAO 109.9 148.0 91.4
REMARK 620 5 3DZ A 901 OAO 109.9 148.1 91.1 0.3
REMARK 620 6 3DZ A 901 OAN 96.0 97.1 156.0 66.4 66.7
REMARK 620 7 3DZ A 901 OAN 95.7 97.4 156.0 66.3 66.6 0.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3DZ A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3DZ A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 914
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 915
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 916
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 917
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 918
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QHP RELATED DB: PDB
REMARK 900 RELATED ID: 4QME RELATED DB: PDB
REMARK 900 RELATED ID: 2GTQ RELATED DB: PDB
DBREF 4QUO A 3 867 UNP E6MUM9 E6MUM9_NEIMH 3 867
SEQADV 4QUO SER A 868 UNP E6MUM9 EXPRESSION TAG
SEQADV 4QUO ASN A 869 UNP E6MUM9 EXPRESSION TAG
SEQADV 4QUO ALA A 870 UNP E6MUM9 EXPRESSION TAG
SEQRES 1 A 868 LYS THR VAL HIS TYR LEU LYS ASP TYR GLN THR PRO ALA
SEQRES 2 A 868 TYR HIS ILE LEU LYS THR ASP LEU HIS PHE ASP ILE ASN
SEQRES 3 A 868 GLU PRO GLN THR VAL VAL LYS SER ARG LEU THR VAL GLU
SEQRES 4 A 868 PRO GLN ARG VAL GLY GLU PRO LEU VAL LEU ASP GLY SER
SEQRES 5 A 868 ALA LYS LEU LEU SER VAL LYS ILE ASN GLY ALA ALA ALA
SEQRES 6 A 868 ASP TYR VAL LEU GLU GLY GLU THR LEU THR ILE ALA GLY
SEQRES 7 A 868 VAL PRO SER GLU ARG PHE THR VAL GLU VAL GLU THR GLU
SEQRES 8 A 868 ILE LEU PRO ALA GLU ASN LYS SER LEU MSE GLY LEU TYR
SEQRES 9 A 868 ALA SER GLY GLY ASN LEU PHE THR GLN CYS GLU PRO GLU
SEQRES 10 A 868 GLY PHE ARG LYS ILE THR PHE TYR ILE ASP ARG PRO ASP
SEQRES 11 A 868 VAL MSE SER LYS PHE THR THR THR ILE VAL ALA ASP LYS
SEQRES 12 A 868 LYS ARG TYR PRO VAL LEU LEU SER ASN GLY ASN LYS ILE
SEQRES 13 A 868 ASP GLY GLY GLU PHE SER ASP GLY ARG HIS TRP VAL LYS
SEQRES 14 A 868 TRP GLU ASP PRO PHE SER LYS PRO SER TYR LEU PHE ALA
SEQRES 15 A 868 LEU VAL ALA GLY ASP LEU ALA VAL THR GLU ASP TYR PHE
SEQRES 16 A 868 THR THR MSE SER GLY ARG ASN VAL LYS ILE GLU PHE TYR
SEQRES 17 A 868 THR THR GLU ALA ASP LYS PRO LYS VAL GLY PHE ALA VAL
SEQRES 18 A 868 GLU SER LEU LYS ASN ALA MSE LYS TRP ASP GLU THR ARG
SEQRES 19 A 868 PHE GLY LEU GLU TYR ASP LEU ASP ILE PHE MSE VAL VAL
SEQRES 20 A 868 ALA VAL GLY ASP PHE ASN MSE GLY ALA MSE GLU ASN LYS
SEQRES 21 A 868 GLY LEU ASN ILE PHE ASN THR LYS PHE VAL LEU ALA ASP
SEQRES 22 A 868 SER ARG THR ALA THR ASP THR ASP PHE GLU GLY ILE GLU
SEQRES 23 A 868 SER VAL VAL GLY HIS GLU TYR PHE HIS ASN TRP THR GLY
SEQRES 24 A 868 ASN ARG VAL THR CYS ARG ASP TRP PHE GLN LEU SER LEU
SEQRES 25 A 868 LYS GLU GLY LEU THR VAL PHE ARG ASP GLN GLU PHE SER
SEQRES 26 A 868 GLY ASP ARG ALA SER ARG ALA VAL ARG ARG ILE GLU ASN
SEQRES 27 A 868 ILE ARG LEU LEU ARG GLN HIS GLN PHE PRO GLU ASP ALA
SEQRES 28 A 868 GLY PRO THR ALA HIS PRO VAL ARG PRO ALA SER TYR GLU
SEQRES 29 A 868 GLU MSE ASN ASN PHE TYR THR MSE THR VAL TYR GLU LYS
SEQRES 30 A 868 GLY ALA GLU VAL VAL ARG MSE TYR HIS THR LEU LEU GLY
SEQRES 31 A 868 GLU GLU GLY PHE GLN LYS GLY MSE LYS LEU TYR PHE GLN
SEQRES 32 A 868 ARG HIS ASP GLY GLN ALA VAL THR CYS ASP ASP PHE ARG
SEQRES 33 A 868 ALA ALA MSE ALA ASP ALA ASN GLY ILE ASN LEU ASP GLN
SEQRES 34 A 868 PHE ALA LEU TRP TYR SER GLN ALA GLY THR PRO VAL LEU
SEQRES 35 A 868 GLU ALA GLU GLY ARG LEU LYS ASN ASN ILE PHE GLU LEU
SEQRES 36 A 868 THR VAL LYS GLN THR VAL PRO PRO THR PRO ASP MSE THR
SEQRES 37 A 868 ASP LYS GLN PRO MSE MSE ILE PRO VAL LYS VAL GLY LEU
SEQRES 38 A 868 LEU ASN ARG ASN GLY GLU ALA VAL ALA PHE ASP TYR GLN
SEQRES 39 A 868 GLY LYS ARG ALA THR GLU ALA VAL LEU LEU LEU THR GLU
SEQRES 40 A 868 ALA GLU GLN THR PHE LEU LEU GLU GLY VAL THR GLU ALA
SEQRES 41 A 868 VAL VAL PRO SER LEU LEU ARG GLY PHE SER ALA PRO VAL
SEQRES 42 A 868 HIS LEU ASN TYR PRO TYR SER ASP ASP ASP LEU LEU LEU
SEQRES 43 A 868 LEU LEU ALA HIS ASP SER ASP ALA PHE THR ARG TRP GLU
SEQRES 44 A 868 ALA ALA GLN THR LEU TYR ARG ARG ALA VAL ALA ALA ASN
SEQRES 45 A 868 LEU ALA THR LEU SER ASP GLY VAL GLU LEU PRO LYS HIS
SEQRES 46 A 868 GLU LYS LEU LEU ALA ALA VAL GLU LYS VAL ILE SER ASP
SEQRES 47 A 868 ASP LEU LEU ASP ASN ALA PHE LYS ALA LEU LEU LEU GLY
SEQRES 48 A 868 VAL PRO SER GLU ALA GLU LEU TRP ASP GLY ALA GLU ASN
SEQRES 49 A 868 ILE ASP PRO LEU ARG TYR HIS GLN ALA ARG GLU ALA LEU
SEQRES 50 A 868 LEU ASP THR LEU ALA VAL HIS PHE LEU PRO LYS TRP HIS
SEQRES 51 A 868 GLU LEU ASN ARG GLN ALA ALA LYS GLN GLU ASN GLN SER
SEQRES 52 A 868 TYR GLU TYR SER PRO GLU ALA ALA GLY TRP ARG THR LEU
SEQRES 53 A 868 ARG ASN VAL CYS ARG ALA PHE VAL LEU ARG ALA ASP PRO
SEQRES 54 A 868 ALA HIS ILE GLU THR VAL ALA GLU LYS TYR GLY GLU MSE
SEQRES 55 A 868 ALA GLN ASN MSE THR HIS GLU TRP GLY ILE LEU SER ALA
SEQRES 56 A 868 VAL ASN GLY ASN GLU SER ASP THR ARG ASN ARG LEU LEU
SEQRES 57 A 868 ALA GLN PHE ALA ASP LYS PHE SER ASP ASP ALA LEU VAL
SEQRES 58 A 868 MSE ASP LYS TYR PHE ALA LEU VAL GLY SER SER ARG ARG
SEQRES 59 A 868 SER ASP THR LEU GLN GLN VAL ARG THR ALA LEU GLN HIS
SEQRES 60 A 868 PRO LYS PHE SER LEU GLU ASN PRO ASN LYS ALA ARG SER
SEQRES 61 A 868 LEU ILE GLY SER PHE SER ARG ASN VAL PRO HIS PHE HIS
SEQRES 62 A 868 ALA GLU ASP GLY SER GLY TYR ARG PHE ILE ALA ASP LYS
SEQRES 63 A 868 VAL ILE GLU ILE ASP ARG PHE ASN PRO GLN VAL ALA ALA
SEQRES 64 A 868 ARG LEU VAL GLN ALA PHE ASN LEU CYS ASN LYS LEU GLU
SEQRES 65 A 868 PRO HIS ARG LYS ASN LEU VAL LYS GLN ALA LEU GLN ARG
SEQRES 66 A 868 ILE ARG ALA GLN GLU GLY LEU SER LYS ASP VAL GLY GLU
SEQRES 67 A 868 ILE VAL GLY LYS ILE LEU ASP SER ASN ALA
MODRES 4QUO MSE A 103 MET SELENOMETHIONINE
MODRES 4QUO MSE A 134 MET SELENOMETHIONINE
MODRES 4QUO MSE A 200 MET SELENOMETHIONINE
MODRES 4QUO MSE A 230 MET SELENOMETHIONINE
MODRES 4QUO MSE A 247 MET SELENOMETHIONINE
MODRES 4QUO MSE A 256 MET SELENOMETHIONINE
MODRES 4QUO MSE A 259 MET SELENOMETHIONINE
MODRES 4QUO MSE A 368 MET SELENOMETHIONINE
MODRES 4QUO MSE A 374 MET SELENOMETHIONINE
MODRES 4QUO MSE A 386 MET SELENOMETHIONINE
MODRES 4QUO MSE A 400 MET SELENOMETHIONINE
MODRES 4QUO MSE A 421 MET SELENOMETHIONINE
MODRES 4QUO MSE A 469 MET SELENOMETHIONINE
MODRES 4QUO MSE A 475 MET SELENOMETHIONINE
MODRES 4QUO MSE A 476 MET SELENOMETHIONINE
MODRES 4QUO MSE A 704 MET SELENOMETHIONINE
MODRES 4QUO MSE A 708 MET SELENOMETHIONINE
MODRES 4QUO MSE A 744 MET SELENOMETHIONINE
HET MSE A 103 16
HET MSE A 134 8
HET MSE A 200 8
HET MSE A 230 8
HET MSE A 247 8
HET MSE A 256 13
HET MSE A 259 8
HET MSE A 368 8
HET MSE A 374 8
HET MSE A 386 8
HET MSE A 400 8
HET MSE A 421 8
HET MSE A 469 8
HET MSE A 475 8
HET MSE A 476 8
HET MSE A 704 8
HET MSE A 708 8
HET MSE A 744 8
HET 3DZ A 901 54
HET GOL A 902 6
HET GOL A 903 6
HET GOL A 904 6
HET GOL A 905 6
HET IMD A 906 5
HET ZN A 907 1
HET 3DZ A 908 27
HET SO4 A 909 5
HET SO4 A 910 5
HET SO4 A 911 5
HET SO4 A 912 5
HET SO4 A 913 5
HET SO4 A 914 5
HET SO4 A 915 5
HET SO4 A 916 5
HET SO4 A 917 5
HET SO4 A 918 5
HETNAM MSE SELENOMETHIONINE
HETNAM 3DZ (2S)-2-[3-(AMINOMETHYL)BENZYL]-3-[(R)-[(1R)-1-AMINO-3-
HETNAM 2 3DZ PHENYLPROPYL](HYDROXY)PHOSPHORYL]PROPANOIC ACID
HETNAM GOL GLYCEROL
HETNAM IMD IMIDAZOLE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 2 3DZ 2(C20 H27 N2 O4 P)
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 IMD C3 H5 N2 1+
FORMUL 8 ZN ZN 2+
FORMUL 10 SO4 10(O4 S 2-)
FORMUL 20 HOH *1041(H2 O)
HELIX 1 1 LYS A 9 TYR A 11 5 3
HELIX 2 2 LEU A 95 ASN A 99 5 5
HELIX 3 3 GLY A 120 ILE A 124 5 5
HELIX 4 4 PRO A 179 PHE A 183 5 5
HELIX 5 5 ASP A 215 LYS A 218 5 4
HELIX 6 6 VAL A 219 GLY A 238 1 20
HELIX 7 7 LYS A 270 VAL A 272 5 3
HELIX 8 8 THR A 280 HIS A 297 1 18
HELIX 9 9 ASP A 308 PHE A 310 5 3
HELIX 10 10 GLN A 311 ALA A 331 1 21
HELIX 11 11 SER A 332 GLY A 354 1 23
HELIX 12 12 GLU A 367 TYR A 372 5 6
HELIX 13 13 THR A 373 ASP A 408 1 36
HELIX 14 14 THR A 413 ASN A 425 1 13
HELIX 15 15 LEU A 429 PHE A 432 5 4
HELIX 16 16 ALA A 433 GLN A 438 1 6
HELIX 17 17 SER A 542 ASP A 553 1 12
HELIX 18 18 ASP A 555 GLY A 581 1 27
HELIX 19 19 HIS A 587 ASP A 600 1 14
HELIX 20 20 ASP A 604 LEU A 612 1 9
HELIX 21 21 SER A 616 TRP A 621 1 6
HELIX 22 22 ASP A 628 PHE A 647 1 20
HELIX 23 23 PHE A 647 ASN A 663 1 17
HELIX 24 24 SER A 669 ASP A 690 1 22
HELIX 25 25 ALA A 692 LYS A 700 1 9
HELIX 26 26 LYS A 700 ALA A 705 1 6
HELIX 27 27 ASN A 707 ASN A 719 1 13
HELIX 28 28 SER A 723 PHE A 737 1 15
HELIX 29 29 ASP A 740 SER A 754 1 15
HELIX 30 30 ASP A 758 LEU A 767 1 10
HELIX 31 31 ASN A 776 ARG A 789 1 14
HELIX 32 32 ASN A 790 HIS A 795 1 6
HELIX 33 33 GLY A 799 ARG A 814 1 16
HELIX 34 34 ASN A 816 VAL A 824 1 9
HELIX 35 35 GLN A 825 ASN A 828 5 4
HELIX 36 36 LEU A 829 LEU A 833 5 5
HELIX 37 37 GLU A 834 ALA A 850 1 17
HELIX 38 38 SER A 855 ASP A 867 1 13
SHEET 1 A 2 HIS A 6 TYR A 7 0
SHEET 2 A 2 SER A 364 TYR A 365 -1 O TYR A 365 N HIS A 6
SHEET 1 B 8 ALA A 65 ALA A 66 0
SHEET 2 B 8 LYS A 56 ILE A 62 -1 N ILE A 62 O ALA A 65
SHEET 3 B 8 PHE A 86 ILE A 94 -1 O GLU A 91 N LEU A 58
SHEET 4 B 8 THR A 32 PRO A 42 -1 N LEU A 38 O VAL A 88
SHEET 5 B 8 TYR A 16 ILE A 27 -1 N LEU A 19 O THR A 39
SHEET 6 B 8 SER A 135 ASP A 144 1 O THR A 138 N LEU A 23
SHEET 7 B 8 ARG A 167 LYS A 178 -1 O TRP A 172 N THR A 139
SHEET 8 B 8 ASN A 156 GLU A 162 -1 N ASN A 156 O GLU A 173
SHEET 1 C 3 LEU A 49 ASP A 52 0
SHEET 2 C 3 THR A 75 ILE A 78 -1 O LEU A 76 N LEU A 51
SHEET 3 C 3 VAL A 70 GLU A 72 -1 N VAL A 70 O THR A 77
SHEET 1 D 4 GLY A 104 SER A 108 0
SHEET 2 D 4 ASN A 111 GLN A 115 -1 O PHE A 113 N TYR A 106
SHEET 3 D 4 LEU A 185 GLY A 188 -1 O ALA A 187 N LEU A 112
SHEET 4 D 4 VAL A 150 SER A 153 -1 N LEU A 152 O VAL A 186
SHEET 1 E 5 ALA A 191 THR A 198 0
SHEET 2 E 5 ASN A 204 THR A 211 -1 O VAL A 205 N PHE A 197
SHEET 3 E 5 ILE A 245 VAL A 251 1 O VAL A 248 N TYR A 210
SHEET 4 E 5 LEU A 264 ASN A 268 1 O PHE A 267 N VAL A 249
SHEET 5 E 5 ALA A 258 MSE A 259 -1 N MSE A 259 O ILE A 266
SHEET 1 F 2 THR A 305 CYS A 306 0
SHEET 2 F 2 ALA A 411 VAL A 412 1 O VAL A 412 N THR A 305
SHEET 1 G 4 GLU A 511 LEU A 516 0
SHEET 2 G 4 ILE A 454 THR A 462 -1 N PHE A 455 O LEU A 516
SHEET 3 G 4 VAL A 443 LYS A 451 -1 N GLU A 447 O THR A 458
SHEET 4 G 4 HIS A 536 ASN A 538 1 O ASN A 538 N ALA A 446
SHEET 1 H 3 ALA A 503 LEU A 507 0
SHEET 2 H 3 ILE A 477 LEU A 484 -1 N VAL A 479 O LEU A 505
SHEET 3 H 3 VAL A 524 LEU A 527 -1 O SER A 526 N GLY A 482
SHEET 1 I 2 PHE A 493 TYR A 495 0
SHEET 2 I 2 LYS A 498 ALA A 500 -1 O ALA A 500 N PHE A 493
LINK C LEU A 102 N AMSE A 103 1555 1555 1.34
LINK C LEU A 102 N BMSE A 103 1555 1555 1.33
LINK C AMSE A 103 N GLY A 104 1555 1555 1.35
LINK C BMSE A 103 N GLY A 104 1555 1555 1.31
LINK C VAL A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N SER A 135 1555 1555 1.32
LINK C THR A 199 N MSE A 200 1555 1555 1.31
LINK C MSE A 200 N SER A 201 1555 1555 1.33
LINK C ALA A 229 N MSE A 230 1555 1555 1.34
LINK C MSE A 230 N LYS A 231 1555 1555 1.33
LINK C PHE A 246 N MSE A 247 1555 1555 1.31
LINK C MSE A 247 N VAL A 248 1555 1555 1.34
LINK C ASN A 255 N AMSE A 256 1555 1555 1.33
LINK C AMSE A 256 N GLY A 257 1555 1555 1.33
LINK C ALA A 258 N MSE A 259 1555 1555 1.32
LINK C MSE A 259 N GLU A 260 1555 1555 1.33
LINK C GLU A 367 N MSE A 368 1555 1555 1.35
LINK C MSE A 368 N ASN A 369 1555 1555 1.34
LINK C THR A 373 N MSE A 374 1555 1555 1.32
LINK C MSE A 374 N THR A 375 1555 1555 1.33
LINK C ARG A 385 N MSE A 386 1555 1555 1.35
LINK C MSE A 386 N TYR A 387 1555 1555 1.34
LINK C GLY A 399 N MSE A 400 1555 1555 1.33
LINK C MSE A 400 N LYS A 401 1555 1555 1.32
LINK C ALA A 420 N MSE A 421 1555 1555 1.34
LINK C MSE A 421 N ALA A 422 1555 1555 1.32
LINK C ASP A 468 N MSE A 469 1555 1555 1.34
LINK C MSE A 469 N THR A 470 1555 1555 1.34
LINK C PRO A 474 N MSE A 475 1555 1555 1.31
LINK C MSE A 475 N MSE A 476 1555 1555 1.33
LINK C MSE A 476 N ILE A 477 1555 1555 1.33
LINK C GLU A 703 N MSE A 704 1555 1555 1.33
LINK C MSE A 704 N ALA A 705 1555 1555 1.33
LINK C ASN A 707 N MSE A 708 1555 1555 1.33
LINK C MSE A 708 N THR A 709 1555 1555 1.33
LINK C VAL A 743 N MSE A 744 1555 1555 1.33
LINK C MSE A 744 N ASP A 745 1555 1555 1.33
LINK NE2 HIS A 293 ZN ZN A 907 1555 1555 2.13
LINK NE2 HIS A 297 ZN ZN A 907 1555 1555 2.12
LINK OE1 GLU A 316 ZN ZN A 907 1555 1555 1.97
LINK OAOB3DZ A 901 ZN ZN A 907 1555 1555 2.17
LINK OAOA3DZ A 901 ZN ZN A 907 1555 1555 2.19
LINK OANB3DZ A 901 ZN ZN A 907 1555 1555 2.19
LINK OANA3DZ A 901 ZN ZN A 907 1555 1555 2.23
CISPEP 1 GLU A 29 PRO A 30 0 -0.67
CISPEP 2 GLU A 117 PRO A 118 0 0.05
SITE 1 AC1 17 GLN A 115 GLU A 117 MSE A 256 GLY A 257
SITE 2 AC1 17 ALA A 258 GLU A 260 VAL A 290 HIS A 293
SITE 3 AC1 17 GLU A 294 HIS A 297 LYS A 315 GLU A 316
SITE 4 AC1 17 ASP A 323 TYR A 377 ZN A 907 HOH A1210
SITE 5 AC1 17 HOH A1562
SITE 1 AC2 6 ASP A 604 ASN A 605 ALA A 606 GLU A 671
SITE 2 AC2 6 TRP A 675 HOH A1948
SITE 1 AC3 5 SER A 542 ASP A 543 ASP A 544 LYS A 589
SITE 2 AC3 5 HOH A1763
SITE 1 AC4 9 THR A 282 TRP A 712 HOH A1090 HOH A1299
SITE 2 AC4 9 HOH A1668 HOH A1685 HOH A1793 HOH A1859
SITE 3 AC4 9 HOH A1914
SITE 1 AC5 2 PHE A 163 SER A 164
SITE 1 AC6 2 ASP A 22 ARG A 37
SITE 1 AC7 4 HIS A 293 HIS A 297 GLU A 316 3DZ A 901
SITE 1 AC8 17 ASN A 156 PRO A 175 PHE A 176 ARG A 203
SITE 2 AC8 17 ASN A 204 TYR A 241 ASP A 242 LEU A 243
SITE 3 AC8 17 ASP A 244 HOH A1026 HOH A1140 HOH A1488
SITE 4 AC8 17 HOH A1553 HOH A1882 HOH A1894 HOH A1931
SITE 5 AC8 17 HOH A2025
SITE 1 AC9 8 MSE A 469 THR A 470 ASP A 471 HOH A1083
SITE 2 AC9 8 HOH A1225 HOH A1618 HOH A1656 HOH A1682
SITE 1 BC1 7 THR A 565 ARG A 568 ARG A 569 HOH A1584
SITE 2 BC1 7 HOH A1727 HOH A1854 HOH A1866
SITE 1 BC2 4 ARG A 449 LEU A 450 HOH A1659 HOH A1709
SITE 1 BC3 8 ALA A 191 VAL A 192 ASN A 831 LYS A 838
SITE 2 BC3 8 LYS A 842 HOH A1196 HOH A1441 HOH A1490
SITE 1 BC4 2 ARG A 499 HOH A1977
SITE 1 BC5 6 ARG A 636 ARG A 755 HOH A1117 HOH A1847
SITE 2 BC5 6 HOH A1869 HOH A1875
SITE 1 BC6 4 LYS A 3 GLY A 161 GLU A 162 HOH A1198
SITE 1 BC7 4 ALA A 331 SER A 332 HOH A1407 HOH A1767
SITE 1 BC8 2 LEU A 402 ARG A 406
SITE 1 BC9 3 GLU A 521 ALA A 522 HOH A1940
CRYST1 223.707 223.707 57.769 90.00 90.00 120.00 H 3 9
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 0.004470 0.002581 0.000000 0.00000
SCALE2 0.000000 0.005162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017310 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
