HEADER ISOMERASE, PROTEIN BINDING 09-AUG-12 4GIV
TITLE CRYSTAL STRUCTURE OF A SMT FUSION PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
TITLE 2 WITH SURFACE MUTATION D44G FROM BURKHOLDERIA PSEUDOMALLEI COMPLEXED
TITLE 3 WITH CJ183
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3, PEPTIDYL-PROLYL CIS-TRANS
COMPND 3 ISOMERASE;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: Q12306 RESIDUES 13-98, Q3JK38 RESIDUES 2-113;
COMPND 6 EC: 5.2.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE, BURKHOLDERIA
SOURCE 3 PSEUDOMALLEI;
SOURCE 4 ORGANISM_TAXID: 559292, 320372;
SOURCE 5 STRAIN: 1710B, S288C;
SOURCE 6 GENE: BURPS1710B_A0907, SMT3, YDR510W, D9719.15;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28-HISSMT
KEYWDS SSGCID, ISOMERASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS
KEYWDS 2 CENTER FOR INFECTIOUS DISEASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 6 28-FEB-24 4GIV 1 REMARK SEQADV
REVDAT 5 11-OCT-17 4GIV 1 REMARK
REVDAT 4 12-JUL-17 4GIV 1 COMPND REMARK HETNAM FORMUL
REVDAT 3 19-MAR-14 4GIV 1 REMARK
REVDAT 2 12-MAR-14 4GIV 1 JRNL
REVDAT 1 05-SEP-12 4GIV 0
JRNL AUTH D.W.BEGLEY,D.FOX,D.JENNER,C.JULI,P.G.PIERCE,J.ABENDROTH,
JRNL AUTH 2 M.MURUTHI,K.SAFFORD,V.ANDERSON,K.ATKINS,S.R.BARNES,S.O.MOEN,
JRNL AUTH 3 A.C.RAYMOND,R.STACY,P.J.MYLER,B.L.STAKER,N.J.HARMER,
JRNL AUTH 4 I.H.NORVILLE,U.HOLZGRABE,M.SARKAR-TYSON,T.E.EDWARDS,
JRNL AUTH 5 D.D.LORIMER
JRNL TITL A STRUCTURAL BIOLOGY APPROACH ENABLES THE DEVELOPMENT OF
JRNL TITL 2 ANTIMICROBIALS TARGETING BACTERIAL IMMUNOPHILINS.
JRNL REF ANTIMICROB.AGENTS CHEMOTHER. V. 58 1458 2014
JRNL REFN ISSN 0066-4804
JRNL PMID 24366729
JRNL DOI 10.1128/AAC.01875-13
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15513
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 790
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) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1025
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2705
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.58000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : -1.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.98000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.496
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.287
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.172
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.569
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2805 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1831 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3802 ; 1.612 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4456 ; 1.392 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 373 ; 6.582 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;28.906 ;24.037
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 401 ;17.268 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.476 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 427 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3216 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 578 ; 0.002 ; 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 -78 A -44
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9838 -7.6512 68.5582
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.1665
REMARK 3 T33: 0.1872 T12: -0.0318
REMARK 3 T13: 0.0048 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.6582 L22: 7.0022
REMARK 3 L33: 5.0708 L12: -1.6432
REMARK 3 L13: 1.2208 L23: -3.0987
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: 0.1353 S13: -0.0047
REMARK 3 S21: -0.2178 S22: 0.0992 S23: 0.1772
REMARK 3 S31: 0.0930 S32: -0.0899 S33: -0.0411
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 -43 A -34
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7327 1.1674 60.5331
REMARK 3 T TENSOR
REMARK 3 T11: 0.3262 T22: 0.5640
REMARK 3 T33: 0.4642 T12: 0.0062
REMARK 3 T13: 0.0731 T23: 0.1403
REMARK 3 L TENSOR
REMARK 3 L11: 2.7465 L22: 10.3184
REMARK 3 L33: 6.4470 L12: 5.2021
REMARK 3 L13: 2.1778 L23: 4.9779
REMARK 3 S TENSOR
REMARK 3 S11: -0.4591 S12: 0.3142 S13: 0.1475
REMARK 3 S21: -0.8065 S22: 0.3166 S23: -0.0056
REMARK 3 S31: 0.0949 S32: 0.5747 S33: 0.1424
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 -33 A 0
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0534 0.9635 72.7934
REMARK 3 T TENSOR
REMARK 3 T11: 0.0204 T22: 0.1798
REMARK 3 T33: 0.2426 T12: 0.0182
REMARK 3 T13: 0.0173 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 2.7961 L22: 5.1659
REMARK 3 L33: 1.6558 L12: 1.8879
REMARK 3 L13: -0.2982 L23: -0.6853
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: 0.0206 S13: 0.2678
REMARK 3 S21: 0.1836 S22: 0.0706 S23: 0.0303
REMARK 3 S31: -0.1085 S32: -0.1676 S33: -0.0341
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 1 A 71
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1132 15.4218 49.0893
REMARK 3 T TENSOR
REMARK 3 T11: 0.2757 T22: 0.2469
REMARK 3 T33: 0.2598 T12: 0.0047
REMARK 3 T13: -0.0476 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.3542 L22: 1.2676
REMARK 3 L33: 2.7714 L12: -1.1382
REMARK 3 L13: -0.2164 L23: -0.1693
REMARK 3 S TENSOR
REMARK 3 S11: 0.1604 S12: 0.2180 S13: 0.0864
REMARK 3 S21: -0.3888 S22: -0.1809 S23: 0.0757
REMARK 3 S31: 0.0738 S32: 0.1218 S33: 0.0205
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 72 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0611 14.5877 50.7848
REMARK 3 T TENSOR
REMARK 3 T11: 0.2398 T22: 0.2071
REMARK 3 T33: 0.1981 T12: 0.0150
REMARK 3 T13: -0.0443 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 2.5683 L22: 2.3789
REMARK 3 L33: 2.6525 L12: 0.9160
REMARK 3 L13: -0.0498 L23: -0.4611
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: 0.1169 S13: 0.0016
REMARK 3 S21: -0.3594 S22: 0.0228 S23: 0.0596
REMARK 3 S31: 0.1638 S32: -0.1308 S33: -0.0026
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 -76 B -50
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8757 29.1507 12.9096
REMARK 3 T TENSOR
REMARK 3 T11: 0.5904 T22: 0.3340
REMARK 3 T33: 0.1997 T12: -0.0957
REMARK 3 T13: -0.1371 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 2.6836 L22: 4.0107
REMARK 3 L33: 2.5575 L12: -1.2894
REMARK 3 L13: 1.7197 L23: -3.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.2550 S12: -0.2202 S13: 0.3593
REMARK 3 S21: 0.1567 S22: -0.1515 S23: 0.2322
REMARK 3 S31: 0.0638 S32: -0.1109 S33: -0.1035
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 -49 B -37
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3832 21.8561 13.6296
REMARK 3 T TENSOR
REMARK 3 T11: 0.7392 T22: 0.3596
REMARK 3 T33: 0.2218 T12: 0.0560
REMARK 3 T13: -0.1981 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 6.2225 L22: 1.8780
REMARK 3 L33: 1.4892 L12: 0.5131
REMARK 3 L13: -2.9649 L23: 0.1264
REMARK 3 S TENSOR
REMARK 3 S11: 0.1235 S12: -0.4452 S13: -0.5756
REMARK 3 S21: 0.2975 S22: -0.3158 S23: -0.3481
REMARK 3 S31: 0.0143 S32: 0.1774 S33: 0.1922
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 -36 B 6
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5887 18.4010 8.4803
REMARK 3 T TENSOR
REMARK 3 T11: 0.5937 T22: 0.2948
REMARK 3 T33: 0.1883 T12: -0.0063
REMARK 3 T13: -0.1616 T23: -0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.2569 L22: 2.6128
REMARK 3 L33: 0.4444 L12: 0.7700
REMARK 3 L13: -0.2172 L23: -0.5412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0212 S12: -0.0033 S13: 0.0153
REMARK 3 S21: -0.3499 S22: -0.1000 S23: 0.2751
REMARK 3 S31: 0.2168 S32: -0.0084 S33: 0.1212
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 7 B 58
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8895 6.6157 28.1966
REMARK 3 T TENSOR
REMARK 3 T11: 0.4613 T22: 0.1774
REMARK 3 T33: 0.0892 T12: -0.0063
REMARK 3 T13: -0.0373 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 3.1754 L22: 3.1247
REMARK 3 L33: 2.3473 L12: 1.3009
REMARK 3 L13: -0.4049 L23: -0.7375
REMARK 3 S TENSOR
REMARK 3 S11: -0.2373 S12: 0.0902 S13: 0.2364
REMARK 3 S21: -0.2304 S22: 0.0278 S23: -0.2844
REMARK 3 S31: 0.1239 S32: 0.0531 S33: 0.2095
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 59 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3154 5.3998 31.4658
REMARK 3 T TENSOR
REMARK 3 T11: 0.3912 T22: 0.1499
REMARK 3 T33: 0.0598 T12: -0.0096
REMARK 3 T13: -0.0749 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 4.6038 L22: 2.4187
REMARK 3 L33: 4.3385 L12: -0.8710
REMARK 3 L13: -2.3228 L23: 0.3678
REMARK 3 S TENSOR
REMARK 3 S11: -0.2908 S12: -0.0241 S13: -0.1684
REMARK 3 S21: -0.1585 S22: 0.0816 S23: 0.3259
REMARK 3 S31: 0.1657 S32: -0.2285 S33: 0.2092
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: U VALUES: WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4GIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-12
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976484
REMARK 200 MONOCHROMATOR : SI(220) ASYMMETRIC CUT SINGLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16480
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.720
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: INTERNAL TRACKING NUMBER 232625A12.
REMARK 280 PUCK IBH5-9, JCSG_A8 OPTIMIZATION SCREEN. 50MM AMMONIUM FORMATE,
REMARK 280 30% PEG3,350, 25% ETHYLENE GLYCOL CRYO-PROTECTED.
REMARK 280 BUPSA.00130.A.D214, 20.00 MG/ML, CJ183 (EBSI2864), PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 42.21000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.21000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.25000
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 362 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -95
REMARK 465 GLY A -94
REMARK 465 HIS A -93
REMARK 465 HIS A -92
REMARK 465 HIS A -91
REMARK 465 HIS A -90
REMARK 465 HIS A -89
REMARK 465 HIS A -88
REMARK 465 SER A -87
REMARK 465 GLY A -86
REMARK 465 GLU A -85
REMARK 465 VAL A -84
REMARK 465 LYS A -83
REMARK 465 PRO A -82
REMARK 465 GLU A -81
REMARK 465 VAL A -80
REMARK 465 LYS A -79
REMARK 465 MET B -95
REMARK 465 GLY B -94
REMARK 465 HIS B -93
REMARK 465 HIS B -92
REMARK 465 HIS B -91
REMARK 465 HIS B -90
REMARK 465 HIS B -89
REMARK 465 HIS B -88
REMARK 465 SER B -87
REMARK 465 GLY B -86
REMARK 465 GLU B -85
REMARK 465 VAL B -84
REMARK 465 LYS B -83
REMARK 465 PRO B -82
REMARK 465 GLU B -81
REMARK 465 VAL B -80
REMARK 465 LYS B -79
REMARK 465 PRO B -78
REMARK 465 GLU B -77
REMARK 465 GLY B -67
REMARK 465 SER B -66
REMARK 465 ILE B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 20
REMARK 465 ALA B 21
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 SER A -65 OG
REMARK 470 LYS A -44 CG CD CE NZ
REMARK 470 LYS A -40 CG CD CE NZ
REMARK 470 GLU A -39 CG CD OE1 OE2
REMARK 470 ASP A -37 CG OD1 OD2
REMARK 470 SER A 19 OG
REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 41 CG CD OE1 NE2
REMARK 470 VAL A 97 CG1 CG2
REMARK 470 VAL A 113 CG1 CG2
REMARK 470 THR B -76 OG1 CG2
REMARK 470 ILE B -74 CG1 CG2 CD1
REMARK 470 ASN B -73 CG OD1 ND2
REMARK 470 LYS B -71 CG CD CE NZ
REMARK 470 ASP B -68 CG OD1 OD2
REMARK 470 ILE B -63 CG1 CG2 CD1
REMARK 470 LYS B -60 CG CD CE NZ
REMARK 470 ILE B -59 CG1 CG2 CD1
REMARK 470 LYS B -58 CG CD CE NZ
REMARK 470 LYS B -57 CG CD CE NZ
REMARK 470 ARG B -52 CG CD NE CZ NH1 NH2
REMARK 470 ARG B -51 CG CD NE CZ NH1 NH2
REMARK 470 LYS B -44 CG CD CE NZ
REMARK 470 ARG B -43 CG CD NE CZ NH1 NH2
REMARK 470 GLN B -42 CG CD OE1 NE2
REMARK 470 LYS B -40 CG CD CE NZ
REMARK 470 ASP B -37 CG OD1 OD2
REMARK 470 ASP B -30 CG OD1 OD2
REMARK 470 ILE B -28 CG1 CG2 CD1
REMARK 470 GLN B -25 CG CD OE1 NE2
REMARK 470 ASP B -23 CG OD1 OD2
REMARK 470 GLN B -22 CG CD OE1 NE2
REMARK 470 ASP B -16 CG OD1 OD2
REMARK 470 MET B -15 CG SD CE
REMARK 470 GLU B -14 CG CD OE1 OE2
REMARK 470 ASP B -13 CG OD1 OD2
REMARK 470 ASN B -12 CG OD1 ND2
REMARK 470 ILE B -10 CG1 CG2 CD1
REMARK 470 ILE B -9 CG1 CG2 CD1
REMARK 470 GLU B -8 CG CD OE1 OE2
REMARK 470 HIS B -6 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B -5 CG CD NE CZ NH1 NH2
REMARK 470 GLU B -4 CG CD OE1 OE2
REMARK 470 GLN B -3 CG CD OE1 NE2
REMARK 470 THR B 2 OG1 CG2
REMARK 470 LYS B 11 CG CD CE NZ
REMARK 470 SER B 19 OG
REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 37 CG CD1 CD2
REMARK 470 ASP B 39 CG OD1 OD2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 ASN B 50 CG OD1 ND2
REMARK 470 GLN B 71 CG CD OE1 NE2
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 VAL B 113 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A -75 CG HIS A -75 CD2 0.058
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A -30 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A -18 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER B 8 -19.75 -49.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 352 DISTANCE = 5.92 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 4GI A 201
REMARK 610 4GI B 300
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4GI A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4GI B 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2KEO RELATED DB: PDB
REMARK 900 RELATED ID: 2KO7 RELATED DB: PDB
REMARK 900 RELATED ID: 2L2S RELATED DB: PDB
REMARK 900 RELATED ID: 3VAW RELATED DB: PDB
REMARK 900 RELATED ID: 3UQB RELATED DB: PDB
REMARK 900 RELATED ID: 3UQA RELATED DB: PDB
REMARK 900 RELATED ID: 4DZ3 RELATED DB: PDB
REMARK 900 RELATED ID: 4DZ2 RELATED DB: PDB
REMARK 900 RELATED ID: 3UF8 RELATED DB: PDB
REMARK 900 RELATED ID: 4FN2 RELATED DB: PDB
REMARK 900 RELATED ID: 4G50 RELATED DB: PDB
REMARK 900 RELATED ID: 4GGQ RELATED DB: PDB
REMARK 900 RELATED ID: SSGCID-BUPSA.00130.A RELATED DB: TARGETTRACK
DBREF 4GIV A -85 0 UNP Q12306 SMT3_YEAST 13 98
DBREF 4GIV A 2 113 UNP Q3JK38 Q3JK38_BURP1 2 113
DBREF 4GIV B -85 0 UNP Q12306 SMT3_YEAST 13 98
DBREF 4GIV B 2 113 UNP Q3JK38 Q3JK38_BURP1 2 113
SEQADV 4GIV MET A -95 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV GLY A -94 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS A -93 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS A -92 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS A -91 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS A -90 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS A -89 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS A -88 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV SER A -87 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV GLY A -86 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV SER A 1 UNP Q12306 LINKER
SEQADV 4GIV GLY A 44 UNP Q3JK38 ASP 44 ENGINEERED MUTATION
SEQADV 4GIV MET B -95 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV GLY B -94 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS B -93 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS B -92 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS B -91 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS B -90 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS B -89 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV HIS B -88 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV SER B -87 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV GLY B -86 UNP Q12306 EXPRESSION TAG
SEQADV 4GIV SER B 1 UNP Q12306 LINKER
SEQADV 4GIV GLY B 44 UNP Q3JK38 ASP 44 ENGINEERED MUTATION
SEQRES 1 A 209 MET GLY HIS HIS HIS HIS HIS HIS SER GLY GLU VAL LYS
SEQRES 2 A 209 PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU LYS VAL
SEQRES 3 A 209 SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS
SEQRES 4 A 209 THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS
SEQRES 5 A 209 ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR
SEQRES 6 A 209 ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP
SEQRES 7 A 209 LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG
SEQRES 8 A 209 GLU GLN ILE GLY GLY SER THR VAL VAL THR THR GLU SER
SEQRES 9 A 209 GLY LEU LYS TYR GLU ASP LEU THR GLU GLY SER GLY ALA
SEQRES 10 A 209 GLU ALA ARG ALA GLY GLN THR VAL SER VAL HIS TYR THR
SEQRES 11 A 209 GLY TRP LEU THR ASP GLY GLN LYS PHE GLY SER SER LYS
SEQRES 12 A 209 ASP ARG ASN ASP PRO PHE ALA PHE VAL LEU GLY GLY GLY
SEQRES 13 A 209 MET VAL ILE LYS GLY TRP ASP GLU GLY VAL GLN GLY MET
SEQRES 14 A 209 LYS VAL GLY GLY VAL ARG ARG LEU THR ILE PRO PRO GLN
SEQRES 15 A 209 LEU GLY TYR GLY ALA ARG GLY ALA GLY GLY VAL ILE PRO
SEQRES 16 A 209 PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU LEU ASP
SEQRES 17 A 209 VAL
SEQRES 1 B 209 MET GLY HIS HIS HIS HIS HIS HIS SER GLY GLU VAL LYS
SEQRES 2 B 209 PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU LYS VAL
SEQRES 3 B 209 SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS
SEQRES 4 B 209 THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS
SEQRES 5 B 209 ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR
SEQRES 6 B 209 ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP
SEQRES 7 B 209 LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG
SEQRES 8 B 209 GLU GLN ILE GLY GLY SER THR VAL VAL THR THR GLU SER
SEQRES 9 B 209 GLY LEU LYS TYR GLU ASP LEU THR GLU GLY SER GLY ALA
SEQRES 10 B 209 GLU ALA ARG ALA GLY GLN THR VAL SER VAL HIS TYR THR
SEQRES 11 B 209 GLY TRP LEU THR ASP GLY GLN LYS PHE GLY SER SER LYS
SEQRES 12 B 209 ASP ARG ASN ASP PRO PHE ALA PHE VAL LEU GLY GLY GLY
SEQRES 13 B 209 MET VAL ILE LYS GLY TRP ASP GLU GLY VAL GLN GLY MET
SEQRES 14 B 209 LYS VAL GLY GLY VAL ARG ARG LEU THR ILE PRO PRO GLN
SEQRES 15 B 209 LEU GLY TYR GLY ALA ARG GLY ALA GLY GLY VAL ILE PRO
SEQRES 16 B 209 PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU LEU ASP
SEQRES 17 B 209 VAL
HET 4GI A 201 21
HET FMT A 202 3
HET FMT A 203 3
HET 4GI B 300 22
HETNAM 4GI 3-(PYRIDIN-3-YL)PROPYL (2S)-1-[(3-NITROPHENYL)
HETNAM 2 4GI SULFONYL]PIPERIDINE-2-CARBOXYLATE
HETNAM FMT FORMIC ACID
FORMUL 3 4GI 2(C20 H23 N3 O6 S)
FORMUL 4 FMT 2(C H2 O2)
FORMUL 7 HOH *84(H2 O)
HELIX 1 1 LEU A -53 GLN A -42 1 12
HELIX 2 2 GLU A -39 LEU A -35 5 5
HELIX 3 3 LYS A 47 ASN A 50 5 4
HELIX 4 4 ILE A 63 GLN A 71 1 9
HELIX 5 5 PRO A 84 GLY A 88 5 5
HELIX 6 6 LEU B -53 GLY B -41 1 13
HELIX 7 7 GLU B -39 ASP B -37 5 3
HELIX 8 8 ILE B 63 VAL B 70 1 8
HELIX 9 9 PRO B 84 GLY B 88 5 5
SHEET 1 A 5 GLU A -64 LYS A -58 0
SHEET 2 A 5 HIS A -75 SER A -69 -1 N VAL A -70 O ILE A -63
SHEET 3 A 5 ASP A -11 HIS A -6 1 O ILE A -9 N LYS A -71
SHEET 4 A 5 ARG A -34 TYR A -31 -1 N ARG A -34 O HIS A -6
SHEET 5 A 5 ILE A -28 ARG A -27 -1 O ILE A -28 N TYR A -31
SHEET 1 B 6 VAL A 4 THR A 5 0
SHEET 2 B 6 LYS A 11 THR A 16 -1 O TYR A 12 N VAL A 4
SHEET 3 B 6 VAL A 78 ILE A 83 -1 O ARG A 80 N GLU A 13
SHEET 4 B 6 LEU A 104 ASP A 112 -1 O LEU A 104 N ILE A 83
SHEET 5 B 6 THR A 28 LEU A 37 -1 N TRP A 36 O VAL A 105
SHEET 6 B 6 LYS A 42 SER A 45 -1 O PHE A 43 N GLY A 35
SHEET 1 C 6 VAL A 4 THR A 5 0
SHEET 2 C 6 LYS A 11 THR A 16 -1 O TYR A 12 N VAL A 4
SHEET 3 C 6 VAL A 78 ILE A 83 -1 O ARG A 80 N GLU A 13
SHEET 4 C 6 LEU A 104 ASP A 112 -1 O LEU A 104 N ILE A 83
SHEET 5 C 6 THR A 28 LEU A 37 -1 N TRP A 36 O VAL A 105
SHEET 6 C 6 PHE A 53 VAL A 56 -1 O PHE A 53 N VAL A 31
SHEET 1 D 5 ILE B -63 LYS B -58 0
SHEET 2 D 5 HIS B -75 SER B -69 -1 N ILE B -74 O ILE B -59
SHEET 3 D 5 ILE B -9 ARG B -5 1 O ILE B -9 N LYS B -71
SHEET 4 D 5 LEU B -35 TYR B -31 -1 N LEU B -32 O GLU B -8
SHEET 5 D 5 ILE B -28 ARG B -27 -1 O ILE B -28 N TYR B -31
SHEET 1 E 6 VAL B 3 THR B 5 0
SHEET 2 E 6 LYS B 11 THR B 16 -1 O TYR B 12 N VAL B 4
SHEET 3 E 6 VAL B 78 ILE B 83 -1 O ARG B 80 N GLU B 13
SHEET 4 E 6 LEU B 104 ASP B 112 -1 O PHE B 106 N LEU B 81
SHEET 5 E 6 THR B 28 LEU B 37 -1 N HIS B 32 O GLU B 109
SHEET 6 E 6 LYS B 42 SER B 45 -1 O GLY B 44 N GLY B 35
SHEET 1 F 6 VAL B 3 THR B 5 0
SHEET 2 F 6 LYS B 11 THR B 16 -1 O TYR B 12 N VAL B 4
SHEET 3 F 6 VAL B 78 ILE B 83 -1 O ARG B 80 N GLU B 13
SHEET 4 F 6 LEU B 104 ASP B 112 -1 O PHE B 106 N LEU B 81
SHEET 5 F 6 THR B 28 LEU B 37 -1 N HIS B 32 O GLU B 109
SHEET 6 F 6 PHE B 53 VAL B 56 -1 O PHE B 53 N VAL B 31
SITE 1 AC1 7 TYR A 33 PHE A 43 VAL A 62 TRP A 66
SITE 2 AC1 7 TYR A 89 PHE A 106 4GI B 300
SITE 1 AC2 7 ARG A -52 ALA A -24 ILE A -28 PRO A -54
SITE 2 AC2 7 ARG A -27 ASP A -23 HOH A 359
SITE 1 AC3 3 ARG A -5 LEU A 15 THR A 16
SITE 1 AC4 7 4GI A 201 TYR B 33 PHE B 43 VAL B 62
SITE 2 AC4 7 TRP B 66 TYR B 89 PHE B 106
CRYST1 84.420 32.500 151.380 90.00 97.52 90.00 C 1 2 1 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 0.011846 0.000000 0.001564 0.00000
SCALE2 0.000000 0.030769 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006663 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
