HEADER LYASE 17-JAN-07 2OKJ
TITLE THE X-RAY CRYSTAL STRUCTURE OF THE 67KDA ISOFORM OF
TITLE 2 GLUTAMIC ACID DECARBOXYLASE (GAD67)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DECARBOXYLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUTAMATE DECARBOXYLASE 67 KDA ISOFORM, GAD-67,
COMPND 5 67 KDA GLUTAMIC ACID DECARBOXYLASE;
COMPND 6 EC: 4.1.1.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GAD1, GAD, GAD67;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: YRD-15;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PRJ
KEYWDS PLP-DEPENDENT DECARBOXYLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BUCKLE,G.FENALTI,R.H.P.LAW,J.C.WHISSTOCK
REVDAT 3 24-FEB-09 2OKJ 1 VERSN
REVDAT 2 24-APR-07 2OKJ 1 JRNL
REVDAT 1 27-MAR-07 2OKJ 0
JRNL AUTH G.FENALTI,R.H.P.LAW,A.M.BUCKLE,C.LANGENDORF,K.TUCK,
JRNL AUTH 2 C.J.ROSADO,N.G.FAUX,K.MAHMOOD,C.S.HAMPE,J.P.BANGA,
JRNL AUTH 3 M.WILCE,J.SCHMIDBERGER,J.ROSSJOHN,O.EL-KABBANI,
JRNL AUTH 4 R.N.PIKE,A.I.SMITH,I.R.MACKAY,M.J.ROWLEY,
JRNL AUTH 5 J.C.WHISSTOCK
JRNL TITL GABA PRODUCTION BY GLUTAMIC ACID DECARBOXYLASE IS
JRNL TITL 2 REGULATED BY A DYNAMIC CATALYTIC LOOP.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 14 280 2007
JRNL REFN ISSN 1545-9993
JRNL PMID 17384644
JRNL DOI 10.1038/NSMB1228
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 97.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 42271
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2118
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1955
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7919
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 359
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.88000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.486
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.242
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8120 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10980 ; 1.148 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1003 ; 5.554 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 360 ;35.656 ;24.250
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1390 ;15.429 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;15.647 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1187 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6129 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4039 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5638 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 488 ; 0.124 ; 0.200
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): 41 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.098 ; 0.200
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): 5139 ; 0.864 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7999 ; 1.528 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3435 ; 2.294 ; 7.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2981 ; 3.534 ;10.000
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 : 25
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 98 A 106 1
REMARK 3 1 B 98 B 106 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 71 ; 0.020 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 71 ; 0.050 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 113 A 138 1
REMARK 3 1 B 113 B 138 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 212 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 2 A (A**2): 212 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 139 A 149 4
REMARK 3 1 B 139 B 149 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 97 ; 0.180 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 97 ; 0.300 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 158 A 172 1
REMARK 3 1 B 158 B 172 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 117 ; 0.020 ; 0.050
REMARK 3 TIGHT THERMAL 4 A (A**2): 117 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 174 A 239 1
REMARK 3 1 B 174 B 239 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 529 ; 0.020 ; 0.050
REMARK 3 TIGHT THERMAL 5 A (A**2): 529 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 245 A 278 4
REMARK 3 1 B 245 B 278 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 6 A (A): 256 ; 0.130 ; 0.500
REMARK 3 MEDIUM THERMAL 6 A (A**2): 256 ; 0.360 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 284 A 286 4
REMARK 3 1 B 284 B 286 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 7 A (A): 26 ; 0.120 ; 0.500
REMARK 3 MEDIUM THERMAL 7 A (A**2): 26 ; 0.460 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 287 A 301 1
REMARK 3 1 B 287 B 301 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 A (A): 111 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 8 A (A**2): 111 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 302 A 319 1
REMARK 3 1 B 302 B 319 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 A (A): 137 ; 0.020 ; 0.050
REMARK 3 TIGHT THERMAL 9 A (A**2): 137 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 321 A 340 4
REMARK 3 1 B 321 B 340 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 10 A (A): 158 ; 0.190 ; 0.500
REMARK 3 MEDIUM THERMAL 10 A (A**2): 158 ; 0.350 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 341 A 404 1
REMARK 3 1 B 341 B 404 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 A (A): 501 ; 0.020 ; 0.050
REMARK 3 TIGHT THERMAL 11 A (A**2): 501 ; 0.050 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 406 A 410 1
REMARK 3 1 B 406 B 410 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 A (A): 35 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 12 A (A**2): 35 ; 0.050 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 411 A 412 4
REMARK 3 1 B 411 B 412 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 13 A (A): 14 ; 0.080 ; 0.500
REMARK 3 MEDIUM THERMAL 13 A (A**2): 14 ; 0.390 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 413 A 430 1
REMARK 3 1 B 413 B 430 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 14 A (A): 131 ; 0.020 ; 0.050
REMARK 3 TIGHT THERMAL 14 A (A**2): 131 ; 0.050 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 449 A 481 1
REMARK 3 1 B 449 B 481 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 15 A (A): 270 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 15 A (A**2): 270 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 483 A 517 1
REMARK 3 1 B 483 B 517 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 16 A (A): 296 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 16 A (A**2): 296 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 17
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 518 A 523 6
REMARK 3 1 B 518 B 523 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 17 A (A): 49 ; 0.190 ; 5.000
REMARK 3 LOOSE THERMAL 17 A (A**2): 49 ; 3.310 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 18
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 531 A 538 4
REMARK 3 1 B 531 B 538 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 18 A (A): 62 ; 0.150 ; 0.500
REMARK 3 MEDIUM THERMAL 18 A (A**2): 62 ; 0.320 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 19
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 539 A 555 1
REMARK 3 1 B 539 B 555 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 19 A (A): 115 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 19 A (A**2): 115 ; 0.030 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 20
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 556 A 566 4
REMARK 3 1 B 556 B 566 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 20 A (A): 93 ; 0.090 ; 0.500
REMARK 3 MEDIUM THERMAL 20 A (A**2): 93 ; 0.300 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 21
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 567 A 573 1
REMARK 3 1 B 567 B 573 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 21 A (A): 55 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 21 A (A**2): 55 ; 0.040 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 22
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 574 A 587 4
REMARK 3 1 B 574 B 587 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 22 A (A): 106 ; 0.130 ; 0.500
REMARK 3 MEDIUM THERMAL 22 A (A**2): 106 ; 0.300 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 23
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 588 A 593 6
REMARK 3 1 B 588 B 593 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 23 A (A): 46 ; 0.460 ; 5.000
REMARK 3 LOOSE THERMAL 23 A (A**2): 46 ; 1.590 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 24
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 432 A 438 6
REMARK 3 1 B 432 B 438 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 24 A (A): 56 ; 0.660 ; 5.000
REMARK 3 LOOSE THERMAL 24 A (A**2): 56 ; 1.570 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 25
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 405 A 405 1
REMARK 3 1 B 405 B 405 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 25 A (A): 24 ; 0.300 ; 0.050
REMARK 3 TIGHT THERMAL 25 A (A**2): 24 ; 0.060 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2OKJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-07.
REMARK 100 THE RCSB ID CODE IS RCSB041250.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42284
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 97.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.19400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1JS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG8,000, 100 MM MES, PH 6.3,
REMARK 280 10 MM 2-MERCAPTOETHANOL AND 20 MM CACL2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 31.36950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THE BIOLOGICAL UNIT CORRESPONDS TO THE DIMER IN THE
REMARK 300 ASYMMETRIC UNIT.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 LEU A 594
REMARK 465 HIS A 595
REMARK 465 HIS A 596
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 THR A 93 OG1 CG2
REMARK 470 SER A 96 OG
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 GLU A 111 CB CG CD OE1 OE2
REMARK 470 LYS A 130 CD CE NZ
REMARK 470 LYS A 137 CE NZ
REMARK 470 GLU A 152 CD OE1 OE2
REMARK 470 LYS A 334 CD CE NZ
REMARK 470 GLU A 364 CD OE1 OE2
REMARK 470 LEU A 411 CG CD1 CD2
REMARK 470 GLU A 498 CG CD OE1 OE2
REMARK 470 GLU A 507 CD OE1 OE2
REMARK 470 VAL A 525 CG1 CG2
REMARK 470 GLN A 530 CG CD OE1 NE2
REMARK 470 ARG A 532 NE CZ NH1 NH2
REMARK 470 GLU A 533 CG CD OE1 OE2
REMARK 470 GLU A 548 CD OE1 OE2
REMARK 470 ASP A 593 CG OD1 OD2
REMARK 470 THR B 93 OG1 CG2
REMARK 470 LYS B 107 CG CD CE NZ
REMARK 470 ASN B 108 CG OD1 ND2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 LYS B 130 CE NZ
REMARK 470 SER B 135 OG
REMARK 470 LEU B 148 O
REMARK 470 GLU B 152 CG CD OE1 OE2
REMARK 470 GLN B 333 CD OE1 NE2
REMARK 470 GLU B 498 CG CD OE1 OE2
REMARK 470 GLU B 507 CD OE1 OE2
REMARK 470 SER B 528 OG
REMARK 470 GLN B 530 CG CD OE1 NE2
REMARK 470 GLU B 533 CG CD OE1 OE2
REMARK 470 LYS B 534 CG CD CE NZ
REMARK 470 GLU B 548 CG CD OE1 OE2
REMARK 470 GLU B 585 CD OE1 OE2
REMARK 470 ASP B 593 CG OD1 OD2
REMARK 470 HIS B 596 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CG ABU B 1002 C1 PLZ B 2001 2.12
REMARK 500 CD ABU B 1002 O4 PLZ B 2001 2.15
REMARK 500 CG ABU B 1002 C5 PLZ B 2001 2.18
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 ASP A 94 -95.35 55.36
REMARK 500 ASN A 210 70.83 39.12
REMARK 500 ALA A 219 54.63 -141.36
REMARK 500 ASP A 243 -142.81 57.20
REMARK 500 PRO A 321 -3.39 -59.40
REMARK 500 ASP A 323 -80.42 65.12
REMARK 500 PHE A 339 -14.58 -150.87
REMARK 500 ALA A 345 7.04 92.63
REMARK 500 VAL A 349 -65.30 -93.58
REMARK 500 TYR A 434 83.18 69.03
REMARK 500 LEU A 435 76.56 -170.26
REMARK 500 PHE A 436 96.45 34.56
REMARK 500 GLN A 437 80.89 62.60
REMARK 500 ASP A 439 41.21 -95.29
REMARK 500 CYS A 455 -85.05 -96.93
REMARK 500 HIS A 510 -153.66 -120.88
REMARK 500 VAL A 525 -75.47 -134.69
REMARK 500 ASN A 564 124.60 -38.05
REMARK 500 SER A 571 -4.63 -141.31
REMARK 500 GLN A 592 54.43 -114.05
REMARK 500 ASP B 94 -82.87 -97.62
REMARK 500 GLU B 152 92.94 -163.01
REMARK 500 ALA B 345 5.20 93.65
REMARK 500 VAL B 349 -66.16 -95.39
REMARK 500 TYR B 434 -42.74 121.99
REMARK 500 GLN B 437 74.11 85.74
REMARK 500 CYS B 455 -86.69 -96.36
REMARK 500 HIS B 510 -153.80 -121.43
REMARK 500 PRO B 526 -147.35 -100.65
REMARK 500 SER B 571 -3.83 -142.06
REMARK 500 ASP B 593 26.14 -143.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 322 ASP A 323 54.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABU A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABU B 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLZ B 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OKK RELATED DB: PDB
DBREF 2OKJ A 93 594 UNP Q99259 DCE1_HUMAN 93 594
DBREF 2OKJ B 93 594 UNP Q99259 DCE1_HUMAN 93 594
SEQADV 2OKJ LLP A 405 UNP Q99259 LYS 405 MODIFIED RESIDUE
SEQADV 2OKJ HIS A 595 UNP Q99259 EXPRESSION TAG
SEQADV 2OKJ HIS A 596 UNP Q99259 EXPRESSION TAG
SEQADV 2OKJ LLP B 405 UNP Q99259 LYS 405 MODIFIED RESIDUE
SEQADV 2OKJ HIS B 595 UNP Q99259 EXPRESSION TAG
SEQADV 2OKJ HIS B 596 UNP Q99259 EXPRESSION TAG
SEQRES 1 A 504 THR ASP PHE SER ASN LEU PHE ALA ARG ASP LEU LEU PRO
SEQRES 2 A 504 ALA LYS ASN GLY GLU GLU GLN THR VAL GLN PHE LEU LEU
SEQRES 3 A 504 GLU VAL VAL ASP ILE LEU LEU ASN TYR VAL ARG LYS THR
SEQRES 4 A 504 PHE ASP ARG SER THR LYS VAL LEU ASP PHE HIS HIS PRO
SEQRES 5 A 504 HIS GLN LEU LEU GLU GLY MET GLU GLY PHE ASN LEU GLU
SEQRES 6 A 504 LEU SER ASP HIS PRO GLU SER LEU GLU GLN ILE LEU VAL
SEQRES 7 A 504 ASP CYS ARG ASP THR LEU LYS TYR GLY VAL ARG THR GLY
SEQRES 8 A 504 HIS PRO ARG PHE PHE ASN GLN LEU SER THR GLY LEU ASP
SEQRES 9 A 504 ILE ILE GLY LEU ALA GLY GLU TRP LEU THR SER THR ALA
SEQRES 10 A 504 ASN THR ASN MET PHE THR TYR GLU ILE ALA PRO VAL PHE
SEQRES 11 A 504 VAL LEU MET GLU GLN ILE THR LEU LYS LYS MET ARG GLU
SEQRES 12 A 504 ILE VAL GLY TRP SER SER LYS ASP GLY ASP GLY ILE PHE
SEQRES 13 A 504 SER PRO GLY GLY ALA ILE SER ASN MET TYR SER ILE MET
SEQRES 14 A 504 ALA ALA ARG TYR LYS TYR PHE PRO GLU VAL LYS THR LYS
SEQRES 15 A 504 GLY MET ALA ALA VAL PRO LYS LEU VAL LEU PHE THR SER
SEQRES 16 A 504 GLU GLN SER HIS TYR SER ILE LYS LYS ALA GLY ALA ALA
SEQRES 17 A 504 LEU GLY PHE GLY THR ASP ASN VAL ILE LEU ILE LYS CYS
SEQRES 18 A 504 ASN GLU ARG GLY LYS ILE ILE PRO ALA ASP PHE GLU ALA
SEQRES 19 A 504 LYS ILE LEU GLU ALA LYS GLN LYS GLY TYR VAL PRO PHE
SEQRES 20 A 504 TYR VAL ASN ALA THR ALA GLY THR THR VAL TYR GLY ALA
SEQRES 21 A 504 PHE ASP PRO ILE GLN GLU ILE ALA ASP ILE CYS GLU LYS
SEQRES 22 A 504 TYR ASN LEU TRP LEU HIS VAL ASP ALA ALA TRP GLY GLY
SEQRES 23 A 504 GLY LEU LEU MET SER ARG LYS HIS ARG HIS LYS LEU ASN
SEQRES 24 A 504 GLY ILE GLU ARG ALA ASN SER VAL THR TRP ASN PRO HIS
SEQRES 25 A 504 LLP MET MET GLY VAL LEU LEU GLN CYS SER ALA ILE LEU
SEQRES 26 A 504 VAL LYS GLU LYS GLY ILE LEU GLN GLY CYS ASN GLN MET
SEQRES 27 A 504 CYS ALA GLY TYR LEU PHE GLN PRO ASP LYS GLN TYR ASP
SEQRES 28 A 504 VAL SER TYR ASP THR GLY ASP LYS ALA ILE GLN CYS GLY
SEQRES 29 A 504 ARG HIS VAL ASP ILE PHE LYS PHE TRP LEU MET TRP LYS
SEQRES 30 A 504 ALA LYS GLY THR VAL GLY PHE GLU ASN GLN ILE ASN LYS
SEQRES 31 A 504 CYS LEU GLU LEU ALA GLU TYR LEU TYR ALA LYS ILE LYS
SEQRES 32 A 504 ASN ARG GLU GLU PHE GLU MET VAL PHE ASN GLY GLU PRO
SEQRES 33 A 504 GLU HIS THR ASN VAL CYS PHE TRP TYR ILE PRO GLN SER
SEQRES 34 A 504 LEU ARG GLY VAL PRO ASP SER PRO GLN ARG ARG GLU LYS
SEQRES 35 A 504 LEU HIS LYS VAL ALA PRO LYS ILE LYS ALA LEU MET MET
SEQRES 36 A 504 GLU SER GLY THR THR MET VAL GLY TYR GLN PRO GLN GLY
SEQRES 37 A 504 ASP LYS ALA ASN PHE PHE ARG MET VAL ILE SER ASN PRO
SEQRES 38 A 504 ALA ALA THR GLN SER ASP ILE ASP PHE LEU ILE GLU GLU
SEQRES 39 A 504 ILE GLU ARG LEU GLY GLN ASP LEU HIS HIS
SEQRES 1 B 504 THR ASP PHE SER ASN LEU PHE ALA ARG ASP LEU LEU PRO
SEQRES 2 B 504 ALA LYS ASN GLY GLU GLU GLN THR VAL GLN PHE LEU LEU
SEQRES 3 B 504 GLU VAL VAL ASP ILE LEU LEU ASN TYR VAL ARG LYS THR
SEQRES 4 B 504 PHE ASP ARG SER THR LYS VAL LEU ASP PHE HIS HIS PRO
SEQRES 5 B 504 HIS GLN LEU LEU GLU GLY MET GLU GLY PHE ASN LEU GLU
SEQRES 6 B 504 LEU SER ASP HIS PRO GLU SER LEU GLU GLN ILE LEU VAL
SEQRES 7 B 504 ASP CYS ARG ASP THR LEU LYS TYR GLY VAL ARG THR GLY
SEQRES 8 B 504 HIS PRO ARG PHE PHE ASN GLN LEU SER THR GLY LEU ASP
SEQRES 9 B 504 ILE ILE GLY LEU ALA GLY GLU TRP LEU THR SER THR ALA
SEQRES 10 B 504 ASN THR ASN MET PHE THR TYR GLU ILE ALA PRO VAL PHE
SEQRES 11 B 504 VAL LEU MET GLU GLN ILE THR LEU LYS LYS MET ARG GLU
SEQRES 12 B 504 ILE VAL GLY TRP SER SER LYS ASP GLY ASP GLY ILE PHE
SEQRES 13 B 504 SER PRO GLY GLY ALA ILE SER ASN MET TYR SER ILE MET
SEQRES 14 B 504 ALA ALA ARG TYR LYS TYR PHE PRO GLU VAL LYS THR LYS
SEQRES 15 B 504 GLY MET ALA ALA VAL PRO LYS LEU VAL LEU PHE THR SER
SEQRES 16 B 504 GLU GLN SER HIS TYR SER ILE LYS LYS ALA GLY ALA ALA
SEQRES 17 B 504 LEU GLY PHE GLY THR ASP ASN VAL ILE LEU ILE LYS CYS
SEQRES 18 B 504 ASN GLU ARG GLY LYS ILE ILE PRO ALA ASP PHE GLU ALA
SEQRES 19 B 504 LYS ILE LEU GLU ALA LYS GLN LYS GLY TYR VAL PRO PHE
SEQRES 20 B 504 TYR VAL ASN ALA THR ALA GLY THR THR VAL TYR GLY ALA
SEQRES 21 B 504 PHE ASP PRO ILE GLN GLU ILE ALA ASP ILE CYS GLU LYS
SEQRES 22 B 504 TYR ASN LEU TRP LEU HIS VAL ASP ALA ALA TRP GLY GLY
SEQRES 23 B 504 GLY LEU LEU MET SER ARG LYS HIS ARG HIS LYS LEU ASN
SEQRES 24 B 504 GLY ILE GLU ARG ALA ASN SER VAL THR TRP ASN PRO HIS
SEQRES 25 B 504 LLP MET MET GLY VAL LEU LEU GLN CYS SER ALA ILE LEU
SEQRES 26 B 504 VAL LYS GLU LYS GLY ILE LEU GLN GLY CYS ASN GLN MET
SEQRES 27 B 504 CYS ALA GLY TYR LEU PHE GLN PRO ASP LYS GLN TYR ASP
SEQRES 28 B 504 VAL SER TYR ASP THR GLY ASP LYS ALA ILE GLN CYS GLY
SEQRES 29 B 504 ARG HIS VAL ASP ILE PHE LYS PHE TRP LEU MET TRP LYS
SEQRES 30 B 504 ALA LYS GLY THR VAL GLY PHE GLU ASN GLN ILE ASN LYS
SEQRES 31 B 504 CYS LEU GLU LEU ALA GLU TYR LEU TYR ALA LYS ILE LYS
SEQRES 32 B 504 ASN ARG GLU GLU PHE GLU MET VAL PHE ASN GLY GLU PRO
SEQRES 33 B 504 GLU HIS THR ASN VAL CYS PHE TRP TYR ILE PRO GLN SER
SEQRES 34 B 504 LEU ARG GLY VAL PRO ASP SER PRO GLN ARG ARG GLU LYS
SEQRES 35 B 504 LEU HIS LYS VAL ALA PRO LYS ILE LYS ALA LEU MET MET
SEQRES 36 B 504 GLU SER GLY THR THR MET VAL GLY TYR GLN PRO GLN GLY
SEQRES 37 B 504 ASP LYS ALA ASN PHE PHE ARG MET VAL ILE SER ASN PRO
SEQRES 38 B 504 ALA ALA THR GLN SER ASP ILE ASP PHE LEU ILE GLU GLU
SEQRES 39 B 504 ILE GLU ARG LEU GLY GLN ASP LEU HIS HIS
MODRES 2OKJ LLP A 405 LYS
MODRES 2OKJ LLP B 405 LYS
HET LLP A 405 24
HET LLP B 405 24
HET ABU A1001 7
HET ABU B1002 7
HET PLZ B2001 22
HETNAM LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-
HETNAM 2 LLP PYRIDIN-4-YLMETHANE)
HETNAM ABU GAMMA-AMINO-BUTANOIC ACID
HETNAM PLZ 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 PLZ METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
HETSYN ABU GAMMA(AMINO)-BUTYRIC ACID
FORMUL 1 LLP 2(C14 H24 N3 O7 P)
FORMUL 3 ABU 2(C4 H9 N O2)
FORMUL 5 PLZ C12 H19 N2 O7 P
FORMUL 6 HOH *359(H2 O)
HELIX 1 1 PHE A 99 LEU A 103 5 5
HELIX 2 2 GLY A 109 PHE A 132 1 24
HELIX 3 3 HIS A 143 GLU A 149 1 7
HELIX 4 4 SER A 164 TYR A 178 1 15
HELIX 5 5 ASP A 196 ASN A 210 1 15
HELIX 6 6 ALA A 219 GLY A 238 1 20
HELIX 7 7 GLY A 251 PHE A 268 1 18
HELIX 8 8 GLU A 270 GLY A 275 1 6
HELIX 9 9 MET A 276 VAL A 279 5 4
HELIX 10 10 TYR A 292 LEU A 301 1 10
HELIX 11 11 GLY A 304 ASP A 306 5 3
HELIX 12 12 ILE A 320 LYS A 334 1 15
HELIX 13 13 PRO A 355 ASN A 367 1 13
HELIX 14 14 TRP A 376 SER A 383 5 8
HELIX 15 15 HIS A 386 ASN A 391 5 6
HELIX 16 16 GLY A 392 ALA A 396 5 5
HELIX 17 17 GLY A 422 GLN A 429 1 8
HELIX 18 18 ASP A 443 ASP A 447 5 5
HELIX 19 19 THR A 448 ALA A 452 5 5
HELIX 20 20 ASP A 460 LYS A 495 1 36
HELIX 21 21 PRO A 519 ARG A 523 5 5
HELIX 22 22 SER A 528 HIS A 536 1 9
HELIX 23 23 LYS A 537 GLY A 550 1 14
HELIX 24 24 THR A 576 GLN A 592 1 17
HELIX 25 25 ASP B 94 LEU B 98 5 5
HELIX 26 26 PHE B 99 LEU B 103 5 5
HELIX 27 27 GLY B 109 PHE B 132 1 24
HELIX 28 28 HIS B 143 LEU B 148 1 6
HELIX 29 29 SER B 164 TYR B 178 1 15
HELIX 30 30 ASP B 196 ASN B 210 1 15
HELIX 31 31 ALA B 219 GLY B 238 1 20
HELIX 32 32 GLY B 251 PHE B 268 1 18
HELIX 33 33 GLU B 270 GLY B 275 1 6
HELIX 34 34 MET B 276 VAL B 279 5 4
HELIX 35 35 TYR B 292 LEU B 301 1 10
HELIX 36 36 GLY B 304 ASP B 306 5 3
HELIX 37 37 ILE B 320 LYS B 334 1 15
HELIX 38 38 PRO B 355 ASN B 367 1 13
HELIX 39 39 TRP B 376 SER B 383 5 8
HELIX 40 40 HIS B 386 ASN B 391 5 6
HELIX 41 41 GLY B 392 ALA B 396 5 5
HELIX 42 42 GLY B 422 GLN B 429 1 8
HELIX 43 43 ASP B 443 ALA B 452 5 10
HELIX 44 44 ASP B 460 LYS B 495 1 36
HELIX 45 45 PRO B 519 ARG B 523 5 5
HELIX 46 46 SER B 528 HIS B 536 1 9
HELIX 47 47 LYS B 537 GLY B 550 1 14
HELIX 48 48 THR B 576 GLY B 591 1 16
SHEET 1 A 5 PHE A 187 PHE A 188 0
SHEET 2 A 5 MET A 553 GLN A 559 1 O MET A 553 N PHE A 188
SHEET 3 A 5 LYS A 562 MET A 568 -1 O LYS A 562 N GLN A 559
SHEET 4 A 5 VAL A 513 TYR A 517 -1 N VAL A 513 O MET A 568
SHEET 5 A 5 PHE A 500 MET A 502 -1 N GLU A 501 O TRP A 516
SHEET 1 B 7 ASP A 245 SER A 249 0
SHEET 2 B 7 SER A 414 VAL A 418 -1 O SER A 414 N SER A 249
SHEET 3 B 7 SER A 398 TRP A 401 -1 N VAL A 399 O LEU A 417
SHEET 4 B 7 TRP A 369 ALA A 374 1 N VAL A 372 O SER A 398
SHEET 5 B 7 VAL A 337 ALA A 343 1 N PHE A 339 O TRP A 369
SHEET 6 B 7 LEU A 282 SER A 287 1 N PHE A 285 O ASN A 342
SHEET 7 B 7 VAL A 308 ILE A 311 1 O ILE A 309 N LEU A 284
SHEET 1 C 5 PHE B 187 PHE B 188 0
SHEET 2 C 5 MET B 553 GLN B 559 1 O MET B 553 N PHE B 188
SHEET 3 C 5 LYS B 562 MET B 568 -1 O LYS B 562 N GLN B 559
SHEET 4 C 5 VAL B 513 TYR B 517 -1 N VAL B 513 O MET B 568
SHEET 5 C 5 PHE B 500 MET B 502 -1 N GLU B 501 O TRP B 516
SHEET 1 D 7 ASP B 245 SER B 249 0
SHEET 2 D 7 SER B 414 VAL B 418 -1 O SER B 414 N SER B 249
SHEET 3 D 7 SER B 398 TRP B 401 -1 N VAL B 399 O LEU B 417
SHEET 4 D 7 TRP B 369 ALA B 374 1 N VAL B 372 O THR B 400
SHEET 5 D 7 VAL B 337 ALA B 343 1 N ALA B 343 O HIS B 371
SHEET 6 D 7 LEU B 282 SER B 287 1 N PHE B 285 O ASN B 342
SHEET 7 D 7 VAL B 308 ILE B 311 1 O ILE B 309 N LEU B 284
LINK C HIS A 404 N LLP A 405 1555 1555 1.33
LINK C LLP A 405 N MET A 406 1555 1555 1.34
LINK C HIS B 404 N LLP B 405 1555 1555 1.33
LINK NZ LLP B 405 C4ABPLZ B2001 1555 1555 1.71
LINK C LLP B 405 N MET B 406 1555 1555 1.34
LINK CG ABU B1002 O4 BPLZ B2001 1555 1555 1.26
LINK CB AABU B1002 C5 PLZ B2001 1555 1555 2.04
CISPEP 1 LEU A 104 PRO A 105 0 10.80
CISPEP 2 THR A 344 ALA A 345 0 16.92
CISPEP 3 LEU A 411 GLN A 412 0 -1.50
CISPEP 4 GLY A 433 TYR A 434 0 15.26
CISPEP 5 TYR A 434 LEU A 435 0 8.61
CISPEP 6 LEU A 435 PHE A 436 0 -18.18
CISPEP 7 PHE A 436 GLN A 437 0 -10.68
CISPEP 8 ARG A 523 GLY A 524 0 -0.94
CISPEP 9 GLY A 524 VAL A 525 0 3.41
CISPEP 10 VAL A 525 PRO A 526 0 -15.24
CISPEP 11 LEU B 104 PRO B 105 0 10.14
CISPEP 12 MET B 151 GLU B 152 0 -3.32
CISPEP 13 GLU B 152 GLY B 153 0 0.00
CISPEP 14 THR B 344 ALA B 345 0 15.74
CISPEP 15 LEU B 411 GLN B 412 0 -10.35
CISPEP 16 GLY B 433 TYR B 434 0 6.60
CISPEP 17 PHE B 436 GLN B 437 0 13.56
CISPEP 18 VAL B 525 PRO B 526 0 -1.16
SITE 1 AC1 5 GLN A 190 LEU A 191 SER A 192 ARG A 567
SITE 2 AC1 5 TYR B 434
SITE 1 AC2 7 LEU A 435 ASN B 189 GLN B 190 LEU B 191
SITE 2 AC2 7 SER B 192 ARG B 567 PLZ B2001
SITE 1 AC3 20 PHE A 214 CYS A 455 GLY A 456 GLN B 190
SITE 2 AC3 20 LEU B 191 SER B 192 GLY B 251 GLY B 252
SITE 3 AC3 20 ALA B 253 HIS B 291 GLY B 346 THR B 348
SITE 4 AC3 20 ASP B 373 ALA B 375 ASN B 402 HIS B 404
SITE 5 AC3 20 LLP B 405 ABU B1002 HOH B2030 HOH B2035
CRYST1 84.048 62.739 101.346 90.00 106.68 90.00 P 1 21 1 4
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 0.011898 0.000000 0.003566 0.00000
SCALE2 0.000000 0.015939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
