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5tj3.pdb
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5tj3.pdb
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HEADER HYDROLASE 03-OCT-16 5TJ3
TITLE CRYSTAL STRUCTURE OF WILD TYPE ALKALINE PHOSPHATASE PAFA TO 1.7A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALKALINE PHOSPHATASE PAFA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AP PAFA;
COMPND 5 EC: 3.1.3.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THR78 (HERE IN POSITION 69) IS RECORDED AS A
COMPND 8 PHOSPHORYLATED THREONINE (TPO). THE PHOSPHORYLATED FORM WAS PURIFIED
COMPND 9 ENDOGENOUSLY AND IS THE RESULT OF BASELINE ENZYMATIC ACTIVITY.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ELIZABETHKINGIA MENINGOSEPTICA;
SOURCE 3 ORGANISM_TAXID: 238;
SOURCE 4 GENE: PAFA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALKALINE PHOSPHATASE, PAFA, PHOSPHATE MONOESTERASE, SUBSTRATE
KEYWDS 2 SPECIFICITY, COMPARATIVE ENZYMOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.Y.LYUBIMOV,F.SUNDEN,S.RESSL,D.HERSCHLAG
REVDAT 2 13-SEP-17 5TJ3 1 REMARK
REVDAT 1 16-NOV-16 5TJ3 0
JRNL AUTH F.SUNDEN,I.ALSADHAN,A.Y.LYUBIMOV,S.RESSL,H.WIERSMA-KOCH,
JRNL AUTH 2 J.BORLAND,C.L.BROWN,T.A.JOHNSON,Z.SINGH,D.HERSCHLAG
JRNL TITL MECHANISTIC AND EVOLUTIONARY INSIGHTS FROM COMPARATIVE
JRNL TITL 2 ENZYMOLOGY OF PHOSPHOMONOESTERASES AND PHOSPHODIESTERASES
JRNL TITL 3 ACROSS THE ALKALINE PHOSPHATASE SUPERFAMILY.
JRNL REF J.AM.CHEM.SOC. V. 138 14273 2016
JRNL REFN ESSN 1520-5126
JRNL PMID 27670607
JRNL DOI 10.1021/JACS.6B06186
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 48460
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.670
REMARK 3 FREE R VALUE TEST SET COUNT : 1777
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 5.8413 - 3.6387 0.95 3742 202 0.1067 0.1243
REMARK 3 2 3.6387 - 3.0148 0.97 3796 106 0.1229 0.1293
REMARK 3 3 3.0148 - 2.6752 0.94 3676 212 0.1423 0.1634
REMARK 3 4 2.6752 - 2.4503 0.97 3763 105 0.1507 0.1782
REMARK 3 5 2.4503 - 2.2860 0.97 3783 102 0.1600 0.2050
REMARK 3 6 2.2860 - 2.1584 0.94 3624 210 0.1727 0.1836
REMARK 3 7 2.1584 - 2.0552 0.97 3778 102 0.1777 0.2192
REMARK 3 8 2.0552 - 1.9693 0.97 3732 105 0.1862 0.1848
REMARK 3 9 1.9693 - 1.8962 0.92 3549 208 0.2001 0.2323
REMARK 3 10 1.8962 - 1.8329 0.90 3453 99 0.2255 0.2418
REMARK 3 11 1.8329 - 1.7772 0.84 3269 99 0.2317 0.2645
REMARK 3 12 1.7772 - 1.7278 0.85 3201 194 0.2534 0.2652
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.2300
REMARK 3 OPERATOR: -K,-H,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 4270
REMARK 3 ANGLE : 0.614 5828
REMARK 3 CHIRALITY : 0.049 639
REMARK 3 PLANARITY : 0.004 755
REMARK 3 DIHEDRAL : 15.783 2514
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9254 -23.9637 41.6057
REMARK 3 T TENSOR
REMARK 3 T11: 0.0647 T22: 0.0484
REMARK 3 T33: -0.0156 T12: -0.0065
REMARK 3 T13: 0.0007 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0023
REMARK 3 L33: 0.0032 L12: 0.0011
REMARK 3 L13: -0.0009 L23: -0.0036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.0135 S13: -0.0012
REMARK 3 S21: -0.0102 S22: -0.0070 S23: 0.0004
REMARK 3 S31: 0.0056 S32: -0.0041 S33: -0.0037
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5561 -35.6691 18.6555
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.0608
REMARK 3 T33: 0.0194 T12: 0.0067
REMARK 3 T13: 0.0181 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.0050 L22: 0.0006
REMARK 3 L33: 0.0003 L12: 0.0013
REMARK 3 L13: 0.0004 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.0106 S13: -0.0082
REMARK 3 S21: 0.0018 S22: 0.0071 S23: -0.0044
REMARK 3 S31: 0.0038 S32: 0.0008 S33: 0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5358 -36.4435 33.5494
REMARK 3 T TENSOR
REMARK 3 T11: 0.0558 T22: 0.0281
REMARK 3 T33: -0.0095 T12: 0.0181
REMARK 3 T13: -0.0014 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.0089 L22: 0.0279
REMARK 3 L33: 0.0148 L12: 0.0001
REMARK 3 L13: -0.0070 L23: -0.0134
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.0033 S13: -0.0114
REMARK 3 S21: -0.0010 S22: -0.0198 S23: -0.0145
REMARK 3 S31: 0.0115 S32: 0.0140 S33: -0.0218
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9569 -43.3249 41.4468
REMARK 3 T TENSOR
REMARK 3 T11: 0.0772 T22: 0.0311
REMARK 3 T33: 0.0747 T12: -0.0215
REMARK 3 T13: -0.0008 T23: 0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 0.0043 L22: 0.0006
REMARK 3 L33: 0.0045 L12: -0.0005
REMARK 3 L13: -0.0001 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: -0.0111 S13: -0.0145
REMARK 3 S21: 0.0071 S22: -0.0070 S23: -0.0093
REMARK 3 S31: 0.0131 S32: -0.0037 S33: -0.0112
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 242 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4574 -39.8820 42.2905
REMARK 3 T TENSOR
REMARK 3 T11: 0.0671 T22: 0.0252
REMARK 3 T33: 0.0428 T12: -0.0235
REMARK 3 T13: -0.0071 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 0.0062 L22: 0.0101
REMARK 3 L33: 0.0091 L12: -0.0032
REMARK 3 L13: -0.0061 L23: -0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0072 S13: -0.0235
REMARK 3 S21: 0.0093 S22: -0.0074 S23: 0.0029
REMARK 3 S31: 0.0103 S32: 0.0049 S33: -0.0167
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 340 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9139 -25.5617 36.4362
REMARK 3 T TENSOR
REMARK 3 T11: 0.0499 T22: 0.0380
REMARK 3 T33: 0.0301 T12: -0.0089
REMARK 3 T13: 0.0114 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.0010 L22: 0.0027
REMARK 3 L33: 0.0023 L12: -0.0002
REMARK 3 L13: -0.0014 L23: 0.0016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0021 S13: -0.0055
REMARK 3 S21: 0.0086 S22: -0.0164 S23: 0.0054
REMARK 3 S31: -0.0101 S32: 0.0001 S33: -0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2081 -17.3217 10.3184
REMARK 3 T TENSOR
REMARK 3 T11: 0.0495 T22: 0.0614
REMARK 3 T33: -0.0129 T12: 0.0106
REMARK 3 T13: -0.0091 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0027
REMARK 3 L33: 0.0030 L12: -0.0006
REMARK 3 L13: 0.0009 L23: -0.0028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: 0.0117 S13: -0.0094
REMARK 3 S21: -0.0043 S22: -0.0159 S23: 0.0101
REMARK 3 S31: 0.0109 S32: -0.0025 S33: -0.0105
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 467 THROUGH 490 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8426 -22.9074 23.4542
REMARK 3 T TENSOR
REMARK 3 T11: 0.0429 T22: 0.0454
REMARK 3 T33: 0.0084 T12: -0.0060
REMARK 3 T13: 0.0115 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: -0.0001
REMARK 3 L33: 0.0035 L12: 0.0001
REMARK 3 L13: -0.0024 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0027 S13: -0.0035
REMARK 3 S21: -0.0040 S22: -0.0026 S23: 0.0035
REMARK 3 S31: 0.0021 S32: -0.0006 S33: 0.0036
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 491 THROUGH 545 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2566 -16.7147 43.7522
REMARK 3 T TENSOR
REMARK 3 T11: 0.0520 T22: 0.0416
REMARK 3 T33: -0.0094 T12: -0.0193
REMARK 3 T13: -0.0036 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0067
REMARK 3 L33: 0.0046 L12: 0.0012
REMARK 3 L13: 0.0011 L23: 0.0052
REMARK 3 S TENSOR
REMARK 3 S11: -0.0080 S12: -0.0089 S13: 0.0024
REMARK 3 S21: -0.0064 S22: -0.0069 S23: 0.0028
REMARK 3 S31: -0.0074 S32: -0.0075 S33: -0.0118
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.23
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48644
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 35.986
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.28700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: PDB ENTRY 3Q3Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.1 M SODIUM ACETATE, PH
REMARK 280 4.4, 0.2 MM AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 56.89850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.89850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.72100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.89850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.89850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 35.72100
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 56.89850
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 56.89850
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 35.72100
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 56.89850
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 56.89850
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.72100
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -396.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 A1012 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 12
REMARK 465 ASP A 13
REMARK 465 ILE A 14
REMARK 465 GLY A 15
REMARK 465 ILE A 16
REMARK 465 ASP A 17
REMARK 465 SER A 18
REMARK 465 ASP A 19
REMARK 465 PRO A 20
REMARK 465 GLN A 21
REMARK 465 LYS A 22
REMARK 465 THR A 23
REMARK 465 VAL A 373
REMARK 465 GLU A 374
REMARK 465 ARG A 546
REMARK 465 ILE A 547
REMARK 465 GLU A 548
REMARK 465 GLY A 549
REMARK 465 ARG A 550
REMARK 465 SER A 551
REMARK 465 ALA A 552
REMARK 465 TRP A 553
REMARK 465 SER A 554
REMARK 465 HIS A 555
REMARK 465 PRO A 556
REMARK 465 GLN A 557
REMARK 465 PHE A 558
REMARK 465 GLU A 559
REMARK 465 LYS A 560
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 256 CG CD CE NZ
REMARK 470 ASP A 375 CG OD1 OD2
REMARK 470 LYS A 378 CG CD CE NZ
REMARK 470 GLU A 379 CG CD OE1 OE2
REMARK 470 LYS A 407 CG CD CE NZ
REMARK 470 TYR A 479 CG CD1 CD2 CE1 CE2 CZ OH
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 O HOH A 1199 O HOH A 1277 2.15
REMARK 500 O HOH A 1019 O HOH A 1067 2.17
REMARK 500 ND2 ASN A 206 O HOH A 702 2.17
REMARK 500 O HOH A 942 O HOH A 1250 2.19
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 73 37.87 -98.38
REMARK 500 THR A 267 40.05 -97.05
REMARK 500 ASP A 291 -168.71 -103.83
REMARK 500 HIS A 353 169.31 175.91
REMARK 500 SER A 487 -12.24 -177.99
REMARK 500 SER A 487 -14.62 -175.02
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 A1307 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1308 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A1309 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A1310 DISTANCE = 6.39 ANGSTROMS
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 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 38 OD1
REMARK 620 2 TPO A 79 OG1 131.5
REMARK 620 3 ASP A 352 OD2 101.8 93.9
REMARK 620 4 HIS A 353 NE2 107.7 113.2 102.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO A 79 O3P
REMARK 620 2 ASP A 305 OD1 88.2
REMARK 620 3 ASP A 305 OD2 76.8 52.7
REMARK 620 4 HIS A 309 NE2 160.9 98.5 93.0
REMARK 620 5 HIS A 486 NE2 96.0 103.9 155.1 99.6
REMARK 620 6 HOH A 896 O 78.2 153.2 101.3 88.3 100.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 603 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 233 O
REMARK 620 2 ASP A 233 OD1 80.1
REMARK 620 3 GLU A 238 OE2 88.8 168.8
REMARK 620 4 PRO A 247 O 77.9 92.0 87.0
REMARK 620 5 GLU A 317 OE1 158.5 104.1 85.8 122.4
REMARK 620 6 GLU A 317 OE2 151.8 89.8 100.7 76.1 49.7
REMARK 620 7 HOH A 717 O 83.0 96.1 81.0 157.6 75.6 124.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 604 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 291 OD1
REMARK 620 2 ILE A 293 O 92.6
REMARK 620 3 ASP A 295 OD2 149.8 103.0
REMARK 620 4 HOH A 810 O 72.3 150.1 81.8
REMARK 620 5 HOH A 847 O 82.9 73.4 77.3 79.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 604
DBREF 5TJ3 A 21 546 UNP Q9KJX5 ALPH_ELIME 21 546
SEQADV 5TJ3 MET A 12 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ASP A 13 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ILE A 14 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 GLY A 15 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ILE A 16 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ASP A 17 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 SER A 18 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ASP A 19 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 PRO A 20 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ILE A 547 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 GLU A 548 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 GLY A 549 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ARG A 550 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 SER A 551 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 ALA A 552 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 TRP A 553 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 SER A 554 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 HIS A 555 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 PRO A 556 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 GLN A 557 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 PHE A 558 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 GLU A 559 UNP Q9KJX5 EXPRESSION TAG
SEQADV 5TJ3 LYS A 560 UNP Q9KJX5 EXPRESSION TAG
SEQRES 1 A 549 MET ASP ILE GLY ILE ASP SER ASP PRO GLN LYS THR ASN
SEQRES 2 A 549 ALA VAL PRO ARG PRO LYS LEU VAL VAL GLY LEU VAL VAL
SEQRES 3 A 549 ASP GLN MET ARG TRP ASP TYR LEU TYR ARG TYR TYR SER
SEQRES 4 A 549 LYS TYR GLY GLU GLY GLY PHE LYS ARG MET LEU ASN THR
SEQRES 5 A 549 GLY TYR SER LEU ASN ASN VAL HIS ILE ASP TYR VAL PRO
SEQRES 6 A 549 THR VAL TPO ALA ILE GLY HIS THR SER ILE PHE THR GLY
SEQRES 7 A 549 SER VAL PRO SER ILE HIS GLY ILE ALA GLY ASN ASP TRP
SEQRES 8 A 549 TYR ASP LYS GLU LEU GLY LYS SER VAL TYR CYS THR SER
SEQRES 9 A 549 ASP GLU THR VAL GLN PRO VAL GLY THR THR SER ASN SER
SEQRES 10 A 549 VAL GLY GLN HIS SER PRO ARG ASN LEU TRP SER THR THR
SEQRES 11 A 549 VAL THR ASP GLN LEU GLY LEU ALA THR ASN PHE THR SER
SEQRES 12 A 549 LYS VAL VAL GLY VAL SER LEU LYS ASP ARG ALA SER ILE
SEQRES 13 A 549 LEU PRO ALA GLY HIS ASN PRO THR GLY ALA PHE TRP PHE
SEQRES 14 A 549 ASP ASP THR THR GLY LYS PHE ILE THR SER THR TYR TYR
SEQRES 15 A 549 THR LYS GLU LEU PRO LYS TRP VAL ASN ASP PHE ASN ASN
SEQRES 16 A 549 LYS ASN VAL PRO ALA GLN LEU VAL ALA ASN GLY TRP ASN
SEQRES 17 A 549 THR LEU LEU PRO ILE ASN GLN TYR THR GLU SER SER GLU
SEQRES 18 A 549 ASP ASN VAL GLU TRP GLU GLY LEU LEU GLY SER LYS LYS
SEQRES 19 A 549 THR PRO THR PHE PRO TYR THR ASP LEU ALA LYS ASP TYR
SEQRES 20 A 549 GLU ALA LYS LYS GLY LEU ILE ARG THR THR PRO PHE GLY
SEQRES 21 A 549 ASN THR LEU THR LEU GLN MET ALA ASP ALA ALA ILE ASP
SEQRES 22 A 549 GLY ASN GLN MET GLY VAL ASP ASP ILE THR ASP PHE LEU
SEQRES 23 A 549 THR VAL ASN LEU ALA SER THR ASP TYR VAL GLY HIS ASN
SEQRES 24 A 549 PHE GLY PRO ASN SER ILE GLU VAL GLU ASP THR TYR LEU
SEQRES 25 A 549 ARG LEU ASP ARG ASP LEU ALA ASP PHE PHE ASN ASN LEU
SEQRES 26 A 549 ASP LYS LYS VAL GLY LYS GLY ASN TYR LEU VAL PHE LEU
SEQRES 27 A 549 SER ALA ASP HIS GLY ALA ALA HIS SER VAL GLY PHE MET
SEQRES 28 A 549 GLN ALA HIS LYS MET PRO THR GLY PHE PHE VAL GLU ASP
SEQRES 29 A 549 MET LYS LYS GLU MET ASN ALA LYS LEU LYS GLN LYS PHE
SEQRES 30 A 549 GLY ALA ASP ASN ILE ILE ALA ALA ALA MET ASN TYR GLN
SEQRES 31 A 549 VAL TYR PHE ASP ARG LYS VAL LEU ALA ASP SER LYS LEU
SEQRES 32 A 549 GLU LEU ASP ASP VAL ARG ASP TYR VAL MET THR GLU LEU
SEQRES 33 A 549 LYS LYS GLU PRO SER VAL LEU TYR VAL LEU SER THR ASP
SEQRES 34 A 549 GLU ILE TRP GLU SER SER ILE PRO GLU PRO ILE LYS SER
SEQRES 35 A 549 ARG VAL ILE ASN GLY TYR ASN TRP LYS ARG SER GLY ASP
SEQRES 36 A 549 ILE GLN ILE ILE SER LYS ASP GLY TYR LEU SER ALA TYR
SEQRES 37 A 549 SER LYS LYS GLY THR THR HIS SER VAL TRP ASN SER TYR
SEQRES 38 A 549 ASP SER HIS ILE PRO LEU LEU PHE MET GLY TRP GLY ILE
SEQRES 39 A 549 LYS GLN GLY GLU SER ASN GLN PRO TYR HIS MET THR ASP
SEQRES 40 A 549 ILE ALA PRO THR VAL SER SER LEU LEU LYS ILE GLN PHE
SEQRES 41 A 549 PRO SER GLY ALA VAL GLY LYS PRO ILE THR GLU VAL ILE
SEQRES 42 A 549 GLY ARG ILE GLU GLY ARG SER ALA TRP SER HIS PRO GLN
SEQRES 43 A 549 PHE GLU LYS
MODRES 5TJ3 TPO A 79 THR MODIFIED RESIDUE
HET TPO A 79 11
HET ZN A 601 1
HET ZN A 602 1
HET ZN A 603 1
HET ZN A 604 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM ZN ZINC ION
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 ZN 4(ZN 2+)
FORMUL 6 HOH *610(H2 O)
HELIX 1 AA1 ASP A 43 TYR A 48 1 6
HELIX 2 AA2 TYR A 49 TYR A 52 5 4
HELIX 3 AA3 GLY A 56 GLY A 64 1 9
HELIX 4 AA4 VAL A 78 GLY A 89 1 12
HELIX 5 AA5 VAL A 91 GLY A 96 1 6
HELIX 6 AA6 SER A 126 GLN A 131 1 6
HELIX 7 AA7 THR A 141 THR A 150 1 10
HELIX 8 AA8 LYS A 162 GLY A 171 1 10
HELIX 9 AA9 PRO A 198 LYS A 207 1 10
HELIX 10 AB1 ASN A 208 VAL A 214 1 7
HELIX 11 AB2 PRO A 223 TYR A 227 5 5
HELIX 12 AB3 ASP A 253 LYS A 261 1 9
HELIX 13 AB4 LYS A 262 THR A 267 5 6
HELIX 14 AB5 THR A 268 ASN A 286 1 19
HELIX 15 AB6 ALA A 302 GLY A 312 1 11
HELIX 16 AB7 SER A 315 VAL A 340 1 26
HELIX 17 AB8 SER A 358 HIS A 365 1 8
HELIX 18 AB9 MET A 376 GLY A 389 1 14
HELIX 19 AC1 ASP A 405 LYS A 413 1 9
HELIX 20 AC2 GLU A 415 LYS A 429 1 15
HELIX 21 AC3 PRO A 450 TYR A 459 1 10
HELIX 22 AC4 ASN A 490 SER A 494 1 5
HELIX 23 AC5 ASP A 518 LYS A 528 1 11
SHEET 1 AA110 PRO A 121 VAL A 122 0
SHEET 2 AA110 PHE A 187 SER A 190 -1 O THR A 189 N VAL A 122
SHEET 3 AA110 GLY A 176 PHE A 180 -1 N TRP A 179 O ILE A 188
SHEET 4 AA110 VAL A 156 VAL A 159 1 N GLY A 158 O PHE A 178
SHEET 5 AA110 ASP A 295 LEU A 301 1 O THR A 298 N VAL A 159
SHEET 6 AA110 LEU A 31 VAL A 37 1 N GLY A 34 O LEU A 297
SHEET 7 AA110 TYR A 345 SER A 350 1 O LEU A 346 N VAL A 33
SHEET 8 AA110 LEU A 498 GLY A 502 -1 O MET A 501 N VAL A 347
SHEET 9 AA110 TYR A 65 LEU A 67 -1 N LEU A 67 O LEU A 498
SHEET 10 AA110 GLY A 508 SER A 510 1 O SER A 510 N SER A 66
SHEET 1 AA2 3 HIS A 495 ILE A 496 0
SHEET 2 AA2 3 VAL A 70 HIS A 71 -1 N VAL A 70 O ILE A 496
SHEET 3 AA2 3 TYR A 514 HIS A 515 1 O TYR A 514 N HIS A 71
SHEET 1 AA3 2 ASP A 101 ASP A 104 0
SHEET 2 AA3 2 LYS A 109 TYR A 112 -1 O VAL A 111 N TRP A 102
SHEET 1 AA4 2 GLY A 370 PHE A 371 0
SHEET 2 AA4 2 TYR A 475 LEU A 476 1 O LEU A 476 N GLY A 370
SHEET 1 AA5 4 ILE A 394 MET A 398 0
SHEET 2 AA5 4 GLN A 401 PHE A 404 -1 O TYR A 403 N ALA A 396
SHEET 3 AA5 4 ILE A 467 SER A 471 -1 O ILE A 467 N VAL A 402
SHEET 4 AA5 4 VAL A 433 SER A 438 -1 N LEU A 434 O ILE A 470
LINK OD1 ASP A 38 ZN ZN A 601 1555 1555 1.96
LINK C VAL A 78 N TPO A 79 1555 1555 1.33
LINK OG1 TPO A 79 ZN ZN A 601 1555 1555 2.04
LINK O3P TPO A 79 ZN ZN A 602 1555 1555 1.88
LINK C TPO A 79 N ALA A 80 1555 1555 1.33
LINK O ASP A 233 ZN ZN A 603 1555 1555 2.38
LINK OD1 ASP A 233 ZN ZN A 603 1555 1555 2.41
LINK OE2 GLU A 238 ZN ZN A 603 1555 1555 2.35
LINK O PRO A 247 ZN ZN A 603 1555 1555 2.33
LINK OD1 ASP A 291 ZN ZN A 604 1555 1555 2.33
LINK O ILE A 293 ZN ZN A 604 1555 1555 2.35
LINK OD2 ASP A 295 ZN ZN A 604 1555 1555 2.43
LINK OD1 ASP A 305 ZN ZN A 602 1555 1555 2.22
LINK OD2 ASP A 305 ZN ZN A 602 1555 1555 2.66
LINK NE2 HIS A 309 ZN ZN A 602 1555 1555 2.03
LINK OE1 GLU A 317 ZN ZN A 603 1555 1555 2.63
LINK OE2 GLU A 317 ZN ZN A 603 1555 1555 2.59
LINK OD2 ASP A 352 ZN ZN A 601 1555 1555 2.03
LINK NE2 HIS A 353 ZN ZN A 601 1555 1555 2.11
LINK NE2 HIS A 486 ZN ZN A 602 1555 1555 2.15
LINK ZN ZN A 602 O HOH A 896 1555 1555 2.44
LINK ZN ZN A 603 O HOH A 717 1555 1555 2.65
LINK ZN ZN A 604 O HOH A 810 1555 1555 2.68
LINK ZN ZN A 604 O HOH A 847 1555 1555 2.43
CISPEP 1 VAL A 75 PRO A 76 0 0.04
CISPEP 2 PHE A 249 PRO A 250 0 -3.09
CISPEP 3 GLU A 449 PRO A 450 0 2.75
SITE 1 AC1 4 ASP A 38 TPO A 79 ASP A 352 HIS A 353
SITE 1 AC2 5 TPO A 79 ASP A 305 HIS A 309 HIS A 486
SITE 2 AC2 5 HOH A 896
SITE 1 AC3 5 ASP A 233 GLU A 238 PRO A 247 GLU A 317
SITE 2 AC3 5 HOH A 717
SITE 1 AC4 6 ASP A 291 ILE A 293 ASP A 295 HOH A 810
SITE 2 AC4 6 HOH A 847 HOH A 907
CRYST1 113.797 113.797 71.442 90.00 90.00 90.00 I 4 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 0.008788 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008788 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013997 0.00000
ATOM 1 N ASN A 24 25.188 -20.017 58.979 1.00 36.24 N
ANISOU 1 N ASN A 24 4710 4715 4345 4 23 21 N
ATOM 2 CA ASN A 24 25.350 -19.016 57.930 1.00 34.85 C
ANISOU 2 CA ASN A 24 4533 4538 4168 3 22 19 C
ATOM 3 C ASN A 24 24.773 -19.505 56.606 1.00 30.92 C
ANISOU 3 C ASN A 24 4037 4041 3671 2 22 19 C
ATOM 4 O ASN A 24 25.214 -19.083 55.540 1.00 30.95 O
ANISOU 4 O ASN A 24 4040 4044 3675 1 22 19 O
ATOM 5 CB ASN A 24 26.827 -18.654 57.751 1.00 36.14 C
ANISOU 5 CB ASN A 24 4696 4702 4333 4 23 22 C
ATOM 6 CG ASN A 24 27.408 -17.948 58.961 1.00 37.74 C
ANISOU 6 CG ASN A 24 4899 4905 4536 5 22 22 C
ATOM 7 OD1 ASN A 24 26.691 -17.298 59.722 1.00 39.62 O
ANISOU 7 OD1 ASN A 24 5137 5142 4773 6 21 20 O
ATOM 8 ND2 ASN A 24 28.719 -18.068 59.141 1.00 36.26 N
ANISOU 8 ND2 ASN A 24 4711 4718 4349 6 24 25 N
ATOM 9 N ALA A 25 23.788 -20.392 56.674 1.00 26.11 N
ANISOU 9 N ALA A 25 3427 3431 3060 1 22 18 N
ATOM 10 CA ALA A 25 23.162 -20.941 55.482 1.00 23.29 C
ANISOU 10 CA ALA A 25 3072 3073 2703 0 22 17 C
ATOM 11 C ALA A 25 21.886 -20.181 55.139 1.00 20.69 C
ANISOU 11 C ALA A 25 2743 2744 2374 -1 20 13 C
ATOM 12 O ALA A 25 21.252 -19.554 55.993 1.00 20.20 O
ANISOU 12 O ALA A 25 2681 2683 2312 0 19 11 O
ATOM 13 CB ALA A 25 22.851 -22.429 55.667 1.00 25.68 C
ANISOU 13 CB ALA A 25 3376 3377 3006 -1 24 19 C
ATOM 14 N VAL A 26 21.520 -20.241 53.863 1.00 20.15 N
ANISOU 14 N VAL A 26 2676 2673 2306 -3 20 12 N
ATOM 15 CA VAL A 26 20.277 -19.643 53.386 1.00 15.95 C
ANISOU 15 CA VAL A 26 2145 2141 1775 -3 18 9 C
ATOM 16 C VAL A 26 19.117 -20.450 53.957 1.00 11.49 C
ANISOU 16 C VAL A 26 1580 1576 1209 -3 18 8 C
ATOM 17 O VAL A 26 19.060 -21.671 53.755 1.00 9.26 O
ANISOU 17 O VAL A 26 1299 1294 927 -4 20 9 O
ATOM 18 CB VAL A 26 20.230 -19.606 51.850 1.00 17.79 C
ANISOU 18 CB VAL A 26 2379 2370 2008 -5 18 8 C
ATOM 19 CG1 VAL A 26 18.978 -18.890 51.371 1.00 17.85 C
ANISOU 19 CG1 VAL A 26 2388 2378 2017 -5 15 5 C
ATOM 20 CG2 VAL A 26 21.479 -18.941 51.298 1.00 18.46 C
ANISOU 20 CG2 VAL A 26 2465 2455 2094 -5 18 10 C
ATOM 21 N PRO A 27 18.192 -19.830 54.689 1.00 14.86 N
ANISOU 21 N PRO A 27 2007 2005 1635 -2 16 5 N
ATOM 22 CA PRO A 27 17.028 -20.578 55.184 1.00 15.40 C
ANISOU 22 CA PRO A 27 2075 2073 1703 -2 16 4 C
ATOM 23 C PRO A 27 16.169 -21.081 54.032 1.00 14.79 C
ANISOU 23 C PRO A 27 2000 1995 1627 -4 16 3 C
ATOM 24 O PRO A 27 15.762 -20.314 53.157 1.00 16.35 O
ANISOU 24 O PRO A 27 2198 2191 1825 -5 15 1 O
ATOM 25 CB PRO A 27 16.282 -19.547 56.040 1.00 14.88 C
ANISOU 25 CB PRO A 27 2009 2009 1637 -1 14 1 C
ATOM 26 CG PRO A 27 17.320 -18.534 56.409 1.00 16.60 C
ANISOU 26 CG PRO A 27 2227 2227 1855 0 14 2 C
ATOM 27 CD PRO A 27 18.231 -18.456 55.218 1.00 16.37 C
ANISOU 27 CD PRO A 27 2197 2197 1826 -1 14 3 C
ATOM 28 N ARG A 28 15.897 -22.385 54.038 1.00 13.82 N
ANISOU 28 N ARG A 28 1877 1871 1503 -5 18 4 N
ATOM 29 CA ARG A 28 15.146 -23.023 52.966 1.00 13.18 C
ANISOU 29 CA ARG A 28 1798 1788 1423 -7 18 3 C
ATOM 30 C ARG A 28 14.359 -24.196 53.523 1.00 14.29 C
ANISOU 30 C ARG A 28 1938 1929 1562 -7 19 3 C
ATOM 31 O ARG A 28 14.781 -24.811 54.509 1.00 15.50 O
ANISOU 31 O ARG A 28 2091 2084 1715 -6 20 5 O
ATOM 32 CB ARG A 28 16.070 -23.511 51.842 1.00 13.94 C
ANISOU 32 CB ARG A 28 1895 1881 1520 -8 19 5 C
ATOM 33 CG ARG A 28 16.441 -22.434 50.857 1.00 12.98 C
ANISOU 33 CG ARG A 28 1775 1759 1400 -9 18 4 C
ATOM 34 CD ARG A 28 17.427 -22.944 49.846 1.00 16.41 C
ANISOU 34 CD ARG A 28 2211 2190 1835 -10 20 7 C
ATOM 35 NE ARG A 28 17.961 -21.847 49.055 1.00 17.72 N
ANISOU 35 NE ARG A 28 2378 2354 2002 -10 19 6 N
ATOM 36 CZ ARG A 28 19.057 -21.931 48.314 1.00 20.58 C
ANISOU 36 CZ ARG A 28 2741 2713 2364 -10 20 8 C
ATOM 37 NH1 ARG A 28 19.471 -20.875 47.628 1.00 14.66 N
ANISOU 37 NH1 ARG A 28 1992 1963 1616 -11 19 7 N
ATOM 38 NH2 ARG A 28 19.742 -23.067 48.266 1.00 22.84 N
ANISOU 38 NH2 ARG A 28 3028 2999 2651 -11 22 11 N
ATOM 39 N PRO A 29 13.224 -24.534 52.916 1.00 16.60 N
ANISOU 39 N PRO A 29 2233 2220 1855 -8 18 1 N
ATOM 40 CA PRO A 29 12.505 -25.744 53.324 1.00 15.08 C
ANISOU 40 CA PRO A 29 2040 2028 1662 -9 19 2 C
ATOM 41 C PRO A 29 13.241 -26.987 52.851 1.00 14.16 C
ANISOU 41 C PRO A 29 1924 1910 1545 -10 22 5 C
ATOM 42 O PRO A 29 14.047 -26.947 51.919 1.00 11.72 O
ANISOU 42 O PRO A 29 1617 1599 1238 -10 22 6 O
ATOM 43 CB PRO A 29 11.149 -25.598 52.627 1.00 11.99 C
ANISOU 43 CB PRO A 29 1650 1636 1271 -10 18 -1 C
ATOM 44 CG PRO A 29 11.466 -24.819 51.393 1.00 10.65 C
ANISOU 44 CG PRO A 29 1481 1463 1102 -10 17 -2 C
ATOM 45 CD PRO A 29 12.545 -23.841 51.805 1.00 13.75 C
ANISOU 45 CD PRO A 29 1872 1857 1495 -9 17 -1 C
ATOM 46 N LYS A 30 12.958 -28.110 53.517 1.00 12.02 N
ANISOU 46 N LYS A 30 1654 1640 1275 -10 23 6 N
ATOM 47 CA LYS A 30 13.584 -29.363 53.110 1.00 11.67 C
ANISOU 47 CA LYS A 30 1609 1594 1229 -11 25 9 C
ATOM 48 C LYS A 30 12.950 -29.914 51.842 1.00 9.97 C
ANISOU 48 C LYS A 30 1397 1376 1015 -13 26 8 C
ATOM 49 O LYS A 30 13.597 -30.651 51.091 1.00 8.11 O
ANISOU 49 O LYS A 30 1163 1138 781 -14 27 10 O
ATOM 50 CB LYS A 30 13.486 -30.392 54.233 1.00 12.75 C
ANISOU 50 CB LYS A 30 1745 1733 1366 -10 27 10 C
ATOM 51 CG LYS A 30 14.120 -29.941 55.540 1.00 14.77 C
ANISOU 51 CG LYS A 30 2000 1992 1621 -8 27 11 C
ATOM 52 CD LYS A 30 14.255 -31.098 56.507 1.00 18.87 C
ANISOU 52 CD LYS A 30 2519 2512 2140 -8 29 13 C
ATOM 53 CE LYS A 30 15.224 -30.772 57.634 1.00 23.55 C
ANISOU 53 CE LYS A 30 3110 3106 2732 -6 30 15 C
ATOM 54 NZ LYS A 30 15.555 -31.985 58.445 1.00 27.51 N
ANISOU 54 NZ LYS A 30 3611 3608 3233 -6 32 18 N
ATOM 55 N LEU A 31 11.697 -29.555 51.585 1.00 10.50 N
ANISOU 55 N LEU A 31 1465 1442 1082 -13 24 5 N
ATOM 56 CA LEU A 31 10.948 -30.066 50.449 1.00 8.29 C
ANISOU 56 CA LEU A 31 1187 1160 803 -15 24 4 C
ATOM 57 C LEU A 31 9.931 -29.016 50.045 1.00 8.85 C
ANISOU 57 C LEU A 31 1259 1231 875 -15 21 1 C
ATOM 58 O LEU A 31 9.352 -28.347 50.902 1.00 8.09 O
ANISOU 58 O LEU A 31 1160 1136 777 -14 20 -1 O
ATOM 59 CB LEU A 31 10.240 -31.383 50.796 1.00 7.85 C
ANISOU 59 CB LEU A 31 1132 1104 747 -15 25 5 C
ATOM 60 CG LEU A 31 9.257 -31.971 49.784 1.00 9.36 C
ANISOU 60 CG LEU A 31 1325 1292 938 -17 25 3 C
ATOM 61 CD1 LEU A 31 9.998 -32.483 48.560 1.00 6.55 C
ANISOU 61 CD1 LEU A 31 972 932 583 -18 26 5 C
ATOM 62 CD2 LEU A 31 8.435 -33.078 50.423 1.00 10.99 C
ANISOU 62 CD2 LEU A 31 1532 1500 1144 -17 26 3 C
ATOM 63 N VAL A 32 9.724 -28.858 48.746 1.00 6.62 N
ANISOU 63 N VAL A 32 979 945 593 -16 21 0 N
ATOM 64 CA VAL A 32 8.580 -28.106 48.255 1.00 7.53 C
ANISOU 64 CA VAL A 32 1094 1059 708 -16 19 -4 C
ATOM 65 C VAL A 32 7.797 -29.017 47.323 1.00 8.82 C
ANISOU 65 C VAL A 32 1260 1219 872 -18 19 -4 C
ATOM 66 O VAL A 32 8.382 -29.784 46.550 1.00 6.36 O
ANISOU 66 O VAL A 32 950 904 561 -19 21 -2 O
ATOM 67 CB VAL A 32 8.976 -26.771 47.580 1.00 10.41 C
ANISOU 67 CB VAL A 32 1459 1422 1074 -16 17 -5 C
ATOM 68 CG1 VAL A 32 10.483 -26.608 47.488 1.00 8.14 C
ANISOU 68 CG1 VAL A 32 1172 1135 787 -16 19 -2 C
ATOM 69 CG2 VAL A 32 8.284 -26.583 46.245 1.00 13.37 C
ANISOU 69 CG2 VAL A 32 1837 1794 1450 -17 16 -6 C
ATOM 70 N VAL A 33 6.474 -28.979 47.454 1.00 8.58 N
ANISOU 70 N VAL A 33 1229 1189 841 -18 18 -6 N
ATOM 71 CA VAL A 33 5.567 -29.822 46.685 1.00 8.36 C
ANISOU 71 CA VAL A 33 1204 1159 814 -20 18 -7 C
ATOM 72 C VAL A 33 4.709 -28.915 45.821 1.00 7.75 C
ANISOU 72 C VAL A 33 1127 1080 737 -20 16 -10 C
ATOM 73 O VAL A 33 4.040 -28.011 46.337 1.00 7.60 O
ANISOU 73 O VAL A 33 1107 1064 718 -19 14 -12 O
ATOM 74 CB VAL A 33 4.682 -30.694 47.588 1.00 7.65 C
ANISOU 74 CB VAL A 33 1113 1071 722 -20 19 -7 C
ATOM 75 CG1 VAL A 33 3.770 -31.562 46.740 1.00 4.25 C
ANISOU 75 CG1 VAL A 33 684 638 292 -21 19 -8 C
ATOM 76 CG2 VAL A 33 5.530 -31.543 48.513 1.00 6.84 C
ANISOU 76 CG2 VAL A 33 1009 971 620 -19 21 -4 C
ATOM 77 N GLY A 34 4.731 -29.153 44.516 1.00 8.94 N
ANISOU 77 N GLY A 34 1281 1226 888 -21 17 -10 N
ATOM 78 CA GLY A 34 3.855 -28.445 43.611 1.00 6.89 C
ANISOU 78 CA GLY A 34 1023 965 629 -22 15 -12 C
ATOM 79 C GLY A 34 2.707 -29.322 43.164 1.00 6.66 C
ANISOU 79 C GLY A 34 996 934 600 -23 15 -13 C
ATOM 80 O GLY A 34 2.897 -30.240 42.361 1.00 5.34 O
ANISOU 80 O GLY A 34 832 764 434 -24 16 -12 O
ATOM 81 N LEU A 35 1.517 -29.064 43.697 1.00 9.62 N
ANISOU 81 N LEU A 35 1369 1311 974 -23 14 -16 N
ATOM 82 CA LEU A 35 0.310 -29.791 43.328 1.00 8.10 C
ANISOU 82 CA LEU A 35 1178 1118 782 -24 13 -17 C
ATOM 83 C LEU A 35 -0.503 -28.941 42.365 1.00 9.99 C
ANISOU 83 C LEU A 35 1418 1355 1022 -25 12 -19 C
ATOM 84 O LEU A 35 -0.835 -27.795 42.678 1.00 8.98 O
ANISOU 84 O LEU A 35 1288 1229 894 -24 10 -21 O
ATOM 85 CB LEU A 35 -0.540 -30.110 44.559 1.00 8.88 C
ANISOU 85 CB LEU A 35 1275 1221 880 -24 13 -18 C
ATOM 86 CG LEU A 35 0.107 -30.742 45.787 1.00 7.96 C
ANISOU 86 CG LEU A 35 1156 1107 763 -23 14 -16 C
ATOM 87 CD1 LEU A 35 -0.825 -30.614 46.978 1.00 12.43 C
ANISOU 87 CD1 LEU A 35 1720 1677 1328 -22 13 -17 C
ATOM 88 CD2 LEU A 35 0.418 -32.198 45.519 1.00 8.11 C
ANISOU 88 CD2 LEU A 35 1177 1124 781 -24 17 -13 C
ATOM 89 N VAL A 36 -0.834 -29.491 41.205 1.00 9.95 N
ANISOU 89 N VAL A 36 1416 1345 1017 -26 12 -19 N
ATOM 90 CA VAL A 36 -1.754 -28.823 40.296 1.00 11.22 C
ANISOU 90 CA VAL A 36 1578 1504 1179 -27 10 -22 C
ATOM 91 C VAL A 36 -2.902 -29.782 40.010 1.00 12.25 C
ANISOU 91 C VAL A 36 1710 1633 1309 -28 10 -22 C
ATOM 92 O VAL A 36 -2.699 -30.873 39.461 1.00 16.63 O
ANISOU 92 O VAL A 36 2268 2185 1864 -29 12 -21 O
ATOM 93 CB VAL A 36 -1.059 -28.316 39.018 1.00 13.57 C
ANISOU 93 CB VAL A 36 1880 1798 1478 -27 10 -21 C
ATOM 94 CG1 VAL A 36 0.350 -28.863 38.894 1.00 12.99 C
ANISOU 94 CG1 VAL A 36 1807 1723 1405 -27 12 -18 C
ATOM 95 CG2 VAL A 36 -1.910 -28.531 37.769 1.00 12.97 C
ANISOU 95 CG2 VAL A 36 1807 1719 1404 -28 10 -22 C
ATOM 96 N VAL A 37 -4.095 -29.393 40.451 1.00 8.58 N
ANISOU 96 N VAL A 37 1244 1171 844 -28 9 -25 N
ATOM 97 CA VAL A 37 -5.302 -30.196 40.295 1.00 5.24 C
ANISOU 97 CA VAL A 37 823 749 421 -29 9 -26 C
ATOM 98 C VAL A 37 -5.867 -29.898 38.915 1.00 4.83 C
ANISOU 98 C VAL A 37 773 692 370 -30 8 -27 C
ATOM 99 O VAL A 37 -6.309 -28.781 38.639 1.00 6.58 O
ANISOU 99 O VAL A 37 994 914 592 -29 6 -29 O
ATOM 100 CB VAL A 37 -6.326 -29.894 41.392 1.00 7.94 C
ANISOU 100 CB VAL A 37 1161 1094 762 -28 7 -28 C
ATOM 101 CG1 VAL A 37 -7.555 -30.770 41.220 1.00 12.34 C
ANISOU 101 CG1 VAL A 37 1719 1651 1318 -29 7 -28 C
ATOM 102 CG2 VAL A 37 -5.703 -30.092 42.762 1.00 8.84 C
ANISOU 102 CG2 VAL A 37 1272 1212 874 -27 8 -26 C
ATOM 103 N ASP A 38 -5.847 -30.899 38.049 1.00 6.25 N
ANISOU 103 N ASP A 38 957 869 551 -31 9 -26 N
ATOM 104 CA ASP A 38 -6.173 -30.689 36.649 1.00 6.19 C
ANISOU 104 CA ASP A 38 952 856 544 -32 9 -26 C
ATOM 105 C ASP A 38 -7.645 -30.320 36.488 1.00 8.03 C
ANISOU 105 C ASP A 38 1185 1090 777 -32 7 -29 C
ATOM 106 O ASP A 38 -8.531 -31.025 36.980 1.00 10.28 O
ANISOU 106 O ASP A 38 1468 1376 1060 -33 7 -30 O
ATOM 107 CB ASP A 38 -5.832 -31.949 35.862 1.00 4.12 C
ANISOU 107 CB ASP A 38 693 589 282 -33 11 -24 C
ATOM 108 CG ASP A 38 -5.532 -31.660 34.423 1.00 8.71 C
ANISOU 108 CG ASP A 38 1279 1166 865 -33 11 -24 C
ATOM 109 OD1 ASP A 38 -6.277 -30.860 33.828 1.00 13.01 O
ANISOU 109 OD1 ASP A 38 1823 1709 1410 -34 9 -26 O
ATOM 110 OD2 ASP A 38 -4.550 -32.222 33.893 1.00 9.75 O
ANISOU 110 OD2 ASP A 38 1413 1295 997 -34 12 -22 O
ATOM 111 N GLN A 39 -7.893 -29.192 35.816 1.00 9.42 N
ANISOU 111 N GLN A 39 1361 1264 953 -32 5 -31 N
ATOM 112 CA GLN A 39 -9.224 -28.671 35.510 1.00 7.92 C
ANISOU 112 CA GLN A 39 1171 1075 764 -32 3 -33 C
ATOM 113 C GLN A 39 -9.962 -28.154 36.741 1.00 6.64 C
ANISOU 113 C GLN A 39 1004 918 600 -31 2 -35 C
ATOM 114 O GLN A 39 -11.194 -28.055 36.730 1.00 7.48 O
ANISOU 114 O GLN A 39 1110 1025 706 -31 0 -37 O
ATOM 115 CB GLN A 39 -10.088 -29.717 34.788 1.00 10.09 C
ANISOU 115 CB GLN A 39 1448 1347 1038 -34 4 -33 C
ATOM 116 CG GLN A 39 -11.139 -29.125 33.868 1.00 9.62 C
ANISOU 116 CG GLN A 39 1389 1285 979 -34 2 -36 C
ATOM 117 CD GLN A 39 -12.132 -30.156 33.364 1.00 11.02 C
ANISOU 117 CD GLN A 39 1569 1460 1156 -36 2 -36 C
ATOM 118 OE1 GLN A 39 -13.272 -30.209 33.825 1.00 8.95 O
ANISOU 118 OE1 GLN A 39 1306 1201 894 -36 1 -37 O
ATOM 119 NE2 GLN A 39 -11.705 -30.975 32.409 1.00 12.02 N
ANISOU 119 NE2 GLN A 39 1701 1583 1285 -37 4 -34 N
ATOM 120 N MET A 40 -9.253 -27.796 37.807 1.00 7.40 N
ANISOU 120 N MET A 40 1098 1018 696 -30 2 -35 N
ATOM 121 CA MET A 40 -9.925 -27.332 39.018 1.00 7.31 C
ANISOU 121 CA MET A 40 1082 1011 683 -29 1 -37 C
ATOM 122 C MET A 40 -10.281 -25.859 38.872 1.00 6.14 C
ANISOU 122 C MET A 40 933 863 535 -28 -2 -39 C
ATOM 123 O MET A 40 -9.419 -24.986 38.971 1.00 3.02 O
ANISOU 123 O MET A 40 537 469 141 -27 -2 -39 O
ATOM 124 CB MET A 40 -9.058 -27.556 40.248 1.00 6.48 C
ANISOU 124 CB MET A 40 976 909 578 -28 2 -35 C
ATOM 125 CG MET A 40 -9.758 -27.125 41.513 1.00 3.04 C
ANISOU 125 CG MET A 40 536 478 141 -27 0 -37 C
ATOM 126 SD MET A 40 -8.840 -27.530 43.001 1.00 8.29 S
ANISOU 126 SD MET A 40 1198 1146 804 -25 2 -35 S
ATOM 127 CE MET A 40 -9.987 -26.944 44.240 1.00 11.45 C
ANISOU 127 CE MET A 40 1595 1550 1204 -24 0 -37 C
ATOM 128 N ARG A 41 -11.559 -25.586 38.620 1.00 8.50 N
ANISOU 128 N ARG A 41 1232 1163 835 -28 -3 -41 N
ATOM 129 CA ARG A 41 -12.080 -24.233 38.734 1.00 8.75 C
ANISOU 129 CA ARG A 41 1262 1196 867 -27 -5 -44 C
ATOM 130 C ARG A 41 -11.906 -23.734 40.162 1.00 6.63 C
ANISOU 130 C ARG A 41 990 933 598 -25 -6 -44 C
ATOM 131 O ARG A 41 -11.983 -24.504 41.121 1.00 7.06 O
ANISOU 131 O ARG A 41 1043 989 651 -25 -5 -44 O