HEADER OXIDOREDUCTASE 14-JUN-13 4BTA
TITLE CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N-
TITLE 2 TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4
TITLE 3 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: COLLAGEN BINDING DOMAIN, RESIDUES 18-261;
COMPND 5 SYNONYM: 4-PH ALPHA-1, PROCOLLAGEN-PROLINE\,2-OXOGLUTARATE-4-
COMPND 6 DIOXYGENASE SUBUNIT ALPHA-1, PROLYL-4 HYDROXYLASE TYPE I;
COMPND 7 EC: 1.14.11.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROLINE RICH PEPTIDE;
COMPND 11 CHAIN: C;
COMPND 12 SYNONYM: 9 RESIDUE PEPTIDE- PPGPPGPRPG;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET15B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS OXIDOREDUCTASE, TETRATRICOPEPTIDE REPEAT MOTIF, COILED-COIL, PROLINE
KEYWDS 2 RICH PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ANANTHARAJAN,M.K.KOSKI,M.PEKKALA,R.K.WIERENGA
REVDAT 6 20-DEC-23 4BTA 1 REMARK
REVDAT 5 17-JUL-19 4BTA 1 REMARK
REVDAT 4 25-DEC-13 4BTA 1 JRNL
REVDAT 3 20-NOV-13 4BTA 1 JRNL
REVDAT 2 16-OCT-13 4BTA 1 JRNL
REVDAT 1 09-OCT-13 4BTA 0
JRNL AUTH J.ANANTHARAJAN,M.K.KOSKI,P.KURSULA,R.HIETA,U.BERGMANN,
JRNL AUTH 2 J.MYLLYHARJU,R.K.WIERENGA
JRNL TITL THE STRUCTURAL MOTIFS FOR SUBSTRATE BINDING AND DIMERIZATION
JRNL TITL 2 OF THE ALPHA SUBUNIT OF COLLAGEN PROLYL 4-HYDROXYLASE
JRNL REF STRUCTURE V. 21 2107 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 24207127
JRNL DOI 10.1016/J.STR.2013.09.005
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 14988
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 748
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 33.8024 - 5.0401 0.99 2998 158 0.2366 0.2954
REMARK 3 2 5.0401 - 4.0026 1.00 2841 149 0.2047 0.2299
REMARK 3 3 4.0026 - 3.4972 1.00 2833 149 0.2150 0.2587
REMARK 3 4 3.4972 - 3.1777 0.99 2760 145 0.2490 0.3398
REMARK 3 5 3.1777 - 2.9501 1.00 2808 147 0.2493 0.3308
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 129.4
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: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 3760
REMARK 3 ANGLE : 1.798 5079
REMARK 3 CHIRALITY : 0.090 567
REMARK 3 PLANARITY : 0.011 650
REMARK 3 DIHEDRAL : 14.621 1416
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 3 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1582 -1.8464 -16.9978
REMARK 3 T TENSOR
REMARK 3 T11: 0.7160 T22: 0.8097
REMARK 3 T33: 1.0777 T12: -0.1564
REMARK 3 T13: 0.2576 T23: -0.1150
REMARK 3 L TENSOR
REMARK 3 L11: 7.9643 L22: 6.1630
REMARK 3 L33: 0.7622 L12: 6.5912
REMARK 3 L13: 2.2104 L23: 1.0309
REMARK 3 S TENSOR
REMARK 3 S11: 0.8295 S12: 0.0711 S13: 0.1636
REMARK 3 S21: 2.1086 S22: -0.4776 S23: 1.5626
REMARK 3 S31: 0.2797 S32: 0.0832 S33: -0.2311
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 54 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3065 -23.4207 -21.5531
REMARK 3 T TENSOR
REMARK 3 T11: 0.7857 T22: 0.9067
REMARK 3 T33: 2.1375 T12: -0.0893
REMARK 3 T13: 0.0389 T23: -0.2049
REMARK 3 L TENSOR
REMARK 3 L11: 5.0707 L22: 1.5090
REMARK 3 L33: 5.3503 L12: 2.2004
REMARK 3 L13: 0.1894 L23: -1.6981
REMARK 3 S TENSOR
REMARK 3 S11: 0.4829 S12: 0.6814 S13: -0.9924
REMARK 3 S21: 0.1770 S22: 0.3132 S23: -0.2389
REMARK 3 S31: 1.0574 S32: -0.8308 S33: -0.7087
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 91 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9412 19.0390 -25.3674
REMARK 3 T TENSOR
REMARK 3 T11: 0.6777 T22: 0.5191
REMARK 3 T33: 0.5964 T12: -0.1000
REMARK 3 T13: -0.0729 T23: -0.1947
REMARK 3 L TENSOR
REMARK 3 L11: 6.4972 L22: 9.1536
REMARK 3 L33: 4.7190 L12: 2.2315
REMARK 3 L13: -4.7148 L23: -4.9442
REMARK 3 S TENSOR
REMARK 3 S11: 0.2171 S12: -0.4545 S13: 0.1403
REMARK 3 S21: 0.1899 S22: -0.4759 S23: 0.1434
REMARK 3 S31: -0.2560 S32: -0.0104 S33: 0.2431
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 147 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.7507 18.2754 -39.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.6596 T22: 0.6626
REMARK 3 T33: 0.4125 T12: 0.0179
REMARK 3 T13: -0.0124 T23: -0.1294
REMARK 3 L TENSOR
REMARK 3 L11: 4.6022 L22: 5.3151
REMARK 3 L33: 4.8303 L12: -0.9775
REMARK 3 L13: 1.7282 L23: -2.3251
REMARK 3 S TENSOR
REMARK 3 S11: -0.1944 S12: 0.6039 S13: -0.5751
REMARK 3 S21: 0.5212 S22: 0.1337 S23: -0.5087
REMARK 3 S31: 0.4322 S32: -0.4331 S33: -0.0100
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 187 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3395 21.4955 -55.9871
REMARK 3 T TENSOR
REMARK 3 T11: 1.2223 T22: 0.9905
REMARK 3 T33: 0.5656 T12: -0.0575
REMARK 3 T13: -0.0874 T23: -0.1121
REMARK 3 L TENSOR
REMARK 3 L11: 4.4584 L22: 5.0122
REMARK 3 L33: 3.3613 L12: -0.8718
REMARK 3 L13: 2.3498 L23: -3.8608
REMARK 3 S TENSOR
REMARK 3 S11: -0.1435 S12: 0.9277 S13: -0.3139
REMARK 3 S21: -1.6276 S22: 0.1491 S23: 0.1255
REMARK 3 S31: 0.2707 S32: 0.0025 S33: -0.0370
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESID 7 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7699 -7.4768 -24.8413
REMARK 3 T TENSOR
REMARK 3 T11: 0.6727 T22: 0.8169
REMARK 3 T33: 1.3295 T12: 0.0161
REMARK 3 T13: 0.1221 T23: -0.3205
REMARK 3 L TENSOR
REMARK 3 L11: 5.2051 L22: 4.9443
REMARK 3 L33: 2.0095 L12: 2.2105
REMARK 3 L13: 1.1607 L23: 0.5734
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: 1.3086 S13: -1.0133
REMARK 3 S21: 0.0351 S22: 0.3678 S23: 0.5667
REMARK 3 S31: 0.3698 S32: 0.3800 S33: -0.4220
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESID 62 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1346 -7.0082 -23.7452
REMARK 3 T TENSOR
REMARK 3 T11: 0.5816 T22: 0.8107
REMARK 3 T33: 1.9062 T12: -0.0348
REMARK 3 T13: 0.1577 T23: -0.2422
REMARK 3 L TENSOR
REMARK 3 L11: 4.4903 L22: 6.2156
REMARK 3 L33: 0.9270 L12: 5.3313
REMARK 3 L13: 1.1470 L23: -1.6091
REMARK 3 S TENSOR
REMARK 3 S11: 0.1071 S12: 0.9933 S13: -0.7697
REMARK 3 S21: -0.5268 S22: 0.6478 S23: 0.8269
REMARK 3 S31: -0.0165 S32: -0.2940 S33: -0.4767
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESID 124 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4642 -34.3275 -7.7291
REMARK 3 T TENSOR
REMARK 3 T11: 1.5164 T22: 1.4515
REMARK 3 T33: 2.3985 T12: 0.1517
REMARK 3 T13: -0.7388 T23: 0.4584
REMARK 3 L TENSOR
REMARK 3 L11: 4.1687 L22: 7.5365
REMARK 3 L33: 6.7314 L12: -1.9570
REMARK 3 L13: -4.7378 L23: 4.7994
REMARK 3 S TENSOR
REMARK 3 S11: -0.3707 S12: -1.3111 S13: 0.5802
REMARK 3 S21: 1.3010 S22: 1.3050 S23: 0.1154
REMARK 3 S31: 1.8858 S32: 0.7881 S33: -1.0372
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESID 163 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5652 -32.6509 -1.9448
REMARK 3 T TENSOR
REMARK 3 T11: 1.2356 T22: 1.9644
REMARK 3 T33: 1.8785 T12: 0.0649
REMARK 3 T13: -0.1245 T23: 0.4489
REMARK 3 L TENSOR
REMARK 3 L11: 4.2435 L22: 3.1399
REMARK 3 L33: 7.9387 L12: 3.0746
REMARK 3 L13: -2.5477 L23: 0.5346
REMARK 3 S TENSOR
REMARK 3 S11: 0.9979 S12: -2.0726 S13: -0.7259
REMARK 3 S21: 0.8605 S22: -0.5695 S23: 0.7765
REMARK 3 S31: 1.1310 S32: 1.8023 S33: -0.6585
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESID 187 THROUGH 204 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9124 -28.5213 5.6070
REMARK 3 T TENSOR
REMARK 3 T11: 1.2483 T22: 2.1520
REMARK 3 T33: 2.3370 T12: 0.0745
REMARK 3 T13: -0.1869 T23: 0.6615
REMARK 3 L TENSOR
REMARK 3 L11: 4.0579 L22: 4.9401
REMARK 3 L33: 7.4026 L12: -4.1470
REMARK 3 L13: -4.8256 L23: 3.8094
REMARK 3 S TENSOR
REMARK 3 S11: 1.2051 S12: -0.0206 S13: 1.2686
REMARK 3 S21: -1.9740 S22: 0.6470 S23: -1.8663
REMARK 3 S31: -0.1000 S32: -0.9594 S33: -1.5805
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESID 205 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9043 -30.6310 12.7661
REMARK 3 T TENSOR
REMARK 3 T11: 1.9353 T22: 2.7492
REMARK 3 T33: 1.9292 T12: -0.3198
REMARK 3 T13: -0.2538 T23: 0.1626
REMARK 3 L TENSOR
REMARK 3 L11: 9.5288 L22: 5.6670
REMARK 3 L33: 2.7181 L12: -7.0253
REMARK 3 L13: -1.4618 L23: 2.1819
REMARK 3 S TENSOR
REMARK 3 S11: -0.8123 S12: -0.6997 S13: -1.7382
REMARK 3 S21: 0.0088 S22: 1.7636 S23: 2.7344
REMARK 3 S31: 2.4437 S32: -1.3361 S33: -0.7760
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESID 218 THROUGH 234 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9408 -23.5108 15.7205
REMARK 3 T TENSOR
REMARK 3 T11: 1.9579 T22: 2.1569
REMARK 3 T33: 1.7065 T12: -0.4045
REMARK 3 T13: -0.5604 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 8.4960 L22: 9.5096
REMARK 3 L33: 1.6599 L12: 5.1088
REMARK 3 L13: -0.9239 L23: -0.0782
REMARK 3 S TENSOR
REMARK 3 S11: 1.0340 S12: -1.9032 S13: 1.3719
REMARK 3 S21: 0.3662 S22: -1.6277 S23: -0.6082
REMARK 3 S31: -0.3982 S32: 0.0897 S33: 0.1457
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5055 26.8730 -54.9199
REMARK 3 T TENSOR
REMARK 3 T11: 1.4103 T22: 2.2338
REMARK 3 T33: 0.9165 T12: 0.1324
REMARK 3 T13: -0.0533 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.4946 L22: 5.8912
REMARK 3 L33: 0.0530 L12: 2.8115
REMARK 3 L13: 0.1998 L23: 0.5502
REMARK 3 S TENSOR
REMARK 3 S11: 0.4429 S12: 0.8134 S13: 1.0675
REMARK 3 S21: -1.6137 S22: 1.1874 S23: 2.0401
REMARK 3 S31: 0.1861 S32: 0.7685 S33: -1.1980
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 4BTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1290057177.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14997
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 33.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.010
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.330
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: PDB ENTRY 2YQ8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEGMME5000, 10% DMSO, 10% MPD, 0.1
REMARK 280 M MES, PH 6.0, 5MM (PRO-PRO-GLY)3
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 117.33000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.92500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 117.33000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.92500
REMARK 290 SMTRY3 4 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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 240
REMARK 465 VAL A 241
REMARK 465 ASN A 242
REMARK 465 LYS A 243
REMARK 465 SER A 244
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 PHE B 4
REMARK 465 PHE B 5
REMARK 465 THR B 6
REMARK 465 GLY B 134
REMARK 465 ASN B 135
REMARK 465 LEU B 136
REMARK 465 PRO B 137
REMARK 465 GLY B 138
REMARK 465 VAL B 139
REMARK 465 LYS B 140
REMARK 465 HIS B 141
REMARK 465 LYS B 142
REMARK 465 SER B 143
REMARK 465 PHE B 144
REMARK 465 LEU B 145
REMARK 465 THR B 146
REMARK 465 GLN B 200
REMARK 465 GLN B 201
REMARK 465 GLY B 202
REMARK 465 ASP B 203
REMARK 465 MET B 235
REMARK 465 ALA B 236
REMARK 465 LYS B 237
REMARK 465 GLU B 238
REMARK 465 LYS B 239
REMARK 465 ASP B 240
REMARK 465 VAL B 241
REMARK 465 ASN B 242
REMARK 465 LYS B 243
REMARK 465 SER B 244
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 NH2 ARG A 101 OE1 GLU B 82 1.98
REMARK 500 O PHE A 60 ND2 ASN A 66 2.08
REMARK 500 OE1 GLU A 82 NH2 ARG B 101 2.13
REMARK 500 NZ LYS A 69 OD2 ASP B 149 2.19
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 LEU A 120 CA - CB - CG ANGL. DEV. = 17.9 DEGREES
REMARK 500 LEU A 120 CB - CG - CD2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 PRO B 219 C - N - CA ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO B 219 C - N - CD ANGL. DEV. = -12.7 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 ASP A 56 70.87 -157.20
REMARK 500 THR A 76 -53.51 -121.71
REMARK 500 ASN A 106 -166.67 -115.08
REMARK 500 ASN A 135 47.49 -79.62
REMARK 500 GLU A 238 30.07 -88.08
REMARK 500 ASP B 56 86.12 -155.49
REMARK 500 ASN B 106 -165.59 -122.24
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 PRO A 137 GLY A 138 -137.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BT8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE APO FORM OF N-TERMINAL DOMAIN AND PEPTIDE
REMARK 900 SUBSTRATE BINDING DOMAIN OF PROLYL- 4 HYDROXYLASE TYPE I FROM HUMAN
REMARK 900 RELATED ID: 4BT9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N-
REMARK 900 TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4
REMARK 900 HYDROXYLASE (RESIDUES 1-238 ) TYPE I FROM HUMAN
REMARK 900 RELATED ID: 4BTB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTIDE(PRO)9 BOUND COMPLEX OF N-TERMINAL
REMARK 900 DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE
REMARK 900 (RESIDUES 1-238) TYPE I FROM HUMAN
DBREF 4BTA A 1 244 UNP P13674 P4HA1_HUMAN 18 261
DBREF 4BTA B 1 244 UNP P13674 P4HA1_HUMAN 18 261
DBREF 4BTA C 1 9 PDB 4BTA 4BTA 1 9
SEQADV 4BTA MET A -6 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS A -5 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS A -4 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS A -3 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS A -2 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS A -1 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS A 0 UNP P13674 EXPRESSION TAG
SEQADV 4BTA MET B -6 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS B -5 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS B -4 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS B -3 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS B -2 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS B -1 UNP P13674 EXPRESSION TAG
SEQADV 4BTA HIS B 0 UNP P13674 EXPRESSION TAG
SEQRES 1 A 251 MET HIS HIS HIS HIS HIS HIS HIS PRO GLY PHE PHE THR
SEQRES 2 A 251 SER ILE GLY GLN MET THR ASP LEU ILE HIS THR GLU LYS
SEQRES 3 A 251 ASP LEU VAL THR SER LEU LYS ASP TYR ILE LYS ALA GLU
SEQRES 4 A 251 GLU ASP LYS LEU GLU GLN ILE LYS LYS TRP ALA GLU LYS
SEQRES 5 A 251 LEU ASP ARG LEU THR SER THR ALA THR LYS ASP PRO GLU
SEQRES 6 A 251 GLY PHE VAL GLY HIS PRO VAL ASN ALA PHE LYS LEU MET
SEQRES 7 A 251 LYS ARG LEU ASN THR GLU TRP SER GLU LEU GLU ASN LEU
SEQRES 8 A 251 VAL LEU LYS ASP MET SER ASP GLY PHE ILE SER ASN LEU
SEQRES 9 A 251 THR ILE GLN ARG GLN TYR PHE PRO ASN ASP GLU ASP GLN
SEQRES 10 A 251 VAL GLY ALA ALA LYS ALA LEU LEU ARG LEU GLN ASP THR
SEQRES 11 A 251 TYR ASN LEU ASP THR ASP THR ILE SER LYS GLY ASN LEU
SEQRES 12 A 251 PRO GLY VAL LYS HIS LYS SER PHE LEU THR ALA GLU ASP
SEQRES 13 A 251 CYS PHE GLU LEU GLY LYS VAL ALA TYR THR GLU ALA ASP
SEQRES 14 A 251 TYR TYR HIS THR GLU LEU TRP MET GLU GLN ALA LEU ARG
SEQRES 15 A 251 GLN LEU ASP GLU GLY GLU ILE SER THR ILE ASP LYS VAL
SEQRES 16 A 251 SER VAL LEU ASP TYR LEU SER TYR ALA VAL TYR GLN GLN
SEQRES 17 A 251 GLY ASP LEU ASP LYS ALA LEU LEU LEU THR LYS LYS LEU
SEQRES 18 A 251 LEU GLU LEU ASP PRO GLU HIS GLN ARG ALA ASN GLY ASN
SEQRES 19 A 251 LEU LYS TYR PHE GLU TYR ILE MET ALA LYS GLU LYS ASP
SEQRES 20 A 251 VAL ASN LYS SER
SEQRES 1 B 251 MET HIS HIS HIS HIS HIS HIS HIS PRO GLY PHE PHE THR
SEQRES 2 B 251 SER ILE GLY GLN MET THR ASP LEU ILE HIS THR GLU LYS
SEQRES 3 B 251 ASP LEU VAL THR SER LEU LYS ASP TYR ILE LYS ALA GLU
SEQRES 4 B 251 GLU ASP LYS LEU GLU GLN ILE LYS LYS TRP ALA GLU LYS
SEQRES 5 B 251 LEU ASP ARG LEU THR SER THR ALA THR LYS ASP PRO GLU
SEQRES 6 B 251 GLY PHE VAL GLY HIS PRO VAL ASN ALA PHE LYS LEU MET
SEQRES 7 B 251 LYS ARG LEU ASN THR GLU TRP SER GLU LEU GLU ASN LEU
SEQRES 8 B 251 VAL LEU LYS ASP MET SER ASP GLY PHE ILE SER ASN LEU
SEQRES 9 B 251 THR ILE GLN ARG GLN TYR PHE PRO ASN ASP GLU ASP GLN
SEQRES 10 B 251 VAL GLY ALA ALA LYS ALA LEU LEU ARG LEU GLN ASP THR
SEQRES 11 B 251 TYR ASN LEU ASP THR ASP THR ILE SER LYS GLY ASN LEU
SEQRES 12 B 251 PRO GLY VAL LYS HIS LYS SER PHE LEU THR ALA GLU ASP
SEQRES 13 B 251 CYS PHE GLU LEU GLY LYS VAL ALA TYR THR GLU ALA ASP
SEQRES 14 B 251 TYR TYR HIS THR GLU LEU TRP MET GLU GLN ALA LEU ARG
SEQRES 15 B 251 GLN LEU ASP GLU GLY GLU ILE SER THR ILE ASP LYS VAL
SEQRES 16 B 251 SER VAL LEU ASP TYR LEU SER TYR ALA VAL TYR GLN GLN
SEQRES 17 B 251 GLY ASP LEU ASP LYS ALA LEU LEU LEU THR LYS LYS LEU
SEQRES 18 B 251 LEU GLU LEU ASP PRO GLU HIS GLN ARG ALA ASN GLY ASN
SEQRES 19 B 251 LEU LYS TYR PHE GLU TYR ILE MET ALA LYS GLU LYS ASP
SEQRES 20 B 251 VAL ASN LYS SER
SEQRES 1 C 9 PRO PRO GLY PRO PRO GLY PRO PRO GLY
HELIX 1 1 GLY A 3 LYS A 55 1 53
HELIX 2 2 ASP A 56 HIS A 63 1 8
HELIX 3 3 HIS A 63 THR A 76 1 14
HELIX 4 4 THR A 76 LYS A 87 1 12
HELIX 5 5 SER A 90 ARG A 101 1 12
HELIX 6 6 GLN A 102 PHE A 104 5 3
HELIX 7 7 ASN A 106 ASN A 125 1 20
HELIX 8 8 ASP A 127 LYS A 133 1 7
HELIX 9 9 THR A 146 GLU A 160 1 15
HELIX 10 10 ASP A 162 GLU A 179 1 18
HELIX 11 11 ASP A 186 GLN A 201 1 16
HELIX 12 12 ASP A 203 ASP A 218 1 16
HELIX 13 13 HIS A 221 GLU A 238 1 18
HELIX 14 14 ILE B 8 ASP B 56 1 49
HELIX 15 15 ASP B 56 HIS B 63 1 8
HELIX 16 16 HIS B 63 THR B 76 1 14
HELIX 17 17 THR B 76 LYS B 87 1 12
HELIX 18 18 SER B 90 ARG B 101 1 12
HELIX 19 19 GLN B 102 PHE B 104 5 3
HELIX 20 20 ASN B 106 TYR B 124 1 19
HELIX 21 21 ASP B 127 LYS B 133 1 7
HELIX 22 22 ALA B 147 GLU B 160 1 14
HELIX 23 23 ASP B 162 GLU B 179 1 18
HELIX 24 24 ASP B 186 TYR B 199 1 14
HELIX 25 25 LEU B 204 ASP B 218 1 15
HELIX 26 26 HIS B 221 ILE B 234 1 14
CISPEP 1 LYS A 140 HIS A 141 0 24.11
CISPEP 2 PRO C 8 GLY C 9 0 -7.26
CRYST1 234.660 47.850 60.290 90.00 90.00 90.00 P 21 21 2 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 0.004261 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016586 0.00000
(ATOM LINES ARE NOT SHOWN.)
END