HEADER HYDROLASE 02-NOV-17 6EVL
TITLE CRYSTAL STRUCTURE OF AN UNLIGNADED PEPTIDE-SUBSTRATE-BINDING DOMAIN OF
TITLE 2 HUMAN TYPE II COLLAGEN PROLYL 4-HYDROXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 4-PH ALPHA-2,PROCOLLAGEN-PROLINE,2-OXOGLUTARATE-4-
COMPND 5 DIOXYGENASE SUBUNIT ALPHA-2;
COMPND 6 EC: 1.14.11.2;
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: P4HA2, UNQ290/PRO330;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22B(+)
KEYWDS TETRATRICOPEPTIDE REPEAT, COLLAGEN SYNTHESIS, PROLYL 4-HYDROXYLASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.V.MURTHY,R.SULU,M.K.KOSKI,R.K.WIERENGA
REVDAT 3 17-JAN-24 6EVL 1 REMARK
REVDAT 2 31-OCT-18 6EVL 1 JRNL
REVDAT 1 12-SEP-18 6EVL 0
JRNL AUTH A.V.MURTHY,R.SULU,M.K.KOSKI,H.TU,J.ANANTHARAJAN,
JRNL AUTH 2 S.K.SAH-TELI,J.MYLLYHARJU,R.K.WIERENGA
JRNL TITL STRUCTURAL ENZYMOLOGY BINDING STUDIES OF THE
JRNL TITL 2 PEPTIDE-SUBSTRATE-BINDING DOMAIN OF HUMAN COLLAGEN PROLYL
JRNL TITL 3 4-HYDROXYLASE (TYPE-II): HIGH AFFINITY PEPTIDES HAVE A PXGP
JRNL TITL 4 SEQUENCE MOTIF.
JRNL REF PROTEIN SCI. V. 27 1692 2018
JRNL REFN ESSN 1469-896X
JRNL PMID 30168208
JRNL DOI 10.1002/PRO.3450
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
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) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 10951
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.180
REMARK 3 FREE R VALUE TEST SET COUNT : 2071
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 48.0361 - 4.6106 0.98 1198 148 0.1627 0.1723
REMARK 3 2 4.6106 - 3.6600 1.00 1206 142 0.1198 0.1536
REMARK 3 3 3.6600 - 3.1975 1.00 1237 138 0.1480 0.1991
REMARK 3 4 3.1975 - 2.9052 1.00 1210 140 0.1505 0.2443
REMARK 3 5 2.9052 - 2.6969 1.00 1245 126 0.1584 0.1980
REMARK 3 6 2.6969 - 2.5379 1.00 1204 142 0.1663 0.2259
REMARK 3 7 2.5379 - 2.4109 1.00 1213 130 0.1661 0.2130
REMARK 3 8 2.4109 - 2.3059 1.00 1235 135 0.1647 0.2210
REMARK 3 9 2.3059 - 2.2171 1.00 1216 138 0.1898 0.2364
REMARK 3 10 2.2171 - 2.1406 1.00 1228 148 0.2087 0.2771
REMARK 3 11 2.1406 - 2.0737 1.00 1240 140 0.2168 0.2655
REMARK 3 12 2.0737 - 2.0144 1.00 1189 136 0.2495 0.2403
REMARK 3 13 2.0144 - 1.9614 1.00 1236 137 0.2722 0.2660
REMARK 3 14 1.9614 - 1.9135 1.00 1199 134 0.2833 0.3682
REMARK 3 15 1.9135 - 1.8700 0.97 1221 137 0.3314 0.3986
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 834
REMARK 3 ANGLE : 0.759 1131
REMARK 3 CHIRALITY : 0.042 119
REMARK 3 PLANARITY : 0.004 147
REMARK 3 DIHEDRAL : 7.554 663
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6EVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : HELIOS MX MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NONIUS KAPPA CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XPREP PROTEUM 2 PACKAGE
REMARK 200 DATA SCALING SOFTWARE : SADABS PROTEUM 2 PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10985
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.30
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.62900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 CODE 2V5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.45 M AMMONIUM SULPHATE, 10% DMSO,
REMARK 280 100 MM MOPS, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.80333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.90167
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.90167
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.80333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 515 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 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 HIS A 141
REMARK 465 HIS A 142
REMARK 465 HIS A 143
REMARK 465 GLU A 238
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 OE1 GLU A 171 O HOH A 401 2.01
REMARK 500 O HOH A 437 O HOH A 480 2.02
REMARK 500 OD2 ASP A 149 O HOH A 402 2.09
REMARK 500 O HOH A 488 O HOH A 503 2.10
REMARK 500 O HOH A 488 O HOH A 512 2.13
REMARK 500 O GLY A 304 O HOH A 403 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 483 O HOH A 499 3655 2.06
REMARK 500 O HOH A 478 O HOH A 514 3655 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 218 65.09 -154.38
REMARK 500 GLU A 236 61.26 -119.63
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLY A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLY A 304
DBREF 6EVL A 144 238 UNP O15460 P4HA2_HUMAN 163 257
SEQADV 6EVL MET A 137 UNP O15460 INITIATING METHIONINE
SEQADV 6EVL HIS A 138 UNP O15460 EXPRESSION TAG
SEQADV 6EVL HIS A 139 UNP O15460 EXPRESSION TAG
SEQADV 6EVL HIS A 140 UNP O15460 EXPRESSION TAG
SEQADV 6EVL HIS A 141 UNP O15460 EXPRESSION TAG
SEQADV 6EVL HIS A 142 UNP O15460 EXPRESSION TAG
SEQADV 6EVL HIS A 143 UNP O15460 EXPRESSION TAG
SEQRES 1 A 102 MET HIS HIS HIS HIS HIS HIS MET LEU SER VAL ASP ASP
SEQRES 2 A 102 CYS PHE GLY MET GLY ARG SER ALA TYR ASN GLU GLY ASP
SEQRES 3 A 102 TYR TYR HIS THR VAL LEU TRP MET GLU GLN VAL LEU LYS
SEQRES 4 A 102 GLN LEU ASP ALA GLY GLU GLU ALA THR THR THR LYS SER
SEQRES 5 A 102 GLN VAL LEU ASP TYR LEU SER TYR ALA VAL PHE GLN LEU
SEQRES 6 A 102 GLY ASP LEU HIS ARG ALA LEU GLU LEU THR ARG ARG LEU
SEQRES 7 A 102 LEU SER LEU ASP PRO SER HIS GLU ARG ALA GLY GLY ASN
SEQRES 8 A 102 LEU ARG TYR PHE GLU GLN LEU LEU GLU GLU GLU
HET SO4 A 301 5
HET DMS A 302 4
HET GLY A 303 5
HET GLY A 304 5
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM GLY GLYCINE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 DMS C2 H6 O S
FORMUL 4 GLY 2(C2 H5 N O2)
FORMUL 6 HOH *122(H2 O)
HELIX 1 AA1 SER A 146 GLU A 160 1 15
HELIX 2 AA2 ASP A 162 ALA A 179 1 18
HELIX 3 AA3 THR A 186 LEU A 201 1 16
HELIX 4 AA4 ASP A 203 ASP A 218 1 16
HELIX 5 AA5 HIS A 221 GLU A 236 1 16
SITE 1 AC1 4 ARG A 206 GLU A 209 ARG A 213 HOH A 410
SITE 1 AC2 3 TRP A 169 PRO A 219 HOH A 452
SITE 1 AC3 5 TYR A 158 ASP A 192 TYR A 193 LEU A 235
SITE 2 AC3 5 HOH A 465
SITE 1 AC4 4 TYR A 196 ASN A 227 HOH A 403 HOH A 429
CRYST1 55.449 55.449 71.705 90.00 90.00 120.00 P 32 2 1 6
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 0.018035 0.010412 0.000000 0.00000
SCALE2 0.000000 0.020825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013946 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
